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Wu P, Su Y, Feng L, Jiang W, Kuang S, Tang L, Jiang J, Liu Y, Zhou X. Optimal DL-Methionyl-DL-Methionine Supplementation Improved Intestinal Physical Barrier Function by Changing Antioxidant Capacity, Apoptosis and Tight Junction Proteins in the Intestine of Juvenile Grass Carp (Ctenopharyngodon idella). Antioxidants (Basel) 2022; 11:antiox11091652. [PMID: 36139725 PMCID: PMC9495950 DOI: 10.3390/antiox11091652] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 06/25/2022] [Revised: 08/16/2022] [Accepted: 08/19/2022] [Indexed: 11/16/2022] Open
Abstract
The present study was a part of a larger research project that aimed to investigate the effects of Met-Met supplementation on fish growth and intestinal health. This study mainly focused on the relationship between dietary Met-Met and intestinal physical barrier function in fish. Seven iso-nitrogenous diets supplemented with 2.50 g/kg DL-methionine (DL-Met) and six graded levels of Met-Met (0.00, 0.79, 1.44, 1.84, 2.22, and 2.85 g/kg) were used to feed juvenile grass carp for 10 weeks, after which a 14-day Aeromonas hydrophila challenge test was performed. The results indicated that optimum levels of Met-Met decreased intestinal oxidative damage, probably by increasing total antioxidant capacity, and the activity and gene expression levels of several antioxidant enzymes, which were closely related to the changed Nrf2/Keap1 signaling. Meanwhile, optimum levels of Met-Met decreased intestinal apoptosis and improved the intestinal tight junction, as evident by the downregulated mRNA levels of initiator and executioner caspases; the pro-apoptotic-related proteins FasL, Apaf-1, and Bax; and upregulated mRNA levels of the anti-apoptotic proteins Bcl-2, Mcl-1b, and IAP and the TJ proteins claudins, occludin, and ZOs. Furthermore, the positive effects of Met-Met on improving intestinal physical barrier function were superior to those of DL-Met in fish. These findings showed that optimal Met-Met supplementation improved intestinal physical barrier function, probably by changing antioxidant capacity, apoptosis, and tight junction proteins in fish.
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Affiliation(s)
- Pei Wu
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
- Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, China
- Key Laboratory of Animal Disease-Resistance Nutrition, Ministry of Education, Ministry of Agriculture and Rural Affairs, Key Laboratory of Sichuan Province, Chengdu 611130, China
| | - Yuening Su
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
| | - Lin Feng
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
- Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, China
- Key Laboratory of Animal Disease-Resistance Nutrition, Ministry of Education, Ministry of Agriculture and Rural Affairs, Key Laboratory of Sichuan Province, Chengdu 611130, China
| | - Weidan Jiang
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
- Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, China
- Key Laboratory of Animal Disease-Resistance Nutrition, Ministry of Education, Ministry of Agriculture and Rural Affairs, Key Laboratory of Sichuan Province, Chengdu 611130, China
| | - Shengyao Kuang
- Animal Nutrition Institute, Sichuan Academy of Animal Science, Sichuan Animtech Feed Co., Ltd., Chengdu 610066, China
| | - Ling Tang
- Animal Nutrition Institute, Sichuan Academy of Animal Science, Sichuan Animtech Feed Co., Ltd., Chengdu 610066, China
| | - Jun Jiang
- College of Animal Science and Technology, Sichuan Agricultural University, Chengdu 611130, China
| | - Yang Liu
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
- Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, China
- Key Laboratory of Animal Disease-Resistance Nutrition, Ministry of Education, Ministry of Agriculture and Rural Affairs, Key Laboratory of Sichuan Province, Chengdu 611130, China
- Correspondence: (Y.L.); (X.Z.)
| | - Xiaoqiu Zhou
- Animal Nutrition Institute, Sichuan Agricultural University, Chengdu 611130, China
- Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu 611130, China
- Key Laboratory of Animal Disease-Resistance Nutrition, Ministry of Education, Ministry of Agriculture and Rural Affairs, Key Laboratory of Sichuan Province, Chengdu 611130, China
- Correspondence: (Y.L.); (X.Z.)
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Effects of Different Methionine Sources on Methionine Metabolism in the IPEC-J2 Cells. BIOMED RESEARCH INTERNATIONAL 2019; 2019:5464906. [PMID: 31380429 PMCID: PMC6662248 DOI: 10.1155/2019/5464906] [Citation(s) in RCA: 6] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Received: 04/16/2019] [Accepted: 06/11/2019] [Indexed: 01/01/2023]
Abstract
As one of the essential amino acids, methionine (Met) plays an important role in biological events such as methylation and antioxidant properties besides its function in protein synthesis. Different Met sources have been used in animal production, but their effects on Met metabolic pathways are not well understood. In the present study, we investigated the effects of different Met sources (L-Met, DL-Met, DL-2-hydroxy-4-(methylthio)butanoic acid (DL-HMTBA), and DL-methionyl-DL-methionine (DL-MM)) on the metabolism of Met in small intestinal porcine epithelial cell line (IPEC-J2) and the contents of extracellular Met sources. The results showed that concentrations of intracellular Met, S-adenosylmethionine (SAM), S-adenosylhomocysteine (SAH), and the ratio of SAM to SAH in the DL-HMTBA group were significantly lower than that in other Met source groups, while the content of 5-methyltetrahydrofolate (5-MTHF) was significantly higher. Moreover, the mRNA levels of MAT2A, AHcy, CBS, MTHFR, and MTR in the DL-HMTBA group were significantly higher than those in other Met source groups. Further study showed that the total content of extracellular Met sources was highest in the DL-HMTBA group, followed by DL-MM group, followed by L-Met and DL-Met groups. These results demonstrated that DL-HMTBA mainly affects the transmethylation and remethylation of Met and it can promote the trans-sulfur metabolism of Met when compared with other Met sources. In addition, most DL-HMTBA and a small amount of DL-MM can escape the intestinal first-pass metabolism and then provide more extracellular Met sources than L-Met and DL-Met. Therefore, this study can provide a theoretical basis for the selection of Met sources in livestock.
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Orozco ZGA, Soma S, Kaneko T, Watanabe S. Spatial mRNA Expression and Response to Fasting and Refeeding of Neutral Amino Acid Transporters slc6a18 and slc6a19a in the Intestinal Epithelium of Mozambique tilapia. Front Physiol 2018; 9:212. [PMID: 29593569 PMCID: PMC5859172 DOI: 10.3389/fphys.2018.00212] [Citation(s) in RCA: 9] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/28/2017] [Accepted: 02/26/2018] [Indexed: 12/17/2022] Open
Abstract
The mRNA expressions of the epithelial neutral amino acid transporters slc6a18 and slc6a19a in the five segments (HL, PMC, GL, DMC, and TS) of the intestine of Mozambique tilapia, and their responses to fasting and refeeding were investigated for a better understanding of the functional and nutritional characteristics of slc6a18 and slc6a19a. Although both slc6a18 and slc6a19a were expressed mainly in the intestine, these genes showed opposing spatial distributions along the intestine. The slc6a18 was mainly expressed in the middle (GL) and posterior (DMC and TS) intestines, while slc6a19a was specifically expressed in the anterior intestine (HL and PMC). Large decreases of amino acid concentrations from the HL to GL imply that amino acids are mainly absorbed before reaching the GL, suggesting an important role of slc6a19a in the absorption. Moreover, substantial amounts of some neutral amino acids with the isoelectric point close to 6 remain in the GL. These are most likely the remaining unabsorbed amino acids or those from of amino acid antiporters which release neutral amino acids in exchange for uptake of its substrates. These amino acids were diminished in the TS, suggesting active absorption in the posterior intestine. This suggests that slc6a18 is essential to complete the absorption of neutral amino acids. At fasting, significant downregulation of slc6a19a expression was observed from the initial up to day 2 and became stable from day 4 to day 14 in the HL and PMC suggesting that slc6a19a expression reflects nutritional condition in the intestinal lumen. Refeeding stimulates slc6a19a expression, although expressions did not exceed the initial level within 3 days after refeeding. The slc6a18 expression was decreased during fasting in the GL but no significant change was observed in the DMC. Only a transient decrease was observed at day 2 in the TS. Refeeding did not stimulate slc6a18 expression. Results in this study suggest that Slc6a18 and Slc6a19 have different roles in the intestine, and that both of these contribute to establish the efficient neutral amino acid absorption system in the tilapia.
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Affiliation(s)
- Zenith Gaye A Orozco
- Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan
| | - Satoshi Soma
- Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan
| | - Toyoji Kaneko
- Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan
| | - Soichi Watanabe
- Department of Aquatic Bioscience, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan
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Su YN, Wu P, Feng L, Jiang WD, Jiang J, Zhang YA, Figueiredo-Silva C, Zhou XQ, Liu Y. The improved growth performance and enhanced immune function by DL-methionyl-DL-methionine are associated with NF-κB and TOR signalling in intestine of juvenile grass carp (Ctenopharyngodon idella). FISH & SHELLFISH IMMUNOLOGY 2018; 74:101-118. [PMID: 29292200 DOI: 10.1016/j.fsi.2017.12.051] [Citation(s) in RCA: 35] [Impact Index Per Article: 5.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Received: 07/25/2017] [Revised: 12/26/2017] [Accepted: 12/27/2017] [Indexed: 06/07/2023]
Abstract
The present study investigated the effects of dietary DL-methionyl-DL-methionine (Met-Met) on growth performance, intestinal immune function and the underlying signalling molecules in juvenile grass carp (Ctenopharyngodon idella). Fish were fed one DL-methionine (DL-Met) group (2.50 g/kg diet) and six graded levels of Met-Met groups (0, 0.79, 1.44, 1.84, 2.22 and 2.85 g/kg diet) for 10 weeks, and then challenged with Aeromonas hydrophila for 14 days. Results indicated that the optimal Met-Met supplementation: (1) increased fish growth performance, intestinal lysozyme (LZ) and acid phosphatase (ACP) activities, complement (C3 and C4) and immunoglobulin M (IgM) contents, up-regulated hepcidin, liver expressed antimicrobial peptide 2A (LEAP-2A), LEAP-2B, β-defensin-1 and Mucin2 mRNA levels; (2) down-regulated tumour necrosis factor α (TNF-α), interferon γ2 (IFN-γ2), interleukin 1β (IL-1β), IL-8 [only in the distal intestine (DI)], IL-12p35, IL-12p40 and IL-15 (not IL-17D) mRNA levels partially related to the down-regulation of IκB kinase β (IKKβ) and IKKγ (rather than IKKα), nuclear factor kappa B (NF-κB) p65 and c-Rel (rather than NF-κB p52) mRNA levels and the up-regulation of inhibitor of κBα (IκBα) mRNA levels; (3) up-regulated IL-4/13A, IL-4/13B, IL-6, IL-10, IL-11 and transforming growth factor (TGF)-β1 (not TGF-β2) mRNA levels partially associated with the target of rapamycin (TOR) signalling pathway [TOR/ribosomal protein S6 kinases 1 (S6K1), eIF4E-binding proteins (4E-BP)] in three intestinal segments of juvenile grass carp. These results suggest that Met-Met supplementation improves growth and intestinal immune function in fish. Furthermore, according to a positive effect, the optimal Met-Met supplementation was superior to the optimal DL-Met supplementation at improving the growth performance and enhancing the intestinal immune function in fish. Finally, based on percent weight gain (PWG), protection against enteritis morbidity and immune index (LZ activity), the optimal Met-Met supplementation for juvenile grass carp was estimated as 1.61, 1.64 and 1.68 g/kg diet, respectively, as the basal diet contains 8.03 g/kg total sulfur amino acids (TSAA) (4.26 g methionine/kg and 3.77 g cysteine/kg).
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Affiliation(s)
- Yue-Ning Su
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China
| | - Pei Wu
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Key Laboratory for Animal Disease-Resistance Nutrition of China Ministry of Education, Sichuan Agricultural University, Sichuan, Chengdu 611130, China
| | - Lin Feng
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Key Laboratory for Animal Disease-Resistance Nutrition of China Ministry of Education, Sichuan Agricultural University, Sichuan, Chengdu 611130, China
| | - Wei-Dan Jiang
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Key Laboratory for Animal Disease-Resistance Nutrition of China Ministry of Education, Sichuan Agricultural University, Sichuan, Chengdu 611130, China
| | - Jun Jiang
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China
| | - Yong-An Zhang
- Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China
| | - Claudia Figueiredo-Silva
- Evonik Nutrition & Care GmbH, NC, 10-B531, Postfach 1345, Rodenbacher Chausse 4, 63404 Hanau, Germany
| | - Xiao-Qiu Zhou
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Key Laboratory for Animal Disease-Resistance Nutrition of China Ministry of Education, Sichuan Agricultural University, Sichuan, Chengdu 611130, China.
| | - Yang Liu
- Animal Nutrition Institute, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Fish Nutrition and Safety Production University Key Laboratory of Sichuan Province, Sichuan Agricultural University, Sichuan, Chengdu 611130, China; Key Laboratory for Animal Disease-Resistance Nutrition of China Ministry of Education, Sichuan Agricultural University, Sichuan, Chengdu 611130, China.
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Boudry G, David ES, Douard V, Monteiro IM, Le Huërou-Luron I, Ferraris RP. Role of intestinal transporters in neonatal nutrition: carbohydrates, proteins, lipids, minerals, and vitamins. J Pediatr Gastroenterol Nutr 2010; 51:380-401. [PMID: 20808244 DOI: 10.1097/mpg.0b013e3181eb5ad6] [Citation(s) in RCA: 47] [Impact Index Per Article: 3.1] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Indexed: 01/19/2023]
Abstract
To support rapid growth and a high metabolic rate, infants require enormous amounts of nutrients. The small intestine must have the complete array of transporters that absorb the nutrients released from digested food. Failure of intestinal transporters to function properly often presents symptoms as "failure to thrive" because nutrients are not absorbed and as diarrhea because unabsorbed nutrients upset luminal osmolality or become substrates of intestinal bacteria. We enumerate the nutrients that constitute human milk and various infant milk formulas, explain their importance in neonatal nutrition, then describe for each nutrient the transporter(s) that absorbs it from the intestinal lumen into the enterocyte cytosol and from the cytosol to the portal blood. More than 100 membrane and cytosolic transporters are now thought to facilitate absorption of minerals and vitamins as well as products of digestion of the macronutrients carbohydrates, proteins, and lipids. We highlight research areas that should yield information needed to better understand the important role of these transporters during normal development.
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Affiliation(s)
- Gaëlle Boudry
- Institut National de Recherche Agronomique, UMR1079 Système d'Elevage, Nutrition, Animale et Humaine, St-Gilles, France
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Effects of Dietary Protein Levels on Amino Acid Digestibility at Different Sites of Male Adult Chicken Intestines. J Poult Sci 2010. [DOI: 10.2141/jpsa.009123] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/21/2022] Open
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Drozdowski LA, Clandinin MT, Thomson ABR. Morphological, kinetic, membrane biochemical and genetic aspects of intestinal enteroplasticity. World J Gastroenterol 2009; 15:774-87. [PMID: 19230039 PMCID: PMC2653378 DOI: 10.3748/wjg.15.774] [Citation(s) in RCA: 17] [Impact Index Per Article: 1.1] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Indexed: 02/06/2023] Open
Abstract
The process of intestinal adaptation (“enteroplasticity”) is complex and multifaceted. Although a number of trophic nutrients and non-nutritive factors have been identified in animal studies, successful, reproducible clinical trials in humans are awaited. Understanding mechanisms underlying this adaptive process may direct research toward strategies that maximize intestinal function and impart a true clinical benefit to patients with short bowel syndrome, or to persons in whom nutrient absorption needs to be maximized. In this review, we consider the morphological, kinetic and membrane biochemical aspects of enteroplasticity, focus on the importance of nutritional factors, provide an overview of the many hormones that may alter the adaptive process, and consider some of the possible molecular profiles. While most of the data is derived from rodent studies, wherever possible, the results of human studies of intestinal enteroplasticity are provided.
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Crampton RF. Nutritional and metabolic aspects of peptide transport. CIBA FOUNDATION SYMPOSIUM 2008:1-10. [PMID: 4949895 DOI: 10.1002/9780470719879.ch1] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/13/2023]
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Gilbert ER, Wong EA, Webb KE. Board-invited review: Peptide absorption and utilization: Implications for animal nutrition and health. J Anim Sci 2008; 86:2135-55. [PMID: 18441086 DOI: 10.2527/jas.2007-0826] [Citation(s) in RCA: 218] [Impact Index Per Article: 12.8] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/12/2022] Open
Abstract
Over the last 50 yr, the study of intestinal peptide transport has rapidly evolved into a field with exciting nutritional and biomedical applications. In this review, we describe from a historical and current perspective intestinal peptide transport, the importance of peptides to whole-body nutrition, and the cloning and characterization of the intestinal peptide transporter, PepT1. We focus on the nutritional significance of peptide transport and relate these findings to livestock and poultry. Amino acids are transported into the enterocyte as free AA by a variety of AA transporters that vary in substrate specificity or as di- and tripeptides by the peptide transporter, PepT1. Expression of PepT1 is largely restricted to the small intestine in most species; however, in ruminants, peptide transport and activity is observed in the rumen and omasum. The extent to which peptides are absorbed and utilized is still unclear. In ruminants, peptides make a contribution to the portal-drained visceral flux of total AA and are detected in circulating plasma. Peptides can be utilized by the mammary gland for milk protein synthesis and by a variety of other tissues. We discuss the factors known to regulate expression of PepT1 including development, diet, hormones, diurnal rhythm, and disease. Expression of PepT1 is detected during embryological stages in both birds and mammals and increases with age, a strategic event that allows for the immediate uptake of nutrients after hatch or birth. Both increasing levels of protein in the diet and dietary protein deficiencies are found to upregulate the peptide transporter. We also include in this review a discussion of the use of dietary peptides and potential alternate routes of nutrient delivery to the cell. Our goal is to impart to the reader the nutritional implications of peptide transport and dietary peptides and share discoveries that shed light on various biological processes, including rapid establishment of intestinal function in early neonates and maintenance of intestinal function during fasting, starvation, and disease states.
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Affiliation(s)
- E R Gilbert
- Department of Animal and Poultry Sciences, Virginia Polytechnic Institute and State University, Blacksburg 24061-0306, USA
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Zhou Z, Isshiki Y, Yamauchi K, Nakahiro Y. Effects of force‐feeding and dietary cereals on gastrointestinal size, intestinal absorptive ability and endogenous nitrogen in ducks. Br Poult Sci 2007. [DOI: 10.1080/00071669008417261] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 10/22/2022]
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Abstract
Intestinal failure is a condition characterized by malnutrition and/or dehydration as a result of the inadequate digestion and absorption of nutrients. The most common cause of intestinal failure is short bowel syndrome, which occurs when the functional gut mass is reduced below the level necessary for adequate nutrient and water absorption. This condition may be congenital, or may be acquired as a result of a massive resection of the small bowel. Following resection, the intestine is capable of adaptation in response to enteral nutrients as well as other trophic stimuli. Identifying factors that may enhance the process of intestinal adaptation is an exciting area of research with important potential clinical applications.
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Tappenden KA. Mechanisms of enteral nutrient-enhanced intestinal adaptation. Gastroenterology 2006; 130:S93-9. [PMID: 16473079 DOI: 10.1053/j.gastro.2005.11.051] [Citation(s) in RCA: 71] [Impact Index Per Article: 3.7] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 02/11/2005] [Accepted: 11/14/2005] [Indexed: 12/02/2022]
Abstract
The role of enteral nutrients in maintaining small intestinal structure and function is well established. Evidence that enteral nutrients induce intestinal adaptation include the structural and functional gradient along the length of the healthy intestine, the atrophy and functional compromise induced by fasting and parenteral nutrition, and the enhanced adaptive capacity of the distal intestine following partial enterectomy. Key mechanisms contributing to enteral nutrient-induced intestinal adaptation include nonspecific luminal stimulation and that provided by specific nutrients, "functional workload" induced by polymeric nutrients, potential stimulation of pancreaticobiliary secretions, secretion of humoral mediators, and induction of intestinal hyperemia.
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Affiliation(s)
- Kelly A Tappenden
- Department of Food Science and Human Nutrition, Division of Nutritional Sciences, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
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Thiesen A, Drozdowski L, Iordache C, Neo CC, Woudstra TD, Xenodemetropoulos T, Keelan M, Clandinin MT, Thomson ABR, Wild G. Adaptation following intestinal resection: mechanisms and signals. Best Pract Res Clin Gastroenterol 2003; 17:981-95. [PMID: 14642861 DOI: 10.1016/s1521-6918(03)00097-0] [Citation(s) in RCA: 26] [Impact Index Per Article: 1.2] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Indexed: 01/31/2023]
Abstract
The intestine has an inherent ability to adapt morphologically and functionally in response to internal and external environmental changes. The functional adaptations encompass modifications of the brush border membrane fluidity and permeability, as well as up- or down-regulation of carrier-mediated transport. Intestinal adaptation improves the nutritional status following the loss of a major portion of the small intestine, following chronic ingestion of ethanol, following sublethal doses of abdominal irradiation, in diabetes, in pregnancy and lactation, with ageing, and with fasting and malnutrition. Following intestinal resection, morphological and functional changes occur depending upon the extent of the intestine removed, the site studied, and the lipid content of the diet. Therefore, intestinal adaptation has important implications in the survival potential and welfare of the host. An understanding of the mechanisms of, and signals for, intestinal adaptation in the experimental setting forms the basis for the use of management strategies in humans with the short-bowel syndrome.
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Affiliation(s)
- A Thiesen
- Nutrition and Metabolism Research Group, Division of Gastroenterology, Department of Medicine, University of Alberta, 519 Newton Research Building, 205 College Plaza, 8215-112 Street, Edmonton, Alta, Canada T6G 2C2.
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16
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Polache A, Martin-Algarra RV, Guerri C. Effects of chronic alcohol consumption on enzyme activities and active methionine absorption in the small intestine of pregnant rats. Alcohol Clin Exp Res 1996; 20:1237-42. [PMID: 8904977 DOI: 10.1111/j.1530-0277.1996.tb01118.x] [Citation(s) in RCA: 17] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 02/02/2023]
Abstract
The present study evaluates the effect of chronic alcohol intake on the intestinal transport of methionine during pregnancy. For this purpose, we have used an in vitro technique that allows measurement of the unidirectional influx of the amino acids across the brush-border membrane of the rat mid-jejunum, and the basolateral membrane enzyme Na+, K+-ATPase was also evaluated in the duodenum and jejunum. For chronic alcohol treatment, the rats were fed a liquid diet containing ethanol (36% of calories) or an isocaloric diet-(pair-fed control) for 5 weeks before and during pregnancy. Animals were killed at 21 days of gestation. Results from the kinetic analysis revealed that chronic ethanol treatment reduces the maximum transport (Jm) of methionine uptake when compared with controls. Further experiments performed in the presence and absence of sodium have shown that ethanol selectively inhibited Na+-dependent methionine transport. At the same time, this treatment significantly reduced the levels of Na+, K+-ATPase in ethanol-fed rats compared with the controls. Alterations in methionine intestinal transport in pregnant alcohol-fed rats may contribute to the ethanol-induced fetal growth abnormalities.
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Affiliation(s)
- A Polache
- Departamento de Farmacia y Tecnología Farmacéutica, Universidad de Valencia, Spain
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17
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Sanchís D, Alemany M, Remesar X. L-alanine transport in small intestine brush-border membrane vesicles of obese rats. BIOCHIMICA ET BIOPHYSICA ACTA 1994; 1192:159-66. [PMID: 8018696 DOI: 10.1016/0005-2736(94)90114-7] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/28/2023]
Abstract
Membrane vesicles from the small intestine brush border were obtained and used to determine the possible effects of genetic or nutritional obesity on L-alanine uptake. Membrane vesicles from Zucker fa/fa obese rats and cafeteria diet-fed Zucker Fa/? rats showed the same characteristics as those of standard diet-fed lean animals. All preparations showed sodium-dependent transport as the main pathway for L-alanine uptake within the substrate concentration range tested. The apparent substrate affinity constant (Km) values and the pattern of inhibition of Na(+)-dependent L-alanine uptake by other amino acids (L-leucine and L-glutamine), suggests that system B involved in the transport of dipolar amino acids (formerly named Neutral Brush Border System) participates in the Na(+)-dependent transport of L-alanine. The affinity constant (Km) for L-alanine was essentially the same for all the groups studied (in the range of 10 mM). However, there was a higher (P < 0.05) maximal capacity (Vmax) in preparations from diet-induced obese animals (cafeteria diet) than that of genetically obese rats. These results indicate that either nutritional or genetic obesity may modify the capacity but not the affinity of transport systems for L-alanine uptake in the brush border of rat small intestine.
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Affiliation(s)
- D Sanchís
- Departament de Bioquímica i Fisiologia, Facultat de Biologia, Universitat de Barcelona, Spain
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Muñíz R, Burguillo L, del Castillo JR. Effect of starvation on neutral amino acid transport in isolated small-intestinal cells from guinea pigs. Pflugers Arch 1993; 423:59-66. [PMID: 8488093 DOI: 10.1007/bf00374961] [Citation(s) in RCA: 16] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/31/2023]
Abstract
The effects of starvation on neutral amino acid transport were examined in isolated enterocytes. Starvation stimulated L-alanine transport by the Na(+)-dependent system A and the Na(+)-independent system L without producing any changes in either the Na(+)-dependent systems ASC or the passive non-mediated uptake. Starvation produces a twofold increase in Vmax of system A without any change in Kt. Starvation produces an increase in Vmax of system L of 1.7 times without any change in Kt. Activation of systems A and L by starvation was reversible with subsequent refeeding. The effects of a series of amino acids on systems A and L were evaluated. A different inhibition pattern was found in starved animals as compared to controls. Starvation increases Na(+)-dependent L-alanine uptake and Na(+)-independent cycloleucine uptake by small-intestinal brush-border membrane vesicles. These results suggest that starvation stimulates amino acid transport across the apical plasma membrane of the enterocytes by inducing specific carrier units.
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Affiliation(s)
- R Muñíz
- Laboratorio de Fisiología Gastrointestinal, Instituto Venezolano de Investigaciones Científicas (IVIC), Caracas
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Savory CJ. Gastrointestinal morphology and absorption of monosaccharides in fowls conditioned to different types and levels of dietary fibre. Br J Nutr 1992; 67:77-89. [PMID: 1312342 DOI: 10.1079/bjn19920010] [Citation(s) in RCA: 14] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/26/2022]
Abstract
To test a possible influence of dietary fibre on intestinal sugar uptake, rates of absorption of 10 mM-D-[U-14C] glucose and 10 mM-D-[U-14C] xylose were measured in either jejunum or (distal) caecum, by in vivo lumen perfusion, in immature female fowls preconditioned to a standard diet containing (g/kg) either 0, 100, 200 or 400 added dried grass, 200 powdered cellulose, or 200 grass with a polysaccharidase enzyme supplement. When birds were killed after perfusion, dimensions of (unperfused) parts of their alimentary tracts were determined, and recoveries of 14C radioactivity in some body tissues were compared with measured activities absorbed. On average, absorption of glucose was 1.9 and 1.2 times faster than xylose in jejunum and caecum respectively, although these differences varied with dietary treatment and order of perfusion. Increasing grass in the diet caused significant changes in xylose absorption rate in both jejunum and caecum, but only when it was perfused before glucose. With any one sugar and intestinal segment, mean rates of absorption were correlated positively with corresponding mean rates of fluid loss from perfusate. Although their influence on sugar absorption was not well defined, the dietary fibre treatments had more pronounced effects on gross dimensions of parts of the alimentary tract and, hence, potentially on total rates of absorption. Compared with the basal diet, addition of 100, 200 or 400 g grass/kg or 200 g cellulose/kg caused significant increases in small intestine length while 200 g grass/kg with supplementary enzyme did not, and combined caecal length increased with the 400 g grass/kg and the supplementary enzyme treatments. Absorbed 14C activity was recovered in plasma after jejunal perfusions but not caecal ones, whereas it was recovered in liver and in the flushed perfused segment after both types of perfusion. Since there was overlap in absorption rates between jejunum and caecum, this result suggests that the liver may be able to distinguish and treat differently compounds absorbed in the two regions.
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Affiliation(s)
- C J Savory
- AFRC Institute of Animal Physiology and Genetics Research, Roslin, Midlothian
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20
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Cheeseman CI, Harley B. Adaptation of glucose transport across rat enterocyte basolateral membrane in response to altered dietary carbohydrate intake. J Physiol 1991; 437:563-75. [PMID: 1890649 PMCID: PMC1180063 DOI: 10.1113/jphysiol.1991.sp018611] [Citation(s) in RCA: 43] [Impact Index Per Article: 1.3] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/29/2022] Open
Abstract
1. The effect of changes in the carbohydrate content of the diet on D-glucose transport across the basolateral membrane of rat enterocytes has been compared with alterations in transport across the brush-border membrane. 2. Measurement of carrier-mediated D-glucose uptake across the jejunal brush border from animals fed a low- or high-carbohydrate diet showed a change in the maximal rate of transport by 7 days which was maintained for 14 days. The low-carbohydrate diet produced a progressive decline in uptake whereas the high-carbohydrate diet increased the transport. There was no alteration in the apparent affinity constant as a result of the dietary manipulations and no discernible trend for changes in the passive permeability to glucose. 3. Transport of D-glucose across the basolateral membrane was also affected by the dietary composition. After 7 days the maximal transport rate was greater in the animals fed the high-carbohydrate diet. However, while this increase was maintained for 14 days, uptake into vesicles prepared after 2 weeks on the low-carbohydrate diet showed a return to control levels. 4. A detailed analysis of the time course of these responses showed the effect on basolateral membrane transport to be inducible within 3 days of switching from the low- to the high-carbohydrate diet and could be reversed within a similar period. 5. Kinetic studies using purified basolateral membrane vesicles confirmed that the change in transport was the result of an increase in the maximal transport rate. Analysis of cytochalasin B binding to these membranes showed a parallel change in the number of glucose-inhibitable binding sites. 6. The component of the diet responsible for these changes was further investigated by replacing the glucose in the high-carbohydrate food with galactose, fructose, mannose or 3-O-methylglucose. Only glucose and fructose produced any significant change in the transport across the basolateral membrane. 7. It is concluded that in response to changes in the carbohydrate content of the diet there are alterations in the capacity for glucose transport across the basolateral membrane of the enterocyte as well as in the brush-border membrane. The change in transport across the basolateral membrane is best explained by an increase in the number of glucose carriers in this membrane.
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Affiliation(s)
- C I Cheeseman
- Department of Physiology, University of Alberta, Edmonton, Canada
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21
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Poullain MG, Cezard JP, Marche C, Macry J, Roger L, Grasset E, Broyart JP. Effects of dietary whey proteins, their peptides or amino-acids on the ileal mucosa of normally fed and starved rats. Clin Nutr 1991; 10:49-54. [PMID: 16839894 DOI: 10.1016/0261-5614(91)90081-m] [Citation(s) in RCA: 16] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/22/1990] [Accepted: 09/28/1990] [Indexed: 12/29/2022]
Abstract
The effects of three liquid diets, differing only in the molecular form of the nitrogen source (whole whey proteins, WP; trypsic whey protein hydrolysate, WPH, and amino-acid mixture, AAM) were studied on the mucosa morphology and brush border hydrolase (BBH) activities (disaccharidases, peptidases) of the ileum of normally fed male Wistar rats (controls) and during refeeding of rats starved for 72h. All three diets produced repair of the fasting induced mucosal atrophy; the AAM diet gave the most rapid response and highest villus height (p < 0.01). This was correlated with an increase in crypt mitoses (p < 0.01). Similar results were obtained in controls with AAM. The sucrase (S) and acid amino peptidase (AAP) specific activities of controls were higher (p < 0.01) on the WPH diet; neutral amino peptidase (NAP) was unaffected. Dipeptidyl peptidase IV (DDP) was lowest on AAM while glucoamylase (G) highest on WP. Fasting increased S and DDP activity, and produced no change in the other BBH. Large variations in BBH occurred during refeeding except for NAP which remained stable. Control values were restored at 96h, except for AAP. The results show that BBH and mucosa morphology of the ileum in the rat can be modified by the molecular form of the nitrogen source and that the nutritional status interferes with this adaptation. These data could have implications for the therapy of small bowel disease.
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Affiliation(s)
- M G Poullain
- INSERM U120, Robert Debré Hospital, 48 Bd Sérurier, 75019, Paris, France
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22
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23
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Intestinal amino acid transport: an overview. THE INTERNATIONAL JOURNAL OF BIOCHEMISTRY 1990; 22:931-7. [PMID: 1980895 DOI: 10.1016/0020-711x(90)90198-c] [Citation(s) in RCA: 13] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 12/29/2022]
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24
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Dhaunsi G, Sidhu G, Garg U, Singh Y, Chakravarti R, Bhatnagar R. Effects on Intestinal Nutrient Uptake and Brush Border Membrane Enzymes in Response to Atherogenic Diet in Rhesus Monkeys. J Med Primatol 1989. [DOI: 10.1111/j.1600-0684.1989.tb00414.x] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.0] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/29/2022]
Affiliation(s)
- G.S. Dhaunsi
- Department of Experimental MedicinePostgraduate Institute of Medical Education and ResearchChandigarh
| | - G.S. Sidhu
- Department of Experimental MedicinePostgraduate Institute of Medical Education and ResearchChandigarh
| | - U.C. Garg
- Department of Experimental MedicinePostgraduate Institute of Medical Education and ResearchChandigarh
| | - Y. Singh
- Department of BiochemistryV.P. Chest InstituteUniversity of DelhiDelhiIndia
| | - R.N. Chakravarti
- Department of Experimental MedicinePostgraduate Institute of Medical Education and ResearchChandigarh
| | - R. Bhatnagar
- Department of Experimental MedicinePostgraduate Institute of Medical Education and ResearchChandigarh
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Gross CJ, Stiles JE, Savaiano DA. Effect of nutritional state and allopurinol on purine metabolism in the rat small intestine. BIOCHIMICA ET BIOPHYSICA ACTA 1988; 966:168-75. [PMID: 3390463 DOI: 10.1016/0304-4165(88)90140-7] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/05/2023]
Abstract
The effect of fasting and refeeding on the uptake and retention of purines by the small intestine of the rat was studied in vivo. Short-term uptake and incorporation into nucleotides of the purine bases adenine, guanine and hypoxanthine and the nucleoside inosine were evaluated in the proximal jejunum. After 5 min, more label was recovered in the intestinal contents in fasted rats, indicating that total absorption was reduced. However, intestinal retention of purines (50 nmol dose) was elevated with fasting (27.2 vs. 16.6 nmol/g for adenine, 5.7 vs. 3.0 nmol/g for guanine and 16.1 vs. 7.4 nmol/g for hypoxanthine, for fed vs. fasted, respectively). After 1 day of refeeding, retention remained elevated for adenine (27.4 nmol/g) and guanine (5.5 nmol/g). After 3 days of refeeding intestinal weight and retention of labeled purines returned to the unfasted levels. Nucleotide formation from all purine bases was greater in the intestinal tissue of fasted as compared to fed rats (25.4 vs. 11.4 nmol/g for adenine, 1.32 vs. 0.24 nmol/g for guanine, and 2.84 vs. 0.82 nmol/g for hypoxanthine). At a higher dose (3000 nmol) hypoxanthine and inosine were retained to a greater extent in the fasted than in the fed state. Pretreatment with allopurinol (a xanthine oxidase inhibitor) reduced the absorption of hypoxanthine, increased the retention of label in the tissue 4-fold or more, and elevated nucleotide formation 10-fold or more. Fasting and allopurinol treatment, both known affectors of xanthine oxidase activity, enhanced both the retention of dietary purine and nucleotide formation.
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Affiliation(s)
- C J Gross
- Department of Food Science and Nutrition, University of Minnesota, St. Paul 55108
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Abstract
Studies were carried out to determine the role of luminal amino acids and metabolic balance in in vivo amino acid absorption. Previous in vitro studies have shown that adaptation of amino acid transport is a complex phenomenon. In the first series of experiments, parenterally nourished rats received a 7-day jejunal infusion of either 3% aspartic acid, glutamine, lysine, valine, or mixed amino acids. A single-pass perfusion was performed to determine the effects of infusates on 5 mM valine, aspartic acid, and lysine absorption. Compared with controls receiving luminal saline, prior glutamine infusion increased valine absorption; prior valine, glutamine, and aspartic acid infusion significantly increased aspartic acid absorption; and prior valine and lysine infusion significantly increased lysine absorption. The mixed amino acid solution had no effect. The effects of metabolic balance were examined by comparing fasted rats with parenterally fed and orally fed rats. Within 24 h fasting significantly increased valine and aspartic acid absorption, despite a significant decrease in intestinal mass.
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Affiliation(s)
- M L Bierhoff
- Division of Gastroenterology and Nutrition, Albert Einstein Medical Center, Philadelphia, Pennsylvania
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27
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Nutrient Transport Across Vertebrate Intestine. ADVANCES IN COMPARATIVE AND ENVIRONMENTAL PHYSIOLOGY 1988. [DOI: 10.1007/978-3-642-73375-8_4] [Citation(s) in RCA: 18] [Impact Index Per Article: 0.5] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/24/2023]
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28
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Marciani P, Lindi C, Faelli A, Esposito G. Effects of semistarvation on transintestinal D-glucose transport and D-glucose uptake in brush border and basolateral membranes of rat enterocytes. Pflugers Arch 1987; 408:220-3. [PMID: 3575088 DOI: 10.1007/bf02181462] [Citation(s) in RCA: 11] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/06/2023]
Abstract
The present work shows that semistarvation (8-10 g of food for 10 days) increases net D-glucose, Na+ and water transport in the everted and perfused rat jejunum. A linear and positive correlation between cell sugar concentration and transport was found in control and semistarved rats, but the phenomenon was more relevant only in semistarved animals. Membrane vesicle experiments showed that semistarvation increases sugar overshoot only in brush border membrane vesicles, while this situation does not occur in basolateral membrane vesicles. The effect of partial food deprivation seems to enhance net sugar transport by increasing sugar entry across the apical membrane of enterocytes.
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29
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Abstract
Luminal nutrients are a major effector of intestinal adaptation. Amino acids are trophic to the intestine, but their role in regulating amino acid transport is not well documented. The presence of several distinct amino acid transport systems raises the question of whether adaptation is class-specific. Studies were carried out in parenterally nourished rats receiving a 7-day jejunal infusion of a 3% solution of either aminoisobutyric acid, aspartic acid, glutamine, histidine, lysine, or valine. While all amino acids were trophic to the intestine, their effects on the in vitro uptake of 0.1, 1.0 and 10.0 mM aspartic acid, lysine, and valine (representative acid, basic, and neutral amino acids) were variable and nonspecific. Compared to controls receiving either total parenteral nutrition alone or total parenteral nutrition plus luminal saline, prior lysine and aspartic acid infusion significantly increased in vitro uptake of all three amino acids tested, whereas valine had little effect on transport. No effect on transport was seen with glutamine (actively metabolized by the intestine as is aspartic acid), aminoisobutyric acid (a nonmetabolizable amino acid congener), or histidine (the most trophic amino acid). In conclusion, while individual amino acids cause an adaptation of amino acid uptake, the effects are nonspecific and independent of their metabolic or trophic potential.
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Diamond JM, Karasov WH, Cary C, Enders D, Yung R. Effect of dietary carbohydrate on monosaccharide uptake by mouse small intestine in vitro. J Physiol 1984; 349:419-40. [PMID: 6737300 PMCID: PMC1199346 DOI: 10.1113/jphysiol.1984.sp015165] [Citation(s) in RCA: 128] [Impact Index Per Article: 3.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/21/2023] Open
Abstract
Using intestinal sleeves in vitro, we studied the effect of dietary carbohydrate on active monosaccharide uptake in mice. Dietary carbohydrate did not affect numerous parameters of intestinal structure, such as length, circumference, weight, protein content, villus dimensions and density, and area at the villus level. Mice on a carbohydrate-free diet had active D-glucose uptake relatively independent of position along the small intestine. A carbohydrate-containing diet reversibly and within 1 day stimulated uptake except in the ileum, restoring the proximal-to-distal gradient in glucose uptake normally observed. This stimulation involved a 81-116% increase in the Michaelis- Menton constant Vmax, and also an apparent increase in the Michaelis- Menton constant Km, that may however be an artifact arising from unstirred-layer effects. Active uptake of 3-O-methyl-D-glucose also increased, permeability to glucose remained unchanged, and proline uptake reversibly decreased (probably due to the lower protein content of the carbohydrate-containing diets). The effect of fasting on active monosaccharide uptake seemed largely due to withdrawal of dietary carbohydrate, rather than of calories per se. It is concluded that dietary carbohydrate causes induction of monosaccharide carriers in the intestine, along with its more familiar induction of pancreatic amylase and intestinal disaccharidases. Substrate-dependent carrier induction may be physiologically significant in maintaining the proximal-to-distal gradient of glucose transport. An appendix presents measurements of villus area as a function of position along the intestine.
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33
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Wolffram S, Scharrer E. Effect of feeding a high protein diet on amino acid uptake into rat intestinal brush border membrane vesicles. Pflugers Arch 1984; 400:34-9. [PMID: 6709488 DOI: 10.1007/bf00670533] [Citation(s) in RCA: 24] [Impact Index Per Article: 0.6] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/21/2023]
Abstract
Uptake of the neutral amino acid L-leucine into isolated rat intestinal brush border membrane (= BBM) vesicles and into a jejunal mucosa preparation as affected by the protein content of the diet was investigated. Adult rats fed either a high carbohydrate (HC) diet (11% protein) or a high protein (HP) diet (77% protein) for several weeks were used for the experiments. The time course of L-leucine uptake into BBM vesicles prepared from the small intestine of HC- or HP-rats was studied under conditions of an inwardly directed Na+-gradient and under Na+-equilibrium conditions. Furthermore, in one series of experiments the Na+-equilibrium was replaced by a K+-equilibrium. L-leucine uptake under Na+-gradient conditions displayed the overshoot phenomenon typically associated with Na+-gradient-dependent active transport processes in BBM vesicles and the overshoot in group HP exceeded that in group HC significantly. Under both Na+- and K+-equilibrium conditions L-leucine uptake into the BBM-vesicles also was faster in group HP. Finally L-leucine uptake into jejunal mucosa in group HP exceeded that in group HC, too. The results therefore indicate that Na+-dependent and Na+-independent transport of neutral amino acids across the intestinal brush border membrane adapts to the dietary protein level.
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34
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Wolfram S, Giering H, Scharrer E. Na+-gradient dependence of basic amino acid transport into rat intestinal brush border membrane vesicles. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. A, COMPARATIVE PHYSIOLOGY 1984; 78:475-80. [PMID: 6147229 DOI: 10.1016/0300-9629(84)90581-4] [Citation(s) in RCA: 37] [Impact Index Per Article: 0.9] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/18/2023]
Abstract
Uptake of L-arginine and L-lysine into brush border membrane (BBM) vesicles from rats fed either a high protein (HP) or a high carbohydrate (HC) diet was studied under conditions of a transmembrane Na+-gradient (Na+out greater than Na+in) or a Na+-equilibrium (Na+out = Na+in). The Na+-gradient caused a stronger stimulation of basic amino acid transport across the BBM in group HP than in group HC. Replacing Cl- as counter ion of Na+ by SCN- in the Na+-gradient experiments did not affect L-lysine uptake. In one series of experiments inhibitory effects of several amino acids and D-glucose on Na+-gradient-dependent L-arginine transport into BBM vesicles were tested. L-Lysine showed the strongest inhibition of L-arginine uptake, but also L-leucine, L-alanine and D-glucose caused a significant decrease of L-arginine uptake into BBM vesicles. The main conclusions are that a transmembrane Na+-gradient is able to energize the transport of basic amino acids across the intestinal BBM and that the transport mechanism of the intestinal BBM for basic amino acids adapts to the protein content of the diet.
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35
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Karasov WH, Pond RS, Solberg DH, Diamond JM. Regulation of proline and glucose transport in mouse intestine by dietary substrate levels. Proc Natl Acad Sci U S A 1983; 80:7674-7. [PMID: 6584881 PMCID: PMC534403 DOI: 10.1073/pnas.80.24.7674] [Citation(s) in RCA: 45] [Impact Index Per Article: 1.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/20/2023] Open
Abstract
Active uptake of D-glucose and L-proline at 50 mM was measured in everted intestinal sleeves of mice whose dietary carbohydrate and protein levels were being varied experimentally. Compared to a nearly carbohydrate-free meat diet, a 50% carbohydrate laboratory chow diet stimulated active glucose uptake in the proximal intestine without affecting proline uptake, passive glucose permeability, or several measures of mucosal mass. Switching from a low-protein high-carbohydrate to a high-protein no-carbohydrate diet reversibly stimulated proline uptake while inhibiting glucose uptake. For each solute and diet switch, the stimulation of transport was complete within 1 day, while the inhibition required several days. The results imply induction and repression of intestinal glucose and proline transport by dietary substrate levels. This mechanism, in conjunction with the normal gradient of nutrient concentrations along the intestine, is probably largely responsible for the gradient in nutrient transport along the intestine.
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36
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Asghar A, Henrickson RL. Chemical, biochemical, functional, and nutritional characteristics of collagen in food systems. ADVANCES IN FOOD RESEARCH 1982; 28:231-372. [PMID: 6762058 DOI: 10.1016/s0065-2628(08)60113-5] [Citation(s) in RCA: 112] [Impact Index Per Article: 2.6] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/21/2023]
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Abstract
Peptides and not amino acids are the prevailing degradation products of protein digestion which are formed in the intestinal lumen and are absorbed from the mucosa. These two families differ in absorption. The differences become manifest when the absorption of peptide mixtures is compared with that of equimolecular mixtures of free amino acids. The absorption of peptides occurs in two different ways: 1. Transport of intact peptides through the membrane into the mucosal cell and subsequent hydrolysis by intracellular peptide hydrolases. 2. Hydrolysis of the peptides by peptide hydrolases localized on the luminal side of the mucosal cell membrane and subsequent transport of the amino acids thus formed through the membrane. The two mechanisms of absorption do not exclude each other. The way by which energy is supplied for the transport is not yet elucidated. The transport of intact peptides is of nutritive importance only in case of dipeptides and tripeptides. It enables in particular the introduction of peptides that cannot be cleft by membrane-bound peptide hydrolases. The hydrolysis of peptides by membrane-bound peptide hydrolases and the subsequent transport of released amino acids is of importance for long-chain peptides. The difference in absorbing behaviour between the free amino acids released in the intestinal lumen and the amino acids released by peptide hydrolases at the mucosal membrane is discussed.
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LI-CHAN EUNICE, NAKAI SHURYO. Nutrtional Evaluation of Covalently Lysine Enriched Wheat Gluten by Tetrahymena Bioassay. J Food Sci 1981. [DOI: 10.1111/j.1365-2621.1981.tb04500.x] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 11/30/2022]
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39
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Gardner ML, Plumb JA. The differential effects of two salts of 5-fluorouracil and of dietary restriction on absorption by rat small intestine. Biochem Pharmacol 1981; 30:201-7. [PMID: 7225137 DOI: 10.1016/0006-2952(81)90078-2] [Citation(s) in RCA: 3] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/24/2023]
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40
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41
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Matthews D, Payne J. Transmembrane Transport of Small Peptides. CARRIERS AND MEMBRANE TRANSPORT PROTEINS 1980. [DOI: 10.1016/s0070-2161(08)60119-7] [Citation(s) in RCA: 76] [Impact Index Per Article: 1.7] [Reference Citation Analysis] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 12/04/2022]
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42
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Wilson HD, Schedl HP. Effects of diet, energy restriction and diabetes on hexose transport in the rat. Br J Nutr 1979; 41:443-54. [PMID: 465435 DOI: 10.1079/bjn19790059] [Citation(s) in RCA: 2] [Impact Index Per Article: 0.0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 12/15/2022]
Abstract
1. Effects of dietary composition, energy restriction, and diabetes on hexose absorption were examined by feeding male rats isoenergetic, semi-synthetic diets of differing carbohydrate and protein content. Diets were carbohydrate, (g/kg): 890 sucrose; carbohydrate-protien, 500 sucrose, 390 casein; or protein, 890 casein. An additional group was fed on commercial rat chow ad lib. 2. Hexose (3-O-methyl-D-glucose) absorption was measured by luminal perfusion of the entire small intestine in situ. Absorption by the total small intestine, i.e. absorption per rat, and absorption per g dry weight of mucosa (specific absorption) were calculated. 3. When semi-synthetic diets were fed at 210 kJ/d to normal animals absorption depended on composition of diets: carbohydrate enhanced or protein suppressed hexose absorption. Dietary carbohydrate as glucose, dextrimaltose or starch gave the same hexose absorption response as sucrose. 4. When diets of normal rats were restricted to 118 kJ/d, specific absorption was independent of dietary composition and was increased for all dietary groups to the level of the group fed on the carbohydrate diet at 210 kJ/d. 5. When diabetic rats were given 210 kJ/d, hexose specific absorption was the same for all diabetic groups independent of dietary composition and was equal to that of controls given carbohydrate, but greater than that of protein-fed controls. 6. Thus, when two of the three stimuli (i.e. carbohydrate diet plus energy restriction or diabetes) were combined, the effect was not additive, and the response of hexose specific absorption to diabetes and energy restriction was the same: absorption was independent of dietary composition and was stimulated relative to controls fed on diets containing protein. 7. The pattern of response of total small intestinal hexose absorption to the stimuli of dietary composition, energy restriction and diabetes was similar to that of specific absorption. 8. Compared with groups given semi-synthetic diets, rats eating commercial rat chow ad lib. (approximately 286 kJ/d) showed increased mucosal mass and decreased specific absorption, but total absorption was similar to that of the carbohydrate and carbohydrate-protein-fed groups. 9. In a separate study in control rats, specific and total intestinal absorption of L-leucine did not respond to dietary composition, i.e. level of protein fed.
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45
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Stevenson NR, Ferrigni F, Parnicky K, Day S, Fierstein JS. Effect of changes in feeding schedule on the diurnal rhythms and daily activity levels of intestinal brush border enzymes and transport systems. BIOCHIMICA ET BIOPHYSICA ACTA 1975; 406:131-45. [PMID: 240440 DOI: 10.1016/0005-2736(75)90048-6] [Citation(s) in RCA: 59] [Impact Index Per Article: 1.2] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 12/13/2022]
Abstract
The activities of rat intestinal enzymes, sucrase, lactase, maltase, trehalase, gamma-glutamyltransferase, leucylnaphthylamide-hydrolyzing activity, and the transport system for glucose follow diurnal rhythms on ad libitum and restricted feeding regimes. In response to 6 days of restricted feeding, food available between 1400 and 1800 Eastern Standard Time, all rhythms shifted in time and the daily levels of activities were changed. Alkaline phosphatase activity followed a diurnal rhythm only in restricted fed animals. In restricted fed rats several activity patterns were observed, some with short periods of maximum activity, 3 h or less, and some with plateaus of maximum activity, 5-9 h long. In respect to the time of day of the synchronizer, sucrase peaked before feeding, glucose transport peaked during feeding, alkaline phosphatase peaked after feeding, and the other enzymes had higher levels of activity before, during and after feeding. The effect of restricted feeding on the daily activity levels were: a decrease in leucylnaphthylamide-hydrolyzing activity, no change in alkaline phosphatase, and increases in the others. These enzyme and transport systems exhibit a large amount of individual regulation or control as reflected by the lack of a uniform activity pattern and response to the synchronizer, and the variation in direction and magnitude of the adaptations to restricted feeding.
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Zimmer M, Bergner H, Simon O. [Resorption and incorporation of radioactive labeled amino acids during administration of various protein carriers in rats. 1. Resorption of 14C leucine and 3H glycine after intragastric administration]. ARCHIV FUR TIERERNAHRUNG 1975; 25:311-26. [PMID: 1233948 DOI: 10.1080/17450397509423195] [Citation(s) in RCA: 18] [Impact Index Per Article: 0.4] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 12/26/2022]
Abstract
Male Albino rats (90-100 g) were fed ad libitum (with limited periods of feeding) for 14 days. The diets were adjusted to a crude protein content of 10%. Powdered whole egg, fish meal, yeast and gelatine were used as protein sources. Additionally, one group of rats was fed a protein-free diet. On the 15th day of experiment the rats were fed a test diet at a level of 2 g per 100 g of body weight. 2 hrs after that the rats received 25 muCi of 3H glycine and 5 muCi of 14C-L-Leucine per 100 g of body weight administered by way of intragastric infusion. It was found that a large proportion of the radioactive amino acids were absorbed as early as after 0.5 hr. The highest rate of absorption was observed in animals fed dietary proteins of poor quality or a protein free diet, so that in animals receiving a gelatine diet or a protein-free diet only 68.4% or 56.4% of the administered amount of 14C activity were detected inside the gastro intestinal tract after 0.5 hr. Analogous data for the 3H activity were 52.4% and 25.3%. Maximum absorption occurred after 3-7 hrs. Following this the level of radioactivity in the intestinal contents again increased reaching a peak value after 14-24 hrs; in the case of 14C activity this peak value amounted to 25.4% of the administered dose in animals fed the gelatine diet and 32.8% in the group receiving the protein-free diet. It was established that the major proportion of the resecreted amount of 14C activity was present in leucine. Until 72 hrs after the intake of 14C activity the level of radioactivity was again found to decline, a processes which was induced by processes occurring in the large intestines. Moreover, evidence was obtained in confirmation of previous findings, indicating that the composition of faecal amino acids was constant and unaffected by dietary proteins.
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Cook GC. Jejunal absorption rates of glucose, glycine and glycylglycine in Zambian African adults with malnutrition. Br J Nutr 1974; 32:503-13. [PMID: 4139969 DOI: 10.1079/bjn19740104] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/09/2023]
Abstract
1. Absorption rates of glucose (from a 200 mM solution), glycine (from a 100 mM solution), and glycylglycine (from a 50 mM solution) have been estimated in six Zambian African adults with clinical evidence of malnutrition. A double-lumen tube technique was used to determine absorption rates from a 300 mm section of jejunum in vivo.2. Two of the subjects had ileal tuberculosis and Kaposi's sarcoma respectively. A third probably had abdominal tuberculosis. Three of them had pellagra. Mean serum albumin concentration was 24 (14–43) g/l. Absorption rates have been compared with those in Zambian Africans (control subjects), previously studied, who had no clinical evidence of malnutrition, systemic infection or of gastrointestinal disease.3. Mean glucose, glycine and glycylglycine absorption rates in the malnourished subjects were not significantly different from those in the control subjects. Mean net water absorption rate from the glucose solution was similar in the malnourished subjects and controls; during the glycine and glycylglycine perfusions the mean net absorption rate was, however, significantly lower in the malnourished subjects (P < 0.01 and P < 0.05 respectively); mean net water transfer during the glycine perfusions was towards the jejunal lumen in the malnourished subjects. One subject with pellagra had an abnormal excretion of D-xylose after a 25 g oral load; all other tests were normal.4. It seems probable that malnutrition must be very severe, with jejunal mucosal abnormalities, before absorption rates of glucose, glycine and glycylglycine are significantly altered. The present study does not support the view that subclinical malnutrition is important in producing malabsorption of dietary components in Zambian African subjects. Systemic bacterial infections, and raised serum γ-globulin and immunoglobulin IgG concentrations have previously been associated with an impairment of glucose absorption rate in Zambian African subjects; those factors seem much more likely than subclinical malnutrition to be relevant, in the context of absorption, in the pathogenesis of overt malnutrition.
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Cook GC. Effect of systemic infections on glycylglycine absorption rate from the human jejunum in vivo. Br J Nutr 1974; 32:163-7. [PMID: 4846160 DOI: 10.1079/bjn19740066] [Citation(s) in RCA: 5] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/12/2023]
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Furuya S, Yugari Y. Daily rhythmic change of L-histidine and glucose absorptions in rat small intestine in vivo. BIOCHIMICA ET BIOPHYSICA ACTA 1974; 343:558-64. [PMID: 4407033 DOI: 10.1016/0304-4165(74)90274-8] [Citation(s) in RCA: 35] [Impact Index Per Article: 0.7] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/10/2023]
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Matthews DM. Absorption of amino acids and peptides from the intestine. CLINICS IN ENDOCRINOLOGY AND METABOLISM 1974; 3:3-16. [PMID: 4609647 DOI: 10.1016/s0300-595x(74)80022-8] [Citation(s) in RCA: 6] [Impact Index Per Article: 0.1] [Reference Citation Analysis] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/11/2023]
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