Waddingham MT, Edgley AJ, Tsuchimochi H, Kelly DJ, Shirai M, Pearson JT. Contractile apparatus dysfunction early in the pathophysiology of diabetic cardiomyopathy. World J Diabetes 2015; 6(7): 943-960 [PMID: 26185602 DOI: 10.4239/wjd.v6.i7.943]
Corresponding Author of This Article
James T Pearson, PhD, Monash Biomedical Imaging Facility, Monash University, 770 Blackburn Road, Clayton, Victoria 3168, Australia. james.pearson@monash.edu
Research Domain of This Article
Physiology
Article-Type of This Article
Review
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Diabetes. Jul 10, 2015; 6(7): 943-960 Published online Jul 10, 2015. doi: 10.4239/wjd.v6.i7.943
Contractile apparatus dysfunction early in the pathophysiology of diabetic cardiomyopathy
Mark T Waddingham, Amanda J Edgley, Hirotsugu Tsuchimochi, Darren J Kelly, Mikiyasu Shirai, James T Pearson
Mark T Waddingham, Amanda J Edgley, Darren J Kelly, Department of Medicine, St Vincent’s Hospital, University of Melbourne, Melbourne, Victoria 3065, Australia
Amanda J Edgley, James T Pearson, Department of Physiology, Monash University, Clayton, Victoria 3800, Australia
Hirotsugu Tsuchimochi, Mikiyasu Shirai, Department of Cardiac Physiology, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan
James T Pearson, Monash Biomedical Imaging Facility, Monash University, Clayton, Victoria 3168, Australia
James T Pearson, Australian Synchrotron, Clayton, Victoria 3168, Australia
Author contributions: Waddingham MT, Edgley AJ and Pearson JT wrote the paper; all authors provided intellectual input, edited and approved the final manuscript.
Supported by The research funding from the International Synchrotron Access Program (AS/IA133) of the Australian Synchrotron (to Pearson JT); A Grant-in-Aid for Scientific Research (#E056, 26670413) from the Ministry of Education, Culture, Sports, Sciences and Technology of Japan (to Shirai M).
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Correspondence to: James T Pearson, PhD, Monash Biomedical Imaging Facility, Monash University, 770 Blackburn Road, Clayton, Victoria 3168, Australia. james.pearson@monash.edu
Telephone: +61-3-99029783 +61-3-99029500
Received: August 27, 2014 Peer-review started: August 28, 2014 First decision: December 17, 2014 Revised: December 30, 2014 Accepted: March 5, 2015 Article in press: March 9, 2015 Published online: July 10, 2015 Processing time: 317 Days and 8.7 Hours
Core Tip
Core tip: Pathological changes in cardiac muscle underlie diabetic cardiomyopathy (DCM) independent of hypertension and atherosclerosis. In advanced diabetes, fibrosis, hypertrophy and apoptosis, reduce myocardial compliance, which leads to increased diastolic filling pressures and overt left ventricular diastolic dysfunction. However, detrimental changes in sarcomeric and other cytoskeletal proteins in the cardiomyocytes of animal models of diabetes precede remodeling of the cardiac extracellular matrix, which has until now been considered the main contributor to diabetic diastolic dysfunction. An important target for preventing early DCM are the protein kinase C/rho-kinase pathways that drive oxidative stress and reduce myosin head cycling and prolong Ca2+ transients.
