Brief Article
Copyright ©2010 Baishideng. All rights reserved
World J Gastroenterol. Mar 28, 2010; 16(12): 1500-1505
Published online Mar 28, 2010. doi: 10.3748/wjg.v16.i12.1500
Expression of matrix metalloproteinases 2 and 9 in human gastric cancer and superficial gastritis
Clara Luz Sampieri, Sol de la Peña, Mariana Ochoa-Lara, Roberto Zenteno-Cuevas, Kenneth León-Córdoba
Clara Luz Sampieri, Sol de la Peña, Mariana Ochoa-Lara, Roberto Zenteno-Cuevas, Institute of Public Health, Veracruzana University, Xalapa, Veracruz, CP 91190, Mexico
Sol de la Peña, Biomedical Sciences Doctoral Program, Institute of Health Sciences, Veracruzana University, Xalapa, Veracruz, CP 91190, Mexico
Kenneth León-Córdoba, Dr. Miguel Dorantes Mesa Hospital, Xalapa, Veracruz, CP 91120, Mexico
Author contributions: Sampieri CL designed and performed the research, recruited patients, analyzed the data and wrote the paper; de la Peña S and Ochoa-Lara M performed the research and analyzed the data; Zenteno-Cuevas R analyzed the data; León-Córdoba K recruited patients, performed the research and analyzed the data.
Supported by The National Council on Science and Technology (CONACYT: 85675 and 79628), Institute of Public Health (POA: 2008-2010) and Research Office of Veracruzana University and Public Education Secretariat (SEP-PROMEP-UV: PTC-319)
Correspondence to: Dr. Clara Luz Sampieri, Institute of Public Health, Veracruzana University, Av. Luis Castelazo Ayala S/N, Xalapa, Veracruz, CP 91190, Mexico. csampieri@uv.mx
Telephone: +52-228-8418900 Fax: +52-228-8418935
Received: November 24, 2009
Revised: January 1, 2010
Accepted: January 8, 2010
Published online: March 28, 2010
Abstract

AIM: To assess expression of matrix metalloproteinases 2 (MMP2) and MMP9 in gastric cancer, superficial gastritis and normal mucosa, and to measure metalloproteinase activity.

METHODS: MMP2 and MMP9 mRNA expression was determined by quantitative real-time polymerase chain reaction. Normalization was carried out using three different factors. Proteins were analyzed by quantitative gelatin zymography (qGZ).

RESULTS: 18S ribosomal RNA (18SRNA) was very highly expressed, while hypoxanthine ribosyltransferase-1 (HPRT-1) was moderately expressed. MMP2 was highly expressed, while MMP9 was not detected or lowly expressed in normal tissues, moderately or highly expressed in gastritis and highly expressed in cancer. Relative expression of 18SRNA and HPRT-1 showed no significant differences. Significant differences in MMP2 and MMP9 were found between cancer and normal tissue, but not between gastritis and normal tissue. Absolute quantification of MMP9 echoed this pattern, but differential expression of MMP2 proved conflictive. Analysis by qGZ indicated significant differences between cancer and normal tissue in MMP-2, total MMP-9, 250 and 110 kDa bands.

CONCLUSION: MMP9 expression is enhanced in gastric cancer compared to normal mucosa; interpretation of differential expression of MMP2 is difficult to establish.

Keywords: Gastric cancer; Superficial gastritis; Matrix metalloproteinases; Quantitative real-time polymerase chain reaction; Quantitative zymography