Tomasz Guszczyn1, Krzysztof Sobolewski. 1. Department of Medical Biochemistry, Medical Academy of Białystok, ul. Mickiewicza 2, PL-15-089 Białystok, Poland. tombial@mp.pl
Abstract
OBJECTIVE: The defects of collagen metabolism are responsible for the disorganization of extracellular matrix in stomach cancer. Collagen through interaction with integrin receptors regulates the cellular growth, differentiation, gene expression, prolidase and gelatinase activity and plays an important role in tumorigenesis and invasiveness. Although extracellular metalloproteinases initiate the breakdown of collagen in tissues, the final step of its degradation is mediated by prolidase. Therefore, we decided to compare the degradation of collagen in control tissues to gastric cancer tissues. METHODS: We investigated the collagen content (hydroxyproline assay), expressions of beta(1) integrin, prolidase and gelatinases A and B (Western immunoblot) as well activities of prolidase (colorimetric assay) and gelatinases (zymography) in stomach cancer tissue (n = 10). The results were compared with corresponding data obtained for control tissues (n = 10). RESULTS: No differences in the collagen content were found between the studied tissue samples. However, an increase in free proline pool, enhanced gelatinase expression and elevated gelatinolytic activity were found in the tumor tissue. These phenomena were accompanied by a significant elevation in prolidase activity and an increase in beta(1) integrin expression in stomach cancer, compared to control tissue. CONCLUSION: The data presented suggest an enhancement of collagen turnover in stomach cancer. It may be suggested that the increased degradation of collagen by gelatinase in cancer tissue is balanced by an increased biosynthesis of this protein. Copyright 2004 S. Karger AG, Basel.
OBJECTIVE: The defects of collagen metabolism are responsible for the disorganization of extracellular matrix in stomach cancer. Collagen through interaction with integrin receptors regulates the cellular growth, differentiation, gene expression, prolidase and gelatinase activity and plays an important role in tumorigenesis and invasiveness. Although extracellular metalloproteinases initiate the breakdown of collagen in tissues, the final step of its degradation is mediated by prolidase. Therefore, we decided to compare the degradation of collagen in control tissues to gastric cancer tissues. METHODS: We investigated the collagen content (hydroxyproline assay), expressions of beta(1) integrin, prolidase and gelatinases A and B (Western immunoblot) as well activities of prolidase (colorimetric assay) and gelatinases (zymography) in stomach cancer tissue (n = 10). The results were compared with corresponding data obtained for control tissues (n = 10). RESULTS: No differences in the collagen content were found between the studied tissue samples. However, an increase in free proline pool, enhanced gelatinase expression and elevated gelatinolytic activity were found in the tumor tissue. These phenomena were accompanied by a significant elevation in prolidase activity and an increase in beta(1) integrin expression in stomach cancer, compared to control tissue. CONCLUSION: The data presented suggest an enhancement of collagen turnover in stomach cancer. It may be suggested that the increased degradation of collagen by gelatinase in cancer tissue is balanced by an increased biosynthesis of this protein. Copyright 2004 S. Karger AG, Basel.
Authors: Ibrahim Türkbeyler; Tuncer Demir; Yavuz Pehlivan; Davut Sinan Kaplan; Ali Osman Ceribasi; Mustafa Orkmez; Nurten Aksoy; Seyithan Taysi; Bunyamin Kisacik; Ahmet Mesut Onat Journal: Inflammation Date: 2012-10 Impact factor: 4.092