Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology

Riley, Graham P. ORCID: https://orcid.org/0000-0001-5528-5611, Curry, Valerie, DeGroot, Jeroen, van El, Benno, Verzijl, Nicole, Hazleman, Brian L. and Bank, Ruud A. (2002) Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology. Matrix Biology, 21 (2). pp. 185-195. ISSN 1569-1802

Full text not available from this repository.

Abstract

Our aim was to correlate the activity of matrix metalloproteinases (MMPs) with denaturation and the turnover of collagen in normal and pathological human tendons. MMPs were extracted from ruptured supraspinatus tendons (n=10), macroscopically normal (‘control’) supraspinatus tendons (n=29) and normal short head of biceps brachii tendons (n=24). Enzyme activity was measured using fluorogenic substrates selective for MMP-1, MMP-3 and enzymes with gelatinolytic activity (MMP-2, MMP-9 and MMP-13). Collagen denaturation was determined by a-chymotrypsin digestion. Protein turnover was determined by measuring the percentage of d-aspartic acid (% d-Asp). Zymography was conducted to identity specific gelatinases. MMP-1 activity was higher in ruptured supraspinatus compared to control supraspinatus and normal biceps brachii tendons (70.9, 26.4 and 11.5 fmol/mg tendon, respectively; P

Item Type:	Article
UEA Research Groups:	Faculty of Science > Research Groups > Cells and Tissues Faculty of Medicine and Health Sciences > Research Groups > Musculoskeletal Medicine
Depositing User:	Users 2731 not found.
Date Deposited:	18 May 2011 09:19
Last Modified:	24 Sep 2024 10:14
URI:	https://ueaeprints.uea.ac.uk/id/eprint/30748
DOI:	10.1016/S0945-053X(01)00196-2

Actions (login required)

View Item