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

Graham P. Riley, Valerie Curry, Jeroen DeGroot, Benno van El, Nicole Verzijl, Brian L. Hazleman, Ruud A. Bank

Research output: Contribution to journalArticle

278 Citations (Scopus)


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
Original languageEnglish
Pages (from-to)185-195
Number of pages11
JournalMatrix Biology
Issue number2
Publication statusPublished - Mar 2002

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