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

doi:10.1016/S0945-053X(01)00196-2

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 journal › Article

285 Citations (Scopus)

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

Original language	English
Pages (from-to)	185-195
Number of pages	11
Journal	Matrix Biology
Volume	21
Issue number	2
DOIs	https://doi.org/10.1016/S0945-053X(01)00196-2
Publication status	Published - Mar 2002

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10.1016/S0945-053X(01)00196-2

Cite this

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title = "Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology",

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 ({\textquoteleft}control{\textquoteright}) 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",

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year = "2002",

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TY - JOUR

T1 - Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology

AU - Riley, Graham P.

AU - Curry, Valerie

AU - DeGroot, Jeroen

AU - van El, Benno

AU - Verzijl, Nicole

AU - Hazleman, Brian L.

AU - Bank, Ruud A.

PY - 2002/3

Y1 - 2002/3

N2 - 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

AB - 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

U2 - 10.1016/S0945-053X(01)00196-2

DO - 10.1016/S0945-053X(01)00196-2

M3 - Article

VL - 21

SP - 185

EP - 195

JO - Matrix Biology

JF - Matrix Biology

SN - 0945-053X

IS - 2

ER -