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Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) mRNA is constitutively expressed in bovine, human normal, and osteoarthritic articular chondrocytes
Author(s) -
Zafarullah Muhammad,
Su Suming,
MartelPelletier Johanne,
DiBattista John A.,
Costello Bernard G.,
StetlerStevenson William G.,
Pelletier JeanPierre
Publication year - 1996
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19960201)60:2<211::aid-jcb5>3.0.co;2-#
Subject(s) - matrix metalloproteinase , cartilage , messenger rna , extracellular matrix , tissue inhibitor of metalloproteinase , chemistry , chondrocyte , osteoarthritis , microbiology and biotechnology , endocrinology , medicine , biology , pathology , anatomy , biochemistry , gene , alternative medicine
Tissue inhibitors of metalloproteinases (TIMPs) inhibit the extracellular matrix (ECM) metalloproteinases (MMPs). To determine the source of TIMPs in synovial fluids of patients with osteoarthritis (OA), the ability of chondrocytes to express TIMP‐2 and its regulation by agents found in inflammed joints was investigated. The constitutive TIMP‐2 mRNA expression was demonstrated in chondrocytes from normal bovine, human OA and normal cartilage. The cross‐hybridization of human and bovine TIMP‐2 suggested its evolutionary conservation. Serum, IL‐1, IL‐6 and TGF‐β were unable to augment considerably the basal expression of TIMP‐2 mRNA. TIMP‐1 RNA expression in chondrocytes from human OA cartilage was elevated compared to non‐OA chondrocytes, while TIMP‐2 mRNA levels were similar in both. IL‐1β, IL‐6 and TGF‐β did not affect TIMP‐2 expression but TGF‐β induced TIMP‐1 mRNA in human OA chondrocytes. TIMP‐2 and TIMP‐1 are therefore differentially regulated in chondrocytes and the basal TIMP‐2 levels may be needed for the cartilage ECM integrity. © 1996 Wiley‐Liss, Inc.