ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to 1L-1α in bovine nasal cartilage

被引:35
作者
Chubinskaya, S
Mikhail, R
Deutsch, A
Tindal, MH
机构
[1] Rush Med Coll, Rush Presbyterian St Lukes Med Ctr, Dept Biochem, Chicago, IL 60612 USA
[2] Rush Med Coll, Rush Presbyterian St Lukes Med Ctr, Rheumatol Sect, Chicago, IL 60612 USA
[3] Procter & Gamble Pharmaceut Inc, Hlth Care Res Ctr, Mason, OH USA
关键词
human articular cartilage; bovine nasal cartilage; osteoarthritis; ADAM-10; protein; interleukin-1; immunohistochemistry;
D O I
10.1177/002215540104900910
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The objective of our study was to determine the tissue distribution and localization of ADAM-10 protein in human and bovine cartilage and the changes it undergoes with cartilage degeneration seen in osteoarthritis (OA) and under the influence of interleukin-1 (IL-1). Human normal and OA articular cartilage and bovine nasal cartilage cultured in the presence of IL-1 alpha were processed for histology and immunohistochemistry. ADAM-10 protein was extracted from human cartilage and analyzed by Western blotting using anti-ADAM-10 antibodies. Fluor 5 Image analyzer and Quantity One software program were applied to quantify the total amount of ADAM-10. ADAM-10 protein was detected in both human and bovine cartilage. The strongest immunostaining was found in the cytoplasm and/or cell membranes of the superficial and upper middle layer of normal adult human cartilage, in the clusters and fibrillated areas of OA cartilage, and in IL-1 alpha -stimulated bovine nasal cartilage. The distribution of ADAM-10 protein in bovine nasal cartilage was dependent on the length of exposure to IL-1 alpha and corresponded to the areas of proteoglycan depletion. By Western blotting analysis of human cartilage, ADAM-10 was primarily detected in the membrane-enriched fraction and its levels were increased in degenerated and OA cartilage compared to normal cartilage. The results of this study suggest that ADAM-10 might be an important factor associated with cartilage degenerative processes.
引用
收藏
页码:1165 / 1176
页数:12
相关论文
共 32 条
[1]  
Arner EC, 1997, J BIOL CHEM, V272, P9294
[2]   Generation and characterization of aggrecanase - A soluble, cartilage-derived aggrecan-degrading activity [J].
Arner, EC ;
Pratta, MA ;
Trzaskos, JM ;
Decicco, CP ;
Tortorella, MD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (10) :6594-6601
[3]   Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage [J].
Billinghurst, RC ;
Dahlberg, L ;
Ionescu, M ;
Reiner, A ;
Bourne, R ;
Rorabeck, C ;
Mitchell, P ;
Hambor, J ;
Diekmann, O ;
Tschesche, H ;
Chen, J ;
VanWart, H ;
Poole, AR .
JOURNAL OF CLINICAL INVESTIGATION, 1997, 99 (07) :1534-1545
[4]   A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells [J].
Black, RA ;
Rauch, CT ;
Kozlosky, CJ ;
Peschon, JJ ;
Slack, JL ;
Wolfson, MF ;
Castner, BJ ;
Stocking, KL ;
Reddy, P ;
Srinivasan, S ;
Nelson, N ;
Boiani, N ;
Schooley, KA ;
Gerhart, M ;
Davis, R ;
Fitzner, JN ;
Johnson, RS ;
Paxton, RJ ;
March, CJ ;
Cerretti, DP .
NATURE, 1997, 385 (6618) :729-733
[5]   A POTENTIAL FUSION PEPTIDE AND AN INTEGRIN LIGAND DOMAIN IN A PROTEIN ACTIVE IN SPERM-EGG FUSION [J].
BLOBEL, CP ;
WOLFSBERG, TG ;
TURCK, CW ;
MYLES, DG ;
PRIMAKOFF, P ;
WHITE, JM .
NATURE, 1992, 356 (6366) :248-252
[6]   Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and notch [J].
Blobel, CP .
CELL, 1997, 90 (04) :589-592
[7]   STRUCTURAL AND FUNCTIONAL COMPARISON OF ANCHORIN-CII (CARTILAGE ANNEXIN-V) AND MUSCLE ANNEXIN-V [J].
BOHM, BB ;
WILBRINK, B ;
KUETTNER, KE ;
MOLLENHAUER, J .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1994, 314 (01) :64-74
[8]   ADAM-10 message is expressed in human articular cartilage [J].
Chubinskaya, S ;
Cs-Szabo, G ;
Kuettner, KE .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1998, 46 (06) :723-729
[9]  
Chubinskaya S, 1999, LAB INVEST, V79, P1669
[10]  
CHUBINSKAYA S, 1999, T ORTHOP RES SOC, V24, P728