Chondrocyte matrix metalloproteinase-8 - Human articular chondrocytes express neutrophil collagenase

被引:163
作者
Cole, AA
Chubinskaya, S
Schumacher, B
Huch, K
CsSzabo, G
Yao, J
Mikecz, K
Hasty, KA
Kuettner, KE
机构
[1] RUSH PRESBYTERIAN ST LUKES MED CTR, DEPT ORTHOPED SURG, RUSH MED COLL, CHICAGO, IL 60612 USA
[2] UNIV TENNESSEE, CTR HLTH SCI, DEPT ANAT & NEUROBIOL, MEMPHIS, TN 38163 USA
[3] VET ADM MED CTR, MEMPHIS, TN 38104 USA
关键词
D O I
10.1074/jbc.271.18.11023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This study confirms that normal human articular chondrocytes express neutrophil collagenase or matrix metalloproteinase-8 (MMP-8), a gene product previously thought to be expressed exclusively by neutrophil leukocytes. Both MMP-8 protein and mRNA were present in articular cartilages collected from normal human donors. Cartilage extracts were assayed by immunoblotting and by analysis of enzymatic activity on gelatin-substrate gels. Latent MMP-8 extracted from cartilage has a molecular mass of 55 kDa; active MMP-8 was identified at 46 and 42 kDa. In the absence of a reducing agent, MMP-8 migrated in a high molecular mass complex above 200 kDa. Northern blotting results demonstrated the expression of MMP-8 in chondrocytes, which could be up-regulated by stimulation with interleukin 1 beta. In addition, reverse transcription-polymerase chain reaction using nested primers and in situ hybridization revealed the presence of MMP-8 mRNA in chondrocytes. The presence of both MMP-8 protein and message in cartilage supports the concept that neutrophil collagenase could be the enzyme described as ''aggrecanase.''
引用
收藏
页码:11023 / 11026
页数:4
相关论文
共 32 条
[1]   DIFFERENCES BETWEEN SUB-POPULATIONS OF CULTURED BOVINE ARTICULAR CHONDROCYTES .1. MORPHOLOGY AND CARTILAGE MATRIX PRODUCTION [J].
AYDELOTTE, MB ;
KUETTNER, KE .
CONNECTIVE TISSUE RESEARCH, 1988, 18 (03) :205-222
[2]  
BOYUM A, 1968, SCAND J CLIN LAB INV, VS 21, P77
[3]  
BURRIS TS, 1995, T ORTHOP RES SOC, V20, P335
[4]   SINGLE-STEP METHOD OF RNA ISOLATION BY ACID GUANIDINIUM THIOCYANATE PHENOL CHLOROFORM EXTRACTION [J].
CHOMCZYNSKI, P ;
SACCHI, N .
ANALYTICAL BIOCHEMISTRY, 1987, 162 (01) :156-159
[5]  
CHUBINSKAYA S, 1995, T ORTHOP RES SOC, V20, P342
[6]   TYPE-X COLLAGEN DEGRADATION IN LONG-TERM SERUM-FREE CULTURE OF THE EMBRYONIC CHICK TIBIA FOLLOWING PRODUCTION OF ACTIVE COLLAGENASE AND GELATINASE [J].
COLE, AA ;
BOYD, T ;
LUCHENE, L ;
KUETTNER, KE ;
SCHMID, TM .
DEVELOPMENTAL BIOLOGY, 1993, 159 (02) :528-534
[7]   MMP-8 (neutrophil collagenase) mRNA and aggrecanase cleavage products are present in normal and osteoarthritic human articular cartilage [J].
Cole, AA ;
Kuettner, KE .
ACTA ORTHOPAEDICA SCANDINAVICA, 1995, 66 :98-102
[8]   ASSOCIATION OF COLLAGENASE AND TISSUE INHIBITOR OF METALLOPROTEINASES (TIMP) WITH HYPERTROPHIC CELL ENLARGEMENT IN THE GROWTH PLATE [J].
DEAN, DD ;
MUNIZ, OE ;
HOWELL, DS .
MATRIX, 1989, 9 (05) :366-375
[9]   A TECHNIQUE FOR RADIOLABELING DNA RESTRICTION ENDONUCLEASE FRAGMENTS TO HIGH SPECIFIC ACTIVITY [J].
FEINBERG, AP ;
VOGELSTEIN, B .
ANALYTICAL BIOCHEMISTRY, 1983, 132 (01) :6-13
[10]   NEUTROPHIL COLLAGENASE (MMP-8) CLEAVES AT THE AGGRECANASE SITE E(373)-A(374) IN THE INTERGLOBULAR DOMAIN OF CARTILAGE AGGRECAN [J].
FOSANG, AJ ;
LAST, K ;
NEAME, PJ ;
MURPHY, G ;
KNAUPER, V ;
TSCHESCHE, H ;
HUGHES, CE ;
CATERSON, B ;
HARDINGHAM, TE .
BIOCHEMICAL JOURNAL, 1994, 304 :347-351