PMID- 1602738
OWN - NLM
STAT- MEDLINE
DCOM- 19920710
LR  - 20141120
IS  - 0023-6837 (Print)
IS  - 0023-6837 (Linking)
VI  - 66
IP  - 6
DP  - 1992 Jun
TI  - Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic 
      cartilage and synovium.
PG  - 680-90
AB  - Degradation of proteoglycans is an initial change in osteoarthritic cartilage. 
      Matrix metalloproteinase-3 (MMP-3; stromelysin) capable of degrading cartilage 
      proteoglycans and type IX collagen was immunolocalized in osteoarthritic and 
      normal cartilage. Immunohistochemical studies showed MMP-3 in chondrocytes of the 
      superficial and transition zones in approximately 90% of osteoarthritic cartilage 
      (60 of 67 samples) and in 31% of those of the superficial zone in some normal 
      cartilage (4 of 13 samples). MMP-3 staining correlated directly with the 
      histological histochemical scores of Mankin and with proteoglycan depletion, up 
      to a certain grade of severity. Chondrocytes in the deep radial zone, clusters, 
      and osteophytes were immunostained only when proteoglycan depletion and fissures 
      affected them. Culture media from osteoarthritic cartilage contained 
      significantly higher levels of metalloproteinase activity that was identified as 
      MMP-3 by immunoblotting and lower amounts of tissue inhibitor of 
      metalloproteinases compared with those in the control samples. MMP-3 was also 
      immunolocalized in the lining cells of most osteoarthritic synovium (20 of 23 
      specimens, 87%) with a direct correlation with scores of inflammatory cell 
      infiltration in the synovium, but it was not detected in the normal synovium. 
      Light and electron microscopic studies demonstrated that MMP-3 digests 
      proteoglycan aggregates in human articular cartilage. Treatment of normal and 
      osteoarthritic cartilage slices with tumor necrosis factor-alpha and/or 
      interleukin-1 alpha increased the number of MMP-3-immunoreactive chondrocytes and 
      the intensity of the staining. These data suggest that MMP-3 produced by the 
      chondrocytes and synovial lining cells under stimulation with these cytokines may 
      be important in proteoglycan degradation in human ostoearthritic cartilage.
FAU - Okada, Y
AU  - Okada Y
AD  - Department of Pathology, and Orthopedic Surgery, School of Medicine, Kanazawa 
      University, Japan.
FAU - Shinmei, M
AU  - Shinmei M
FAU - Tanaka, O
AU  - Tanaka O
FAU - Naka, K
AU  - Naka K
FAU - Kimura, A
AU  - Kimura A
FAU - Nakanishi, I
AU  - Nakanishi I
FAU - Bayliss, M T
AU  - Bayliss MT
FAU - Iwata, K
AU  - Iwata K
FAU - Nagase, H
AU  - Nagase H
LA  - eng
GR  - AR 39189/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Lab Invest
JT  - Laboratory investigation; a journal of technical methods and pathology
JID - 0376617
RN  - 0 (Glycoproteins)
RN  - 0 (Interleukin-1)
RN  - 0 (Proteoglycans)
RN  - 0 (Tissue Inhibitor of Metalloproteinases)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.17 (Matrix Metalloproteinase 3)
SB  - IM
MH  - Cartilage Diseases/*enzymology/metabolism
MH  - Glycoproteins/analysis
MH  - Humans
MH  - Immunoblotting
MH  - Immunoenzyme Techniques
MH  - In Vitro Techniques
MH  - Interleukin-1/pharmacology
MH  - Matrix Metalloproteinase 3
MH  - Metalloendopeptidases/drug effects/*metabolism
MH  - Osteoarthritis/*enzymology/metabolism
MH  - Proteoglycans/metabolism
MH  - Synovial Membrane/*enzymology/metabolism
MH  - Tissue Inhibitor of Metalloproteinases
MH  - Tumor Necrosis Factor-alpha/pharmacology
EDAT- 1992/06/01 00:00
MHDA- 1992/06/01 00:01
CRDT- 1992/06/01 00:00
PHST- 1992/06/01 00:00 [pubmed]
PHST- 1992/06/01 00:01 [medline]
PHST- 1992/06/01 00:00 [entrez]
PST - ppublish
SO  - Lab Invest. 1992 Jun;66(6):680-90.