Immunolocalization of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human chondrosarcomas

A. Kawashima, Y. Okada, I. Nakanishi, Y. Ueda, K. Iwata, A. Roessner

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

We have immunohistochemically examined the localization of matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs) in human chondrosarcomas (CHS) (23 cases) and benign chondroid lesions (BCL) (16 cases of osteochondromas and 11 cases of enchondromas). In CHS, all the MMPs and TIMPs examined were positive. Among them, MMP-1 was immunolocalized in more than 90% of both CHS and BCL, but positive score of MMP-1 was significantly higher in CHS than that in BCL (p < 0.01). Compared with BCL, CHS expressed MMP-3 at a low level, and more often positive in MMP-9. It is possible that chondrosarcoma might have a tendency to lose the ability to secrete MMP-3, which is a metalloproteinase that can degrade cartilage proteoglycans and is related to normal cartilage turnover. MMP-2, TIMP-1 and TIMP-2 were immunolocalized in more than 70% of the cases of both BCL and CHS, but the positive scores of these were not statistically different between the two groups. Interestingly, in several cases of CHS, both MMP-1 and MMP-9 immunostains were observed preferentially within the cells at the marginal areas of cartilaginous lobules. These findings suggest that increased expression of MMP-1 and MMP-9 and decrease in MMP-3 expression are associated with the malignant phenotype of the cartilaginour tumors.

Original languageEnglish
Pages (from-to)129-137
Number of pages9
JournalGeneral and Diagnostic Pathology
Volume142
Issue number3-4
Publication statusPublished - 1997
Externally publishedYes

Keywords

  • Chondrosarcoma
  • Enchondroma
  • Immunohistochemistry
  • Matrix metalloproteinase
  • Osteochondroma

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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