Externalization of calpain (calcium-dependent neutral cysteine proteinase) in human arthritic cartilage.

Abstract:

OBJECTIVE:Calcium-dependent neutral cysteine proteinase (calpain) was originally referred to as an intracellular enzyme. However, recently it has come to be considered as an extracellular matrix proteinase, as well having a degrading effect on cartilage proteoglycan. In the present study we sought to determine whether human articular cartilage chondrocytes themselves have the capability to produce and secrete this interesting proteinase. METHODS:Human articular cartilage tissue cultures from osteoarthritic (11 specimens from 7 patients) and rheumatoid arthritic (3 specimens from 2 patients) knee joints were established, and the m-calpain released into the culture medium was concentrated and detected by immunoelectrophoretic blotting. The presence of m-calpain in the arthritic cartilage was also examined by immunohistochemistry before and after culturing. RESULTS:M-calpain was detectable in all of the cartilage tissue culture supernatants (conditioned medium) by western blotting. Positive intracellular immunostaining of m-calpain in chondrocytes was observed in all samples. Furthermore, m-calpain was found to be present in the matrix and on the articular surface of the cartilage in half of the specimens. CONCLUSION:The findings of our experiment suggest that cartilage chondrocytes may actively take part in m-calpain production and that they may have the capacity to release it into the extracellular matrices.

journal_name

Clin Exp Rheumatol

authors

Szomor Z,Shimizu K,Yamamoto S,Yasuda T,Ishikawa H,Nakamura T

keywords:

subject

Has Abstract

pub_date

1999-09-01 00:00:00

pages

569-74

issue

5

eissn

0392-856X

issn

1593-098X

journal_volume

17

pub_type

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