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Identification of human intervertebral disc stromelysin and its involvement in matrix degradation
Author(s) -
Liu J.,
Roughley P. J.,
Mort J. S.
Publication year - 1991
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100090413
Subject(s) - intervertebral disc , matrix metalloproteinase , cartilage , extracellular matrix , articular cartilage , matrix (chemical analysis) , matrix metalloproteinase 3 , chemistry , intervertebral disk , metalloproteinase , microbiology and biotechnology , anatomy , osteoarthritis , pathology , biology , medicine , biochemistry , lumbar , alternative medicine , chromatography
Human intervertebral disc when maintained in organ culture released a latent casein‐degrading metalloproteinase into the medium in a manner analogous to cultures of human cartilage. This enzyme was demonstrated to be immunologically identical to prostromelysin. It was also found that the amount of procollagenase secreated by both cartilage and disc cells was considerably less than that of prostromelysin. Tissue extraction confirmed that the low level of procollagenase observed was not due to retention of the enzyme within the tissue. Human intervertebral disc link proteins were found to possess the same N‐termini as those of their counterparts in human articular articular cartilage, whee it appears that stromelysin is responsible for generating molecular heterogeneity. These results suggest that intervertebral disc cells are capable of secreting prostromelysin, which can become activated within the extracellular matrix and hence contribute to the age‐related and degenerative changes in the disc.