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Two major tenascin-C (TN-C) isoforms are generated by the
alternative splicing of the pre-mRNA. The large isoform contains seven
extra type three repeats that, by contrast, are omitted in the small
TN-C isoform. The large TN-C isoform is mainly expressed at the onset
of cellular processes that entail active cell migration, proliferation,
or tissue remodeling such as occur in neoplasia, wound healing, and
during development. Thus, the large TN-C isoform seems to be a specific
component of the provisional extracellular matrix. Here we have studied
the degradation of the large and small TN-C isoforms by matrix
metalloproteinases (MMPs) 2, 3, 7, and 9. Among these proteolytic
enzymes only MMP-7 can degrade the small TN-C isoform removing the
NH
Volume 270,
Number 15,
Issue of April 14, pp. 8650-8654, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-terminal knob. The large TN-C isoform shows the same
MMP-7-sensitive site adjacent to the NH-terminal sequence,
but is further degraded in the splicing area where three
fibronectin-like type III repeats are completely digested. Moreover,
the large TN-C isoform is degraded by MMP-2 and MMP-3 which completely
digest a single type III repeat inside the splicing area. By contrast,
the large TN-C isoform is resistant to MMP-9 digestion. The results
show that the presence of the spliced sequence introduces new
protease-sensitive sites in the large TN-C isoform.
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