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J. Biol. Chem., Vol. 268, Issue 21, 15435-15441, Jul, 1993
G Murphy, JP Segain, M O'Shea, M Cockett, C Ioannou, O Lefebvre, P Chambon and P Basset
The putative matrix metalloproteinase mouse stromelysin-3 was expressed
from Escherichia coli and from a mouse myeloma cell line. In the former
case a single major protein of 58-kDa was detectable by immunoblotting, but
no proteolytic activity could be elicited by zymography or trypsin or
organomercurial treatment as would be expected for a typical matrix
metalloproteinase. In the latter case immunodetectable proteins of 55- 58
and 27-28-kDa were produced. The effect of trypsin or organomercurial
treatment of the 55-58-kDa forms was to generate a 51- kDa form and lower
molecular mass fragments. Upon zymographic analysis only the 27-28-kDa
forms showed caseinolytic activity. N-terminal sequencing and
immunoblotting analysis with antibodies specific to distinct domains of
stromelysin-3 indicated that the 27-28-Da stromelysin-3 forms had lost the
predicted propeptide and the majority of the C-terminal domain. The
purified 28-kDa form of stromelysin-3 could weakly degrade a number of
extracellular matrix proteins and was inhibited by TIMP. However, the
evidence that mature full-length stromelysin-3 is a metalloproteinase could
not be substantiated and the precise role of this protein in vivo remains
to be elucidated. By partial analogy with interstitial collagenase, one
hypothesis is that stromelysin-3 with an intact C-terminal domain has
specific properties for an as yet undefined substrate.
The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase
Strangeways Research Laboratory, Cambridge, United Kingdom.
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