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Characterization of a metalloproteinase: A late stage specific gelatinase activity in the sea urchin embryo
Author(s) -
Robinson John J.
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970901)66:3<337::aid-jcb6>3.0.co;2-q
Subject(s) - gelatinase , sea urchin , metalloproteinase , embryo , microbiology and biotechnology , chemistry , biology , matrix metalloproteinase , biochemistry
We have partially purified and characterized an 87 kDa gelatinase activity expressed in later stage sea urchin embryos. Cleavage activity was specific for gelatin and no cleavage of sea urchin peristome type I collagen, bovine serum albumin or casein was detected. Magnesium and Zn 2+ inhibited the gelatinase and Ca 2+ protected against inhibition. Ethylenediamine tetracetic acid, ethylenebisoxyethylenenitriol tetraacetic acid and 1,10‐phenanthroline were inhibitory, suggesting that the gelatinase is a Ca 2+ ‐ and Zn 2+ ‐dependent metalloproteinase. No inhibition was detected with serine or cysteine protease inhibitors and the vertebrate matrix metalloproteinase (MMP) inhibitor, Batimastat, was also ineffective. The vertebrate MMP activator p‐aminophenylmercuric acetate was without effect. These results allow us to identify both similarities and differences between echinoderm and vertebrate gelatinases. J. Cell. Biochem. 66: 337–345, 1997. © 1997 Wiley‐Liss, Inc.