Abstract:
: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 Zn2+ inhibited the gelatinase and Ca2+ 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.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Robinson JJsubject
Has Abstractpub_date
1997-09-01 00:00:00pages
337-45issue
3eissn
0730-2312issn
1097-4644pii
10.1002/(SICI)1097-4644(19970901)66:3<337::AID-JCBjournal_volume
66pub_type
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