CHARACTERIZATION OF A METALLOPROTEINASE - A LATE-STAGE SPECIFIC GELATINASE ACTIVITY IN THE SEA-URCHIN EMBRYO

We have partially purified and characterized an 87 kDa gelatinase acti vity expressed in later stage sea urchin embryos. Cleavage activity wa s specific for gelatin and no cleavage of sea urchin peristome type I collagen, bovine serum albumin or casein was detected. Magnesium and Z n2+ inhibited the gelatinase and Ca2+ protected against inhibition. Et hylenediamine tetracetic acid, ethylenebisoxyethylenenitriol tetraacet ic acid and 1,10-phenanthroline were inhibitory, suggesting that the g elatinase is a Ca2+- and Zn2+-dependent metalloproteinase. No inhibiti on was detected with serine or cysteine protease inhibitors and the ve rtebrate matrix metalloproteinase (MMP) inhibitor, Batimastat, was als o ineffective. The vertebrate MMP activator p-aminophenylmercuric acet ate was without effect. These results allow us to identify both simila rities and differences between echinoderm and vertebrate gelatinases. (C) 1997 Wiley-Liss, Inc.