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Proteolytic processing of a sea urchin, ECM‐localized protein into lower mol mass species possessing collagen‐cleavage activity
Author(s) -
Robinson John J.
Publication year - 2006
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/jcb.20975
Subject(s) - sea urchin , cleavage (geology) , gelatin , protease , benzamidine , chemistry , extracellular matrix , biochemistry , microbiology and biotechnology , serine , biology , enzyme , paleontology , fracture (geology)
The hyaline layer is an apically located extraembryonic matrix, which blankets the sea urchin embryo. Using gelatin substrate gel zymography, we have identified a number of gelatin‐cleaving activities within the hyaline layer and defined a precursor–product processing pathway which leads to the appearance of 40‐ and 38‐kDa activities coincident with the loss of a 50‐kDa species. Proteolytic processing of the precursor required the presence of both CaCl 2 and NaCl at concentrations similar to those found in sea water. The cleavage activities utilized both sea urchin and rat tail tendon gelatins as substrates but demonstrated a species‐specific cleavage activity towards sea urchin collagen. The gelatin‐cleaving activities were refractory to inhibition by 1, 10‐phenanthroline but were inhibited by benzamidine. This latter result defines the serine protease nature of the cleavage activities. Both the 40‐ and 38‐kDa activities were found to comigrate with gelatin‐cleaving activities present in the sea urchin embryo. J. Cell. Biochem. 99: 816–823, 2006. © 2006 Wiley‐Liss, Inc.