We have purified and characterized a collagenase/gelatinase activity expressed during sea urchin embryonic development. The native molecular mass was determined to be 160 kDa, while gelatin substrate gel zymography revealed an active species of 41 kDa, suggesting that the native enzyme is a tetramer
A new extracellular matrix protein of the sea urchin embryo with properties of a substrate adhesion molecule
โ Scribed by Matranga, Valeria ;Ferrol, Daniela ;Zito, Francesca ;Cervello, Melchiorre ;Nakano, Eizo
- Publisher
- Springer-Verlag
- Year
- 1992
- Tongue
- English
- Weight
- 617 KB
- Volume
- 201
- Category
- Article
- ISSN
- 1432-041X
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โฆ Synopsis
A new embryonic extracellular matrix protein has been purified from eggs of the sea urchin Paracentrotus lividus. The molecule is a 210 kD dimer consisting of two 105 kD subunits that are held together by S-S bridges. In the unfertilized egg, the protein is found within granules uniformly distributed throughout the cytoplasm. After the egg is fertilized, the antigen is polarized to the apical surface of ectodermal and endodermal cells during all of the developmental stages examined, until the pluteus larva is formed. The protein promotes the adhesion of blastula cells to the substrate and is antigenically distinct from echinonectin, a well characterized substrate adhesion molecule. This report adds a new candidate to the list of known extracellular matrix molecules for the regulation of differentiation and morphogenesis in the sea urchin embryo.
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