Biochemical and immunological relationships among fibronectin-like proteins from different sea urchin species
✍ Scribed by Matranga, V. ;Zito, F. ;Tesoro, V. ;Yokota, Y. ;Nakano, E.
- Book ID
- 104739003
- Publisher
- Springer-Verlag
- Year
- 1995
- Tongue
- English
- Weight
- 582 KB
- Volume
- 204-204
- Category
- Article
- ISSN
- 1432-041X
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✦ Synopsis
Fibronectin-like proteins were purified from ovaries of the sea urchin species, Paracentrotus lividus (P1), Sphaerechinus granularis (Sg), Arbacia lixula (A1), Pseudocentrotus depressus (Pd), and Anthocidaris crassispina (Ac), by gelatin-Sepharose affinity chromatography. The major component had a molecular mass of 180 kDa and was eluted by 1 M NaCI or 8 M urea, depending on the species used. By substrate adhesion assay, we tested the biological activity of the 180 kDa protein purified from Paracentrotus lividus (PI-180K) and showed that it promotes the adhesion of homologous embryonic cells to the substrate. An antiserum, developed against Temnopleurus hardwickii fibronectin-like protein (Th-180K), was used in Western blots of the proteins purified from the five species. The antibody cross-reacted with PI-180K, Pd-180K and Ac-180K. A peptide map of PI-180K, obtained by V8 protease partial digestion, was compared with those obtained from the other four proteins and showed an homology between 40 and 56%. This report confirms that fibronectin-like proteins can be purified from sea urchins on the basis of their binding to gelatin-Sepharose; the proteins differ for their binding affinity to gelatin and share different epitopes, suggesting that they are members of a sea urchin fibronectin super family.