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Nectins in sea urchin eggs and embryos

Published online by Cambridge University Press:  11 May 2009

Yukio Yokota ,
Valeria Matranga ,
Francesca Zito ,
Melchiorre Cervello  and
Eizo Nakano
Yukio Yokota
Affiliation:
Biological Laboratory, Aichi Prefectural University, Mizuho, Nagoya 467, Japan.
Valeria Matranga
Affiliation:
Istituto di Biologia dello Sviluppo, Consiglio Nazionale delle Ricerche, Via Archirafi 20, 90123 Palermo, Italy.
Francesca Zito
Affiliation:
Istituto di Biologia dello Sviluppo, Consiglio Nazionale delle Ricerche, Via Archirafi 20, 90123 Palermo, Italy.
Melchiorre Cervello
Affiliation:
Istituto di Biologia dello Sviluppo, Consiglio Nazionale delle Ricerche, Via Archirafi 20, 90123 Palermo, Italy.
Eizo Nakano
Affiliation:
Nagoya University, Chikusa, Nagoya 464, Japan
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Extract

The extracellular matrix of the sea urchin involves a protein with a molecular weight of 180 kDa (sea urchin fibronectin), which corresponds to mammalian fibronectin, and a nectin specific to Echinoidea with a molecular weight of 105–115 kDa (sea urchin nectin). Sea urchin fibronectin and sea urchin nectin have cell adhesion protein properties. They are, however, different from each other in biochemical properties, biological functions and intraembryonic distribution. Sea urchin fibronectin isolated from the sea urchin ovary accelerates scattering of micromere-derived cells and promotes spicule formation of micromeres in vitro. Sea urchin nectins identified so far in Paracentrotus lividus (Lamarck), Temnopleurus hardwicki (Gray) and Pseudocentrotus depressus (A. Agassiz) are presumably homologous molecules displayed in different species. They seem to be secreted into the hyaline layer as its constituents, and to play some role in morphogenesis of the embryo.

Type
Research Article
Information
Journal of the Marine Biological Association of the United Kingdom , Volume 74 , Issue 1 , February 1994 , pp. 27 - 34
Copyright
Copyright © Marine Biological Association of the United Kingdom 1994

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