The International Journal of Developmental Biology

Int. J. Dev. Biol. 34: 267 - 274 (1990)

Vol 34, Issue 2

The oocyte lamin persists as a single major component of the nuclear lamina during embryonic development of the surf clam

Published: 1 June 1990

G Dessev and R Goldman

Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.

Abstract

Nuclei and nuclear lamina-enriched fractions, isolated from 1 to 5-day-old embryos of the surf clam, Spisula solidissima, contain only one major lamin protein, which appears to be identical to the oocyte lamin (L67), as judged by 2D IEF/SDS PAGE, reactivity with a polyclonal antibody directed against L67 and 125I tryptic peptide mapping. The same protein is also present in liver, muscle, nerve and testis from adult animals. No proteins--recognized by several poly- and monoclonal antibodies, specific for somatic lamins from different vertebrate species or the oocyte lamin LIII of Xenopus- have been detected in nuclei or NL-enriched preparations, isolated from embryos or adult tissues. Synthesis of L67 is detectable in embryos 2h after fertilization; it reaches a maximum in 6h-old embryos and gradually declines thereafter. These results argue that the composition of the NL bears no obvious relationship to the structural and functional changes that take place during the embryonic development of this invertebrate.

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