Differential regulation of the levels of three gap junction mRNAs in Xenopus embryos.
Open Access
- 1 March 1990
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 110 (3) , 597-605
- https://doi.org/10.1083/jcb.110.3.597
Abstract
Xenopus mRNas that potentially encode gap junction proteins in the oocyte and early embryo have been identified by stringency screening of cDNA libraries with cloned mammalian gap junction cDNAs. The levels of these mRNAs show strikingly different temporal regulation and tissue distribution. Using a nomenclature designed to stress important structural similarities of distinct gap junction gene products, the deduced polypeptides have been designated the Xenopus .alpha.1 and .alpha.2 gap junction proteins. The .alpha.2 gap junction mRNA is a maternal transcript that disappears by the late gastrula stage. It is not detected in any organ of the adult except the ovary, and resides primarily, if not exclusively, in the oocytes and early embryos. The .alpha.1 gap junction mRNA appears during organogenesis, and is detected in RNA from a wide variety of organs. It is also found in full-grown oocytes, but is rapidly degraded upon oocyte maturation, both in vivo and in vitro. The .alpha.1 and .alpha.2 mRNAs encode proteins with different degrees of amino acid sequence similarity to the predominant gap junction subunit of the mammalian heart (connexin 43). Together with our earlier report of a mid-embryonic (.beta.1) gap junction mRNA, the results suggest that intercellular communication during oocyte growth and postfertilization development is a complex phenomenon involving the coordinated regulation of several genes.This publication has 41 references indexed in Scilit:
- Connexin43: a protein from rat heart homologous to a gap junction protein from liver.The Journal of cell biology, 1987
- Gap junctional communication and compaction during preimplantation stages of mouse developmentCell, 1987
- Expression of Functional Cell-Cell Channels from Cloned Rat Liver Gap Junction Complementary DNAScience, 1987
- Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures.Journal of Biological Chemistry, 1987
- Functional assembly of gap junction conductance in lipid bilayers: Demonstration that the major 27 kd protein forms the junctional channelCell, 1987
- Molecular cloning of cDNA for rat liver gap junction protein.The Journal of cell biology, 1986
- Cell interactions and the control of gene activity during early development of Xenopus laevisDevelopmental Biology, 1986
- A dramatic loss of cumulus cell gap junctions is correlated with germinal vesicle breakdown in rat oocytesDevelopmental Biology, 1986
- A conformational preference parameter to predict helices in integral membrane proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Communication between Cells of Different TypeNature, 1971