de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Cloning of a novel phospholipase C-delta isoform from Pacific purple sea urchin (Strongylocentrotus purpuratus) gametes and its expression during early embryonic development

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50470

Poustka,  Albert J.
Evolution and Development (Albert Poustka), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Coward, K., Owen, H., Poustka, A. J., Hibbitt, O., Tunwell, R., Kubota, H., et al. (2004). Cloning of a novel phospholipase C-delta isoform from Pacific purple sea urchin (Strongylocentrotus purpuratus) gametes and its expression during early embryonic development. Biochemical and Biophysical Research Communications, 313(4), 894-901. doi:10.1016/j.bbrc.2003.12.029.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-88F6-5
Abstract
Calcium (Ca2+) is a ubiquitous intracellular messenger, controlling a diverse range of cellular processes, including fertilization and development of the embryo. One of the key mechanisms involved in triggering intracellular calcium release is the generation of the second messenger inositol-1,4,5-phosphate (IP3) by the phospholipase C (PLC) class of enzymes. Although five distinct forms of PLC have been identified in mammals (, , , , and ), only one, PLC, has thus far been detected in echinoderms. In the present study, we describe the isolation of a cDNA encoding a novel PLC isoform of the delta () subclass, PLC-su, from the egg of the Pacific purple sea urchin Strongylocentrotus purpuratus. We also demonstrate the presence of this PLC within the sperm and in the early embryo. The PLC-su cDNA (2.44 kb) encodes a 742 amino acid polypeptide with an open reading frame of 84.6 kDa and a pI of 6.04. All of the characteristic domains found in mammalian PLC isoforms (PH domain, EF hands, an X–Y catalytic region, and a C2 domain) are present in PLC-su. A homology search revealed that PLC-su shares most sequence identity with bovine PLC2 (39%). We present evidence that PLC-su is expressed in unfertilized eggs, fertilized eggs, and in the early embryo. In addition to Northern and polymerase chain reaction (PCR) analyses, in situ hybridization experiments further demonstrated that the embryonic regions within which the PLC-su transcript can be detected during early embryonic development are associated with the highest levels of proliferative activity, suggesting a possible involvement with metabolism or cell cycle regulation.