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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Phospholipase C, delta 4

PLCdelta4, Phospholipase Cdelta4, PLCdelta2
This gene encodes a member of the delta class of phospholipase C enzymes. Phospholipase C enzymes play a critical role in many cellular processes by hydrolyzing phosphatidylinositol 4,5-bisphosphate into two intracellular second messengers, inositol 1,4,5-trisphosphate and diacylglycerol. Expression of this gene may be a marker for cancer. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: PLC, PLCgamma, delta4, ACID, PLCdelta1
Papers on PLCdelta4
Nuclear PLCs affect insulin secretion by targeting PPARγ in pancreatic β cells.
Cocco et al., Bologna, Italy. In Faseb J, 2012
These findings highlight a novel pathway by which nuclear PLCs affect insulin secretion and identify PPARgamma as a novel molecular target of nuclear PLCs.
Physiological functions of phospholipase C delta-type.
Nakamura et al., Hachiōji, Japan. In Adv Enzyme Regul, 2007
PLCd4 is required for the acrosome reaction in fertilization.
Identification and analysis of the promoter region of the human PLC-delta4 gene.
Rha et al., Seoul, South Korea. In Mol Biol Rep, 2007
Serial deletion analysis identified the core PLC-delta4 promoter region as being between -402 and -67, in which an E-box and an AP-1 binding site played important roles in the promoter activity.
Disruption of phospholipase Cdelta4 gene modulates the liver regeneration in cooperation with nuclear protein kinase C.
Tamiya-Koizumi et al., Nagoya, Japan. In J Biochem, 2006
It is concluded that PLC delta4 regulates the liver regeneration in cooperation with nuclear PKC alpha and epsilon
Phospholipase C isozymes are differentially distributed in the rat adrenal medulla.
Bunn et al., Dunedin, New Zealand. In Neurosci Lett, 2006
PLCdelta1 and PLCdelta2 had quite distinct distributions, with the former selectively localized to an endothelial cell population surrounding the chromaffin cells.
Phospholipase Cdelta4 associates with glutamate receptor interacting protein 1 in testis.
Fukami et al., Hachiōji, Japan. In J Biochem, 2005
Here we focused on the function of the C2 domain of PLCdelta4 and report that glutamate receptor-interacting protein1 (GRIP1) was identified as a binding protein of the PLCdelta4-C2 domain on yeast two-hybrid screening.
Phospholipase C delta-type consists of three isozymes: bovine PLCdelta2 is a homologue of human/mouse PLCdelta4.
Fukami et al., Hachiōji, Japan. In Biochem Biophys Res Commun, 2004
Here we report that a screening for mouse PLCdelta2 from a BAC library with primers that amplify a specific region of bovine PLCdelta2 resulted in isolation of one clone containing the mouse PLCdelta4 gene.
The pleckstrin homology domain of phosphoinositide-specific phospholipase Cdelta4 is not a critical determinant of the membrane localization of the enzyme.
Balla et al., Bethesda, United States. In J Biol Chem, 2004
PLCdelta(1) and PLCdelta(4) are probably differentially regulated in distinct cellular compartments by PI(4,5)P(2) and the PH domain of PLCdelta(4) does not act as a localization signal
Phospholipase C delta-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells.
Singer et al., Seattle, United States. In Mol Cancer, 2004
BACKGROUND: The expression of the rodent phosphoinositide-specific phospholipase C delta-4 (PLCdelta4) has been found to be elevated upon mitogenic stimulation and expression analysis have linked the upregulation of PLCdelta4 expression with rapid proliferation in certain rat transformed cell lines.
Cloning of a novel phospholipase C-delta isoform from pacific purple sea urchin (Strongylocentrotus purpuratus) gametes and its expression during early embryonic development.
Parrington et al., Oxford, United Kingdom. In Biochem Biophys Res Commun, 2004
A homology search revealed that PLC-deltasu shares most sequence identity with bovine PLCdelta2 (39%).
Inositol-specific phospholipase C in low and fast proliferating hepatoma cell lines.
Guidotti et al., Bologna, Italy. In Int J Oncol, 2003
The PLC activity is increased in fast proliferating cells, in which PLC delta1 and to a greater extent PLC delta4 are more expressed at cytosolic level, suggesting an involvement of PI specific PLCs in the progression of cell cycle and in the control of cell proliferation and possibly of neoplastic cell growth.
Phospholipase Cdelta4 is required for Ca2+ mobilization essential for acrosome reaction in sperm.
Takenawa et al., Tokyo, Japan. In J Cell Biol, 2003
We previously reported that PLCdelta4 is involved in the ZP-induced acrosome reaction in mouse sperm.
Phospholipase C isoforms in mammalian spermatozoa: potential components of the sperm factor that causes Ca2+ release in eggs.
Swann et al., London, United Kingdom. In Reproduction, 2002
In addition to our previous work on recombinant PLCs, it was also shown that PLCdelta3, PLCdelta4 and its splice variant PLCdelta4 Alt1 fail to cause Ca2+ release.
Requirement of phospholipase Cdelta4 for the zona pellucida-induced acrosome reaction.
Takenawa et al., Tokyo, Japan. In Science, 2001
Several phospholipase C (PLC) isoforms have been found in male and female mammalian gametes, and splicing isoforms of PLCdelta4 are predominantly expressed in testis.
Sperm factor induces intracellular free calcium oscillations by stimulating the phosphoinositide pathway.
Fissore et al., Amherst Center, United States. In Biol Reprod, 2001
Using ammonium sulfate precipitation, chromatographic fractionation, and Western blotting, we determined whether PLCgamma1, PLCgamma2, or PLCdelta4 and/or its splice variants, which are present in sperm and testis, are responsible for the Ca(2+) activity in the extracts.
Insulin secretion, inositol phosphate levels, and phospholipase C isozymes in rodent pancreatic islets.
Zawalich et al., New Haven, United States. In Metabolism, 2000
PLCbeta4 or PLCdelta2 could not be identified in either species.
Growth factor-induced promoter activation of murine phospholipase C delta4 gene.
Takenawa et al., Tokyo, Japan. In Eur J Biochem, 2000
Phospholipase C delta4 (PLCdelta4) is one of the delta-type PLC isozymes, the expression of which is induced in nuclei by treatment with serum and also in some cancer cells.
Changes in the expression of lipid-mediated signal-transducing enzymes in the rat liver after partial hepatectomy.
Nozawa et al., Gifu, Japan. In Surg Today, 1999
The expression of PLCdelta4 peaked at 12 h, but no significant changes in the expression of PLCbeta1 and PLCgamma1 were seen after PH.
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