BIOMAT Database Logo BIOMAT Database Logo

Addition of phosphatidylcholine-phospholipase C induces cellular redistribution and phosphorylation of protein kinase C zeta in C 6 glial cells. 1996

I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Departamento de Bioquímica y Biología Molecular I, Facultad de Químicas, Universidad Complutense, Madrid, Spain.

Phosphatidylcholine breakdown has been shown to play a critical role in signal transduction involving generation of a number of second messengers [Exton, J.H., Biochim. Biophys. Acta, 1212 (1994) 26-42]. In the present report we demonstrate by immunofluorescence that short-treatment of C 6 glial cells with phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC), changes the intracellular localization of protein kinase C (PKC) zeta from the cytoplasm to a perinuclear region. Western blot analysis also showed a redistribution of PKC zeta after incubation of cells with PC-PLC. To test whether these changes were accompanied by an activation of the enzyme, we measured the extent of phosphorylation of PKC zeta by immunoprecipitation from 32P-labelled cells. Short-treatment with PC-PLC resulted in enhanced phosphorylation of the higher Mr PKC zeta in C 6 glial cells.

UI MeSH Term Description Entries
D009457 Neuroglia The non-neuronal cells of the nervous system. They not only provide physical support, but also respond to injury, regulate the ionic and chemical composition of the extracellular milieu, participate in the BLOOD-BRAIN BARRIER and BLOOD-RETINAL BARRIER, form the myelin insulation of nervous pathways, guide neuronal migration during development, and exchange metabolites with neurons. Neuroglia have high-affinity transmitter uptake systems, voltage-dependent and transmitter-gated ion channels, and can release transmitters, but their role in signaling (as in many other functions) is unclear. Bergmann Glia,Bergmann Glia Cells,Bergmann Glial Cells,Glia,Glia Cells,Satellite Glia,Satellite Glia Cells,Satellite Glial Cells,Glial Cells,Neuroglial Cells,Bergmann Glia Cell,Bergmann Glial Cell,Cell, Bergmann Glia,Cell, Bergmann Glial,Cell, Glia,Cell, Glial,Cell, Neuroglial,Cell, Satellite Glia,Cell, Satellite Glial,Glia Cell,Glia Cell, Bergmann,Glia Cell, Satellite,Glia, Bergmann,Glia, Satellite,Glial Cell,Glial Cell, Bergmann,Glial Cell, Satellite,Glias,Neuroglial Cell,Neuroglias,Satellite Glia Cell,Satellite Glial Cell,Satellite Glias
D010713 Phosphatidylcholines Derivatives of PHOSPHATIDIC ACIDS in which the phosphoric acid is bound in ester linkage to a CHOLINE moiety. Choline Phosphoglycerides,Choline Glycerophospholipids,Phosphatidyl Choline,Phosphatidyl Cholines,Phosphatidylcholine,Choline, Phosphatidyl,Cholines, Phosphatidyl,Glycerophospholipids, Choline,Phosphoglycerides, Choline
D010738 Type C Phospholipases A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS. Lecithinase C,Phospholipase C,Phospholipases, Type C,Phospholipases C
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Phosphorylation of Sendai virus phosphoprotein by cellular protein kinase C zeta.
June 1997, The Journal of biological chemistry,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Oxidative stress induces protein kinase C-mediated activation loop phosphorylation and nuclear redistribution of protein kinase D.
June 2004, The Journal of biological chemistry,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Lipopolysaccharide induces jun N-terminal kinase activation in macrophages by a novel Cdc42/Rac-independent pathway involving sequential activation of protein kinase C zeta and phosphatidylcholine-dependent phospholipase C.
October 2000, Blood,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Imidazoline I(1) receptor-induced activation of phosphatidylcholine-specific phospholipase C elicits mitogen-activated protein kinase phosphorylation in PC12 cells.
March 2001, European journal of pharmacology,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Regulation of atypical zeta-protein kinase C in cellular signaling.
September 1994, Experimental cell research,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Platelet-derived growth factor activation of mitogen-activated protein kinase depends on the sequential activation of phosphatidylcholine-specific phospholipase C, protein kinase C-zeta and Raf-1.
July 1997, The Biochemical journal,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Activation loop phosphorylation-independent kinase activity of human protein kinase C zeta.
May 2007, Proteins,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Phospholipase C activates protein kinase C and induces monocytic differentiation of HL-60 cells.
August 1988, Blood,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Modulation of zeta-protein kinase C by cyclic AMP in PC12 cells occurs through phosphorylation by protein kinase A.
September 1996, Journal of neurochemistry,
I Galve-Roperh, and J M Malpartida, and A Haro, and I Diaz-Laviada
Thyrotropin-releasing hormone induces redistribution of protein kinase C in GH4C1 rat pituitary cells.
July 1985, The Journal of biological chemistry,
Copied contents to your clipboard!