BIOMAT Database Logo BIOMAT Database Logo

Rapid aldosterone signaling in vascular smooth muscle cells: involvement of phospholipase C, diacylglycerol and protein kinase C alpha. 1995

M Christ, and C Meyer, and K Sippel, and M Wehling
Division of Clinical Pharmacology, Klinikum Innenstadt, University of Munich, Federal Republic of Germany.

Rapid in vitro effects of aldosterone (ALDO) on intracellular sodium, potassium and calcium, cell volume and the sodium-proton-antiport have been described in human mononuclear leukocytes and rat vascular smooth muscle cells (VSMC). These nongenomic effects are signaled through membrane receptors with a high affinity for aldosterone, but not for hydrocortisone. Effects of ALDO on the production of diacylglycerol (DAG) and protein kinase C alpha (PKC) were measured in VSCM by enzymatic assay and immunoblotting. DAG production was stimulated twofold by ALDO (> or = 1 nM) within 30 sec while hydrocortisone was inactive at concentrations of up to 1 microM. The inhibitors of phospholipase C, neomycin and U-73122 completely blocked this effect. PKC translocation from cytosol to membranes by ALDO occurred within 5 min, the extent of this effect was comparable to that of angiotensin II. These data demonstrate rapid intracellular signaling for ALDO in VSMC through phospholipase C, DAG and PKC in addition to calcium and inositol-1,4,5-trisphosphate as determined earlier.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009131 Muscle, Smooth, Vascular The nonstriated involuntary muscle tissue of blood vessels. Vascular Smooth Muscle,Muscle, Vascular Smooth,Muscles, Vascular Smooth,Smooth Muscle, Vascular,Smooth Muscles, Vascular,Vascular Smooth Muscles
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
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
D002455 Cell Division The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION. M Phase,Cell Division Phase,Cell Divisions,Division Phase, Cell,Division, Cell,Divisions, Cell,M Phases,Phase, Cell Division,Phase, M,Phases, M
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D004075 Diglycerides Glycerides composed of two fatty acids esterified to the trihydric alcohol GLYCEROL. There are two possible forms that exist: 1,2-diacylglycerols and 1,3-diacylglycerols. Diacylglycerol,Diacylglycerols

Related Publications

M Christ, and C Meyer, and K Sippel, and M Wehling
Endothelin stimulates diacylglycerol accumulation and activates protein kinase C in cultured vascular smooth muscle cells.
May 1989, The Journal of biological chemistry,
M Christ, and C Meyer, and K Sippel, and M Wehling
Differentiation of vascular smooth muscle cells and the regulation of protein kinase C-alpha.
January 1995, Circulation research,
M Christ, and C Meyer, and K Sippel, and M Wehling
Protein kinase C does not regulate diacylglycerol metabolism in aortic smooth muscle cells.
July 1990, Molecular and cellular biochemistry,
M Christ, and C Meyer, and K Sippel, and M Wehling
Protein Kinase C- alpha/betaII, delta, and zeta/lambda involvement in ethanol-induced MAPK expression in vascular smooth muscle cells.
May 2007, Cellular and molecular biology (Noisy-le-Grand, France),
M Christ, and C Meyer, and K Sippel, and M Wehling
Fatty acids inhibit growth-factor-induced diacylglycerol kinase alpha activation in vascular smooth-muscle cells.
July 2001, The Biochemical journal,
M Christ, and C Meyer, and K Sippel, and M Wehling
Antisense suppresssion of protein kinase C-alpha and -delta in vascular smooth muscle.
June 1996, The Journal of surgical research,
M Christ, and C Meyer, and K Sippel, and M Wehling
Association of diacylglycerol kinase zeta with protein kinase C alpha: spatial regulation of diacylglycerol signaling.
March 2003, The Journal of cell biology,
M Christ, and C Meyer, and K Sippel, and M Wehling
Sphingosine induces phospholipase D and mitogen activated protein kinase in vascular smooth muscle cells.
December 1998, Biochemistry and molecular biology international,
M Christ, and C Meyer, and K Sippel, and M Wehling
Rapid actions of aldosterone: lymphocytes, vascular smooth muscle and endothelial cells.
January 1999, Steroids,
M Christ, and C Meyer, and K Sippel, and M Wehling
Herbimycin A inhibits protein kinase C in vascular smooth muscle cells.
May 1996, Biochemistry and molecular biology international,
Copied contents to your clipboard!