BIOMAT Database Logo BIOMAT Database Logo

Selective activation of phospholipase C by recombinant G-protein alpha- and beta gamma-subunits. 1994

J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Department of Pharmacology, University of North Carolina School of Medicine, Chapel Hill 27599.

Receptor activation of phospholipase C (PLC) via G-proteins occurs by pertussis toxin-sensitive and toxin-insensitive signaling pathways. The alpha-subunits of the Gq family are presumed to mediate the toxin-insensitive pathway, but the nature of the G-proteins mediating the toxin-sensitive pathway is not established. Recently, PLC-beta has been shown to be activated by G-protein beta gamma-subunits of mixed or undefined composition. The relative activities of G-protein subunits that might activate PLC-beta were examined using defined recombinant alpha- and beta gamma-subunits obtained from the baculovirus expression system by reconstituting the purified subunits with purified bovine brain PLC-beta 1 or turkey erythrocyte PLC-beta in unilamellar phospholipid vesicles. Turkey erythrocyte G alpha 11 and recombinant G alpha 11 and G alpha q obtained after expression in Sf9 cells activated both bovine brain PLC-beta 1 and turkey erythrocyte PLC-beta. In contrast, under the same assay conditions, recombinant G alpha i1, G alpha i2, G alpha i3, and G alpha o were without effect on either type of PLC. All types of beta gamma-subunits tested (r beta 1 gamma 2, r beta 1 gamma 3, r beta 2 gamma 2, r beta 2 gamma 3, bovine brain beta gamma or turkey erythrocyte beta gamma) inhibited G alpha 11-mediated activation of PLC, presumably by promotion of formation of inactive heterotrimeric G-protein. All types of beta gamma-subunits also markedly stimulated the activity of turkey erythrocyte PLC-beta but did not activate bovine brain PLC-beta 1. Of the four different beta gamma complexes of defined composition, three stimulated PLC with similar activities whereas beta 2 gamma 3 was less effective. The data suggest that pertussis toxin-sensitive activation of PLC is mediated by the beta gamma-subunits of G-proteins acting on specific phospholipase C isoenzymes.

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.
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009036 Moths Insects of the suborder Heterocera of the order LEPIDOPTERA. Antheraea,Giant Silkmoths,Giant Silkworms,Silkmoths, Giant,Silkworms, Giant,Antheraeas,Giant Silkmoth,Giant Silkworm,Moth,Silkmoth, Giant,Silkworm, Giant
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
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D001921 Brain The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM. Encephalon
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography

Related Publications

J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phospholipase C isozymes by G protein beta gamma subunits.
March 1993, The Journal of biological chemistry,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phospholipase C-beta 2 mutants by G protein alpha q and beta gamma subunits.
December 1993, The Journal of biological chemistry,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of cytosolic phosphoinositide phospholipase C by G-protein beta gamma subunits.
November 1992, The Journal of biological chemistry,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Isozyme-selective stimulation of phospholipase C-beta 2 by G protein beta gamma-subunits.
December 1992, Nature,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Stimulation of phospholipase C by G-protein beta gamma subunits.
January 1994, Methods in enzymology,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phosphatidylinositol lipid-specific phospholipase C-beta 3 by G-protein beta gamma subunits.
January 1993, FEBS letters,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phospholipase C by G-protein beta gamma subunits in DDT1MF-2 cells.
February 1995, European journal of pharmacology,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phospholipase C by G-protein beta gamma subunits in DDT1MF-2 cells.
February 1995, Biochemical Society transactions,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Regulation of purified subtypes of phosphatidylinositol-specific phospholipase C beta by G protein alpha and beta gamma subunits.
May 1993, The Journal of biological chemistry,
J L Boyer, and S G Graber, and G L Waldo, and T K Harden, and J C Garrison
Activation of phospholipase C beta 2 by the alpha and beta gamma subunits of trimeric GTP-binding protein.
June 1993, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!