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PLCB1  -  phospholipase C, beta 1 (phosphoinositide...

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Disease relevance of PLCB1

  • 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 [1].
  • The protein toxin of Pasteurella multocida PMT is a potent mitogen and activator of phospholipase Cbeta [2].
  • The presence of Gs alpha and pertussis toxin substrates, Gi alpha and Go alpha subunits as well as PLC beta 1 in bovine brain coated vesicles has been confirmed by immunoblot [3].
 

High impact information on PLCB1

  • But at neutral pH, the order of specific activity was PLC-III greater than PLC-II greater than PLC-I [4].
  • The three enzymes were affected differently by bovine serum albumin: inhibition of PLC-I and activation of PLC-III were observed, whereas PLC-II was unaffected [4].
  • We previously reported that cytosolic fractions of bovine brain contain two immunologically distinct phosphoinositide-specific phospholipases C (PLCs), PLC-I and PLC-II [5].
  • We propose, therefore, that PLC-I and its truncated form are weakly associated with membranes [5].
  • In contrast, a PH domain derived from PLC-delta1, which could bind to PIP2, showed a nearly identical inhibition of both PLC-beta1 and PLD activities [6].
 

Biological context of PLCB1

 

Anatomical context of PLCB1

  • 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 [1].
  • Activation of PLC gamma isoforms, rather than PLC beta isoforms, may, therefore, be primarily responsible for BK-stimulated IP3 generation in endothelial cells [12].
  • This isozyme was immunologically identified as PLC-beta, an isozyme previously characterized in bovine brain cytosol and 2 M KCl membrane extracts [13].
 

Associations of PLCB1 with chemical compounds

 

Other interactions of PLCB1

  • More than 90% of PLC-II was found in the cytosolic fractions, whereas the PLC-I-like molecules were equally distributed between cytosolic and particulate fractions [5].
  • Receptor-catalyzed activation of Gq/11 by GTP gamma S, measured as the ability to activate purified phospholipase C-beta 1, paralleled receptor-catalyzed [35S]GTP gamma S binding [7].
 

Analytical, diagnostic and therapeutic context of PLCB1

References

  1. Selective activation of phospholipase C by recombinant G-protein alpha- and beta gamma-subunits. Boyer, J.L., Graber, S.G., Waldo, G.L., Harden, T.K., Garrison, J.C. J. Biol. Chem. (1994) [Pubmed]
  2. Biological activity of a C-terminal fragment of Pasteurella multocida toxin. Busch, C., Orth, J., Djouder, N., Aktories, K. Infect. Immun. (2001) [Pubmed]
  3. Metabotropic glutamate receptor analogues inhibit p[NH]ppG-stimulated phospholipase C activity in bovine brain coated vesicles: involvement of a pertussis toxin-sensitive G-protein. Martín, M., Sanz, J.M., Ros, M., Cubero, A. Biochem. J. (1995) [Pubmed]
  4. Bovine brain cytosol contains three immunologically distinct forms of inositolphospholipid-specific phospholipase C. Ryu, S.H., Suh, P.G., Cho, K.S., Lee, K.Y., Rhee, S.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Phospholipase C associated with particulate fractions of bovine brain. Lee, K.Y., Ryu, S.H., Suh, P.G., Choi, W.C., Rhee, S.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  6. Inhibition of phospholipase D by a protein factor from bovine brain cytosol. Partial purification and characterization of the inhibition mechanism. Kim, J.H., Suh, Y.J., Lee, T.G., Kim, Y., Bae, S.S., Kim, M.J., Lambeth, J.D., Suh, P.G., Ryu, S.H. J. Biol. Chem. (1996) [Pubmed]
  7. Reconstitution of agonist-stimulated phosphatidylinositol 4,5-bisphosphate hydrolysis using purified m1 muscarinic receptor, Gq/11, and phospholipase C-beta 1. Berstein, G., Blank, J.L., Smrcka, A.V., Higashijima, T., Sternweis, P.C., Exton, J.H., Ross, E.M. J. Biol. Chem. (1992) [Pubmed]
  8. Feedback regulation of phospholipase C-beta by protein kinase C. Ryu, S.H., Kim, U.H., Wahl, M.I., Brown, A.B., Carpenter, G., Huang, K.P., Rhee, S.G. J. Biol. Chem. (1990) [Pubmed]
  9. Purification of a novel phospholipase C isozyme from bovine cerebellum. Min, D.S., Kim, D.M., Lee, Y.H., Seo, J., Suh, P.G., Ryu, S.H. J. Biol. Chem. (1993) [Pubmed]
  10. Isoprenylation of the G protein gamma subunit is both necessary and sufficient for beta gamma dimer-mediated stimulation of phospholipase C. Dietrich, A., Brazil, D., Jensen, O.N., Meister, M., Schrader, M., Moomaw, J.F., Mann, M., Illenberger, D., Gierschik, P. Biochemistry (1996) [Pubmed]
  11. Regulation of the rate and extent of phospholipase C beta 2 effector activation by the beta gamma subunits of heterotrimeric G proteins. Runnels, L.W., Scarlata, S.F. Biochemistry (1998) [Pubmed]
  12. Bradykinin stimulates the tyrosine phosphorylation and bradykinin B2 receptor association of phospholipase C gamma 1 in vascular endothelial cells. Venema, V.J., Ju, H., Sun, J., Eaton, D.C., Marrero, M.B., Venema, R.C. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  13. Purification and characterization of PLC-beta m, a muscarinic cholinergic regulated phospholipase C from rabbit brain membrane. Carter, H.R., Wallace, M.A., Fain, J.N. Biochim. Biophys. Acta (1990) [Pubmed]
  14. Purification and characterization of two G-proteins that activate the beta 1 isozyme of phosphoinositide-specific phospholipase C. Identification as members of the Gq class. Blank, J.L., Ross, A.H., Exton, J.H. J. Biol. Chem. (1991) [Pubmed]
  15. Purification of a 110-kDa phosphoinositide phospholipase C that is activated by G-protein beta gamma-subunits. Blank, J.L., Shaw, K., Ross, A.H., Exton, J.H. J. Biol. Chem. (1993) [Pubmed]
  16. Purification and characterization of phosphoinositide-specific phospholipase C from bovine iris sphincter smooth muscle. Zhou, C.J., Akhtar, R.A., Abdel-Latif, A.A. Biochem. J. (1993) [Pubmed]
 
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