Stimulation by GTP-binding proteins (Gi, Go) of partially purified phospholipase C activity from human platelet membranes

Banno, Yoshiko; Nagao, Seiji; Katada, Toshiaki; Nagata, Koh‐ichi; Ui, Michio; Nozawa, Yoshinori

doi:10.1016/0006-291x(87)90610-3

Cited by 46 publications

(10 citation statements)

References 33 publications

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“…An enhanced IP 3 production has been measured in depolarized neurons (Gusovsky et al, 1986). It may be attributed to an accelerated phosphoinositide turnover (Gusovsky et al, 1986;Gurwitz and Sokolovsky, 1987), as well as to the stimulation of receptor tyrosine kinases (Castren et al, 1992;Huang et al, 1999), or activation of trimeric G-proteins (Banno et al, 1987;Berridge and Irvine, 1989;Exton, 1990;Sierro et al, 1992;Anis et al, 1999).…”

Section: Discussionmentioning

confidence: 97%

A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase

Homburg

Visochek

Moran

et al. 2000

The Journal of Cell Biology

130

125

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We present the first evidence for a fast activation of the nuclear protein poly(ADP-ribose) polymerase (PARP) by signals evoked in the cell membrane, constituting a novel mode of signaling to the cell nucleus. PARP, an abundant, highly conserved, chromatin-bound protein found only in eukaryotes, exclusively catalyzes polyADP-ribosylation of DNA-binding proteins, thereby modulating their activity. Activation of PARP, reportedly induced by formation of DNA breaks, is involved in DNA transcription, replication, and repair. Our findings demonstrate an alternative mechanism: a fast activation of PARP, evoked by inositol 1,4,5,-trisphosphate–Ca2+ mobilization, that does not involve DNA breaks. These findings identify PARP as a novel downstream target of phospholipase C, and unveil a novel fast signal–induced modification of DNA-binding proteins by polyADP-ribosylation.

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Section: Discussionmentioning

confidence: 97%

A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase

Homburg

Visochek

Moran

et al. 2000

The Journal of Cell Biology

130

125

View full text Add to dashboard Cite

show abstract

“…This suggests that endogenous Rho does not regulate PLD activity in HL60 membranes. It is perhaps relevant that activation of partially purified phospholipase C by the G i and G o GTP binding proteins was demonstrated (20) prior to the identification of G q and G 11 and that nonphysiological activation of the same phospholipase was detected when p21 ras was over-expressed in NIH3T3 cells (21). Thus, under certain conditions it may be possible to activate phospholipases with inappropriate G-proteins.…”

Section: Discussionmentioning

confidence: 99%

Activation of Phospholipase D and Phosphatidylinositol 4-Phosphate 5-Kinase in HL60 Membranes Is Mediated by Endogenous Arf but Not Rho

Martin

Brown

Hodgkin

et al. 1996

Journal of Biological Chemistry

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“…The function of the G␣ o3 subtype is not clear (14). Phospholipase C activation mediated by activation of G oproteins has been demonstrated in the cell-free system (20), and G o -protein-mediated activation of protein kinase C has been observed in Chinese hamster ovary (CHO) cells (21).…”

mentioning

confidence: 99%

Activation of Go-proteins by Membrane Depolarization Traced by in Situ Photoaffinity Labeling of Gαo-proteins with [α32P]GTP-azidoanilide

Anis¹,

Nürnberg²,

Visochek³

et al. 1999

Journal of Biological Chemistry

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GTP-binding trimeric proteins have been implicated in signal transduction from receptors in the cell membrane to intracellular effectors and ion channels in a variety of cells (1-5). The mechanism involves signal-induced G-protein activation initiated by an exchange of GDP for GTP on the ␣ subunit of the protein (5-7). Subsequent GTPase activity of the G␣ subunit converts the activated G-proteins into their inactive, GDPbound state (7). Activation of G-proteins has been induced experimentally by stimulation of G-protein-coupled receptors in the cell membrane (2,3,8,9). Evidence indicating activation of G-proteins in response to membrane depolarization were previously observed in brain stem synaptoneurosomes (10 -12).G␣ o -proteins are widely distributed in the central nervous system (15-17). Three subtypes showing marked homology but exhibiting functional differences have been identified (13,14,18). The G␣ o1 subtype appears to be involved in the coupling of muscarinic receptors to Ca ϩ2 channels, and the G␣ o2 subtype mediates inhibition of Ca ϩ2 current activated by somatostatin receptors (19). The function of the G␣ o3 subtype is not clear (14). Phospholipase C activation mediated by activation of G oproteins has been demonstrated in the cell-free system (20), and G o -protein-mediated activation of protein kinase C has been observed in Chinese hamster ovary (CHO) cells (21).In the present study, in situ photoaffinity labeling with [␣ 32 P]GTPAA 1 (22, 23) indicated a depolarization-induced accelerated exchange of GDP for [␣ 32 P]GTPAA in G␣ o1 -and G␣ o3 -proteins, implying a depolarization-induced activation of these G o -proteins. [␣ 32 P]-GTPAA was introduced into transiently permeabilized synaptoneurosomes as described before (10). Unlike the endogenously bound guanine nucleotides, [␣ 32 P]GT-PAA, covalently bound to G␣-proteins by photoaffinity labeling, was not displaced during SDS-polyacrylamide gel electrophoresis, providing a possible tool for identification of in situ activated G-proteins.In view of findings indicating a reciprocal influence of depolarization-induced activation of VGSC and uncoupling of Gproteins from muscarinic receptors (12, 24, 25), we examined the possibility that VGSC can be involved in depolarizationinduced activation of G␣ o -proteins. Our results indicated that depolarization-induced activation of G o -proteins can be prevented by preventing VGSC activation. In addition, in depolarized brain-stem and cortical synaptoneurosomes, the ␣ subunit of VGSC cross-linked most efficiently with G␣ o -proteins. In isolated synaptoneurosomal membranes, VGSC-␣ subunit cross-linked most efficiently with GDP␤S-bound rather than GTP␥S-bound G␣ o -proteins. These findings suggest repeated

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Stimulation by GTP-binding proteins (Gi, Go) of partially purified phospholipase C activity from human platelet membranes

Cited by 46 publications

References 33 publications

A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase

A Fast Signal–Induced Activation of Poly(Adp-Ribose) Polymerase

Activation of Phospholipase D and Phosphatidylinositol 4-Phosphate 5-Kinase in HL60 Membranes Is Mediated by Endogenous Arf but Not Rho

Activation of Go-proteins by Membrane Depolarization Traced by in Situ Photoaffinity Labeling of Gαo-proteins with [α32P]GTP-azidoanilide

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