Pertussis toxin substrate is a guanosine 5′-[<i>β</i>-thio]diphosphate-, <i>N</i>-ethylmaleimide-, Mg2+- and temperature-sensitive GTP-binding protein

Wong, Sharon; Martin, Baptiste; Tolkovsky, A M

doi:10.1042/bj2320191

Cited by 32 publications

(18 citation statements)

References 32 publications

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“…As the effect of GH on the ability of PIA to inhibit the lipolytic system was retained in isolated membranes, it allowed further dissection of the basis of the GH effect. Pertussis toxin elicits the ADP-ribosylation of the undissociated G i heterotrimer (Tsai et al 1984, Wong et al 1985; interaction of G i with the activated receptor causes dissociation of G i into the subunit and the subunit with a concomitant decrease in pertussis toxin-catalysed ADP-ribosylation. Thus pertussis toxin-catalysed ADPribosylation along with determination of the total amount of G i by immunoblotting can provide an indication of the proportion of the heterotrimer that has dissociated into and subunits.…”

Section: Tablementioning

confidence: 99%

Regulation of the GTP-binding protein-based antilipolytic system of sheep adipocytes by growth hormone

Doris¹,

Kilgour²,

Houslay³

et al. 1998

Journal of Endocrinology

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Chronic exposure of sheep adipose tissue to growth hormone (GH) in vitro decreases the ability of the adenosine analogue, N 6 -phenylisopropyladenosine (PIA), to inhibit isoprenaline-stimulated lipolysis by a mechanism which is dependent on both gene transcription and protein serine/threonine phosphorylation. The inhibition is not due to a change in ligand binding to the adenosine receptor, the amounts of the three isoforms of the inhibitory GTP-binding protein, G i , or the maximum (forskolin-stimulated) adenylate cyclase activity. The ability of GH to modulate the PIA-activated adenosine receptor to stimulate dissociation of heterotrimeric G i was assessed by measurement of pertussis toxin-catalysed ADP-ribosylation of G i ; GH does not appear to alter the interaction between the activated receptor and G i . The ability of GH to alter the ability of activated G i to inhibit adenylate cyclase activity was assessed by measuring the ability of a GTP analogue, guanosine 5 -[ -imido]triphosphate (p[NH]ppG), to inhibit forskolinstimulated adenylate cyclase activity; chronic exposure to GH prevented this effect of p [NH]ppG. Thus the attenuation of the inhibition of lipolysis by PIA by chronic exposure of adipocytes to GH appears to be due to an impairment in the interaction between adenylate cyclase and the subunit of one or more isoforms of G i .

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Section: Tablementioning

confidence: 99%

Regulation of the GTP-binding protein-based antilipolytic system of sheep adipocytes by growth hormone

Doris¹,

Kilgour²,

Houslay³

et al. 1998

Journal of Endocrinology

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“…It has been demonstrated that IAP can catalyze the transfer of ADP-ribose from N A D to a subunits of Gi and Go, namely Cia and Goa (Katada & Ui 1982;Katada et al 1986). These results suggest that IAP preferably catalyzes the transfer of ADP-ribose from N A D to G i / G o when G proteins are taking the undissociated or GDP-bound form (Codina et al 1984;Wong et al 1985;Katada ef al. Then, the mixture of a subunits of Gi and G o was quantitated as a whole.…”

Section: Discussionmentioning

confidence: 99%

“…Then, the mixture of a subunits of Gi and G o was quantitated as a whole. Perhaps GTP is converted into GDP during the incubation, which might explain why IAP-catalyzed ADP-ribosylation of G i / G o is enhanced by addition of GTP even in the presence of MgCI, (Wong et al 1985) 2). 1 lyzed by IAP was enhanced by GTP and CDPpS both in the absence and presence of MgCI2, whereas, in the case of IAP-mediated ADP-ribosylation with GTPyS and GPP(NH)p, 32P-incorporation was enhanced in the absence of MgC1, but markedly reduced in the presence of 10 m M MgCI?.…”

Section: Discussionmentioning

confidence: 99%

“…Neither the addition of lithium in vitro nor the chronic administration of lithium altered the IAP-sensitive [32P]ADP-ribosylation in either brain region. 1984;Wong et a/. However, several factors that could modify the susceptibility to the enzyme reaction such as phosphorylation of G proteins by cyclic AMP-dependent protein kinase (Watanabe et d. 1988) or by protein kinase C Katada et a/.…”

Section: [32p]adp-ribosylation Of G I / G O Cata-mentioning

confidence: 99%

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Lithium Does Not Alter ADP‐Ribosylation of Gi/Go Catalyzed by Pertussis Toxin in Rat Brain

Odagaki

Koyama

Yamashita

1991

Pharmacology & Toxicology

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The influences of lithium in vitro and ex vivo on the ADP-ribosylation of Gi/Go catalyzed by pertussis toxin (islet-activating protein, IAP) were investigated in cerebral cortical and hippocampal membranes from rats. Incorporation of [32P]ADP-ribose into 40-41 kDa band catalyzed by IAP was markedly reduced by the addition of non-hydrolyzable GTP analogue, guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) or guanosine 5'-(beta, gamma-imido)triphosphate [Gpp(NH)p], in the presence of MgCl2 but not in the absence of MgCl2. The amounts of IAP-catalyzed ADP-ribosylation of Gi/Go in the presence of 100 microM guanosine 5'-O-(2-thiodiphosphate) (GDP beta S) and 50 mM EDTA and in the absence of MgCl2 were in proportion to the protein contents between 30 and 60 micrograms/tube, suggesting that the determination of [32P]ADP-ribosylation could be used quantitatively within this limited range. Addition of LiCl in vitro did not affect the IAP-mediated ADP-ribosylation of Gi/Go up to the concentration of 5 mM. The values of ADP-ribosylation of Gi/Go in the presence of 100 microM GTP gamma S were reduced by MgCl2 concentration-dependently. However, this inhibitory effect of MgCl2 was not influenced by 2 mM LiCl in vitro. Furthermore, chronic treatment with a diet containing 0.2% lithium carbonate did not alter the [32P]ADP-ribosylation of Gi/Go catalyzed by IAP.

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“…Cells were incubated with pertussis toxin (OS-1 gg/ml) for a total of 1 h. After 30 min of incubation the quinZAM was added as already described. Pertussis toxin was preactivated by incubating appropriate portions in 50 mM dithiothreitol for 1 h at 25°C [20].…”

Section: Quin2 Loading and Measurement Of [Cd']imentioning

confidence: 99%

Pertussis toxin inhibits the angiotensin II and serotonin‐induced rise of free cytoplasmic calcium in cultured smooth muscle cells from rat aorta

Berthou

Marmé

1987

FEBS Letters

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Angiotensin II, serotonin and K+-depolarization cause an increase in free cytoplasmic CaZ+ in cultured smooth muscle cells. The involvement of a guanine nucleotide-binding protein has been investigated by using pertussis toxin. When smooth muscle cells were pretreated with pertussis toxin angiotensin II and serotonin-induced rise of cytosolic Ca2+ was found to be significantly reduced whereas the Ca2+ influx mediated by K+-depolarization remained unchanged. These results suggest the participation of a guanine nucleotidebinding protein in the receptor-mediated rise of intracellular Ca2+.

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Pertussis toxin substrate is a guanosine 5′-[β-thio]diphosphate-, N-ethylmaleimide-, Mg2+- and temperature-sensitive GTP-binding protein

Cited by 32 publications

References 32 publications

Regulation of the GTP-binding protein-based antilipolytic system of sheep adipocytes by growth hormone

Regulation of the GTP-binding protein-based antilipolytic system of sheep adipocytes by growth hormone

Lithium Does Not Alter ADP‐Ribosylation of Gi/Go Catalyzed by Pertussis Toxin in Rat Brain

Pertussis toxin inhibits the angiotensin II and serotonin‐induced rise of free cytoplasmic calcium in cultured smooth muscle cells from rat aorta

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