Use of specific antibodies to quantitate the guanine nucleotide-binding protein Go in brain.

Gierschik, Peter; Milligan, Graeme; Pines, Mark; Goldsmith, Paul K.; Codina, Juan; Klee, Werner A.; Spiegel, Allen M.

doi:10.1073/pnas.83.7.2258

Cited by 151 publications

(119 citation statements)

References 16 publications

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“…However, with the purification of two pertussis toxin-sensitive Gproteins from bovine brain [21,22], and the subsequent demonstrations that these proteins were at least immunologically [22,23], if not functionally [24] distinct, it became apparent that a more selective means of assessing the molecular identity of pertussis toxin-sensitive G-proteins was required. The further demonstration that neither antisera which selectively identified the major form of Gr (Gil) or Go from brain were able to cross-react with the major pertussis toxin-sensitive substrate in human neutrophils [25] or in rat glioma cells [26] further added to the complexity of the system. cDNA cloning studies have now identified at least 6 potential G-protein a-subunit gene products which contain the characteristic signature of pertussis toxin substrates, that is, a cysteine residue located 4 amino acids from the C-terminus [4].…”

Section: Discussionmentioning

confidence: 99%

“…We have previously characterised a polyclonal antiserum to rod transducin (CW6) [23] which cross-reacts with the major form of brain Gi (Gil), which on epitope mapping ap: peared to be directed against an epitope(s) within a very limited region of the protein [23,27]. This polyclonal antiserum shows little or no reactivity against the a-subunit of Gr2 [25,26] despite the fact that Gil and Gi2 are some 88% homologous at the primary sequence level. In this particular case one region (epitope) of the protein appeared to be immunodominant.…”

Section: Discussionmentioning

confidence: 99%

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Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes

et al. 1989

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Immunoblotting of rat myometrial membranes with an antiserum (SGl) which recognizes the a-subunits of both G,l and G,2 indicated the presence of detectable levels of an apparently single form of some 40 kDa. A second antiserum (LE2) specific for G,2 also recognized this protein, confirming its identity. Immunoblotting of the myometrial membranes with a series of antipeptide (OCl, IMl, ONl) and polyclonal (RV3) antisera, all of which recognize rat brain G,, produced a more complex pattern. Antisera OCl and ON1 recognized a single polypeptide which essentially comigrated with rat brain G,. In contrast, antisera RV3 and IMI did not recognize the myometrial protein. These data provide evidence for the presence of Gi2 and of a novel G-protein, related immunologically to G,, in rat myometrial membranes.Guanine nucleotide-binding protein; Pertussis toxin; (Myometrium, Brain)

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes

et al. 1989

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“…Gao belongs to the Gai family of G protein a subunits and shares about an 82% homology with Gai and is pertussis toxin sensitive (Neer et al, 1984;Sternweis and Robishaw, 1984;Van Meurs et al, 1987). The tissue distribution of Gao is quite interesting in that Gao is abundantly expressed in neuronal tissue (Gierschik et al, 1986). Intracellularly, Gao is found localized in the growth cones of neuronal tissue, suggesting a role for Gao in neuronal function (Nusse and Neer, 1996).…”

Section: E Ectors For Gao and Gai2mentioning

confidence: 99%

G protein coupled receptor signaling through the Src and Stat3 pathway: role in proliferation and transformation

2001

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“…For that purpose the purified a subunits of transducin (a,) and bovine neutrophils (M,,) were used. The GTP-binding a subunit from bovine neutrophil membranes is a novel pertussis toxin substrate of 40 kDa which can be distinguished immunologically from bovine brain ai and a, [5]. The requirement of transducin fly or bovine brain By subunits for ADP-ribosylation of transducin a subunit is shown in Fig.…”

Section: Requirement Of Fly Subunits For Pertussis-toxin-catalyzed Admentioning

confidence: 99%

Regulation of signal transfer from beta1-adrenoceptor to adenylate cyclase by betagamma subunits in a reconstituted system

et al. 1987

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The By subunits of guanine nucleotide binding proteins from bovine brain and bovine rod outer segments have different structural and immunochemical properties. In spite of these structural differences, py subunits from these sources have been found to be fully interchangeable in terms of their interaction with a subunits of pertussistoxin-sensitive G proteins. In contrast, however, there are striking differences between these by subunits with regard to their ability to deactivate fluoride-stimulated G,. These profound differences were also observed when the interaction of the purified components of the adenylate cyclase system was studied after reconstitution into phospholipid vesicles. Addition of by subunits purified from bovine brain to vesicles containing P-receptor and G, results in a biphasic effect on receptor-stimulated GTPase activity, whereas addition of transducin py was virtually without any effect. Likewise, by from bovine brain, but not transducin by, affected adenylate cyclase activity of a reconstituted system consisting of three purified components (R, G,, C). Thus, the a subunit of G,, but not the a subunits of pertussis-toxin-sensitive G proteins discriminate between structurally different Py subunits.It is now generally accepted that GTP-binding proteins play a universal role as receptor-effector couplers in hormonal and visual signal transduction. But whereas G, and Gi stimulate and inhibit adenylate cyclase, respectively, GI activates a retinal cGMP phosphodiesterase presumably by removing an inhibitory y subunit of the enzyme [l, 21. In addition, there are other G proteins, such as Go, G, and G, [3 -51. It is possible that these G proteins participate in other, not yet defined, receptor-effector coupling systems. All signaltransducing G proteins which have been characterized on a molecular basis have been found to be heterotrimers. The masses of the a subunits of the G proteins which bind and hydrolyze GTP range over 21 -52 kDa. All a subunits are substrates for ADP-ribosylation catalyzed by one or more bacterial toxin. Data obtained by molecular cloning have revealed that all a subunits studied so far differ structurally but that their homologies are great enough to consider them to belong to one class of related proteins [6]. The , ! 3 subunits of the G-protein heterotrimers isolated from different sources contain, with the exception of transducin, two chains with [8] indicate that the 35-kDa chain differs from the 36-kDa one. These data are corroborated by the existence of two genes for subunits [9]. Moreover, the y subunit of transducin seems to differ from all other known y subunits Until now, the information available is scarce on how the structural differences between the various by subunits may be related to functional differences. It was shown, for example, that transducin Py subunits and those from rabbit liver membranes can both support coupling of transducin a to lightactivated rhodopsin [12]. Moreover, it was shown by Cerione et al. [13] that transducin fly subunits can inhib...

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Use of specific antibodies to quantitate the guanine nucleotide-binding protein Go in brain.

Cited by 151 publications

References 16 publications

Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes

Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes

G protein coupled receptor signaling through the Src and Stat3 pathway: role in proliferation and transformation

Regulation of signal transfer from beta1-adrenoceptor to adenylate cyclase by betagamma subunits in a reconstituted system

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Use of specific antibodies to quantitate the guanine nucleotide-binding protein Go in brain.

Cited by 151 publications

References 16 publications

Identification of both Gi2 and a novel, immunologically distinct, form of Go in rat myometrial membranes

Identification of both Gi2 and a novel, immunologically distinct, form of Go in rat myometrial membranes

G protein coupled receptor signaling through the Src and Stat3 pathway: role in proliferation and transformation

Regulation of signal transfer from beta1-adrenoceptor to adenylate cyclase by betagamma subunits in a reconstituted system

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Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes

Identification of both G_i2 and a novel, immunologically distinct, form of G_o in rat myometrial membranes