The differential detergent solubilization of adenylate cyclase and polypeptides ADP‐ribosylated with cholera toxin suggests an excess of G/F protein relative to adenylate cyclase in rat pancreatic plasma membranes

Svoboda, Michal; Furnelle, Jacques; Christophe, Jean

doi:10.1016/0014-5793(81)80978-7

Cited by 8 publications

(7 citation statements)

References 25 publications

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“…We thus decided to check the présence of ADP-ribosylable proteins in the a-subunit of Ns. This was achieved with [a-^^P]NAD^ and choiera toxin, foUowed by SDS-PAGE and autoradiography [9]. Autoradiograms revealed (Fig.…”

Section: Détermination Of the M Of Adp-ribosylated Proteins In The Nmentioning

confidence: 97%

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Adenylate cyclase stimulation by VIP in rat and human parotid membranes

Bogaert¹,

Soukias

Dehaye³

et al. 1987

Regulatory Peptides

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Adenylate cyclase activity was stimulated by vasoactive intestinal peptide (VIP) in rat parotid membranes, in the presence of 100 microM guanosine triphosphate (GTP). The threshold concentration of VIP was 300 nM and the activity doubled at the maximal VIP concentration tested (30 microM). The relative potency of peptides of the VIP family was: VIP greater than peptide histidine isoleucinamide (PHI) greater than secretin. The beta-adrenergic agent isoproterenol was a more efficient activator of rat parotid adenylate cyclase and its stimulatory effect, like that of VIP, depended on the presence of GTP. The effects of VIP and isoproterenol were both potentiated by 10 microM forskolin. By comparison with rat parotid preparations, membranes from a human parotid gland responded similarly to the VIP family of peptides (VIP greater than PHI greater than secretin). In both rat and human parotid membranes, two proteins (Mr 44 kDa and 53 kDa) of the alpha-subunit of Ns (the guanyl nucleotide-binding stimulatory protein) were labelled by ADP-ribosylation, in the presence of cholera toxin. Taken together, these results indicate that VIP receptors, when coupled to Ns, were able to activate the adenylate cyclase system in rat and human parotid membranes.

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Section: Détermination Of the M Of Adp-ribosylated Proteins In The Nmentioning

confidence: 97%

“…The M, of ADP-ribosylable constituents of the a-subunit of Ns was estimated after transfer of the ADP-ribose moiety of NAD"^ in the présence of choiera toxin [8], followed by SDS-PAGE and autoradiography of the separated proteins, as described in [9].…”

Section: The Mr Of Proteins Adp-ribosylated With Choiera Toxinmentioning

confidence: 99%

Adenylate cyclase stimulation by VIP in rat and human parotid membranes

Bogaert¹,

Soukias

Dehaye³

et al. 1987

Regulatory Peptides

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“…The two forms of G,cu (42 and 48 kDa) previously detected in rat pancreatic plasma membranes and AR l-4-25 membranes [3,12] by ADP-ribosylation in the presence of CT seemed to be absent from ZG membranes ( Fig. 2A).…”

Section: Adp-ribosylation In the Presence Of Bacterial Toxinsmentioning

confidence: 75%

“…1). Crosslinking specificity was shown by low residual labelling when the incuba- [3,12] by ADP-ribosylation in the presence of CT seemed to be absent from ZG membranes ( Fig. 2A).…”

Section: Crosslinking Of [Cy--'~p/gtp On Membrane Proteinsmentioning

confidence: 93%

“…CCK can also stimulate PC hydrolysis by phospholipase D, contributing to DAG formation [2]; to our knowledge, the role of a Gprotein in the coupling of CCK receptors to phospholipase D has not yet been investigated. [3] are detected by ADP-ribosylation in the presence of CT. Low-affinity CCK receptors, whose occupancy correlates with the downstroke of the dose-response curve for enzyme secretion, are also coupled through G, with adenylate cyclase in the rat pancreas [4,5]. Pancreatic adenylate cyclase is submitted to a negative regulation through somatostatin receptors [6] coupled to adenylate cyclase through Gi [7] already identified by ADP-ribosylation in the presence of PT [8].…”

Section: Introductionmentioning

confidence: 99%

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Novel GTP‐binding proteins in plasma membranes and zymogen granule membranes from rat pancreas and in pancreatic AR 4‐2J cell membranes

1990

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Stimulation by cholera toxin of ADP‐ribosylation of membrane proteins, adenylate cyclase and insulilin release in pancreatic islets

Svoboda

García-Morales

Dufrane

et al. 1985

Cell Biochemistry & Function

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In rat pancreatic islet membranes exposed to [alpha-32P]NAD, cholera toxin stimulated the labelling of three peptides with Mr close to 22 000, 42 000 and 48 000, respectively. In the islets, the toxin-stimulated ADP-ribosylation of the heavy form of the Ns alpha-subunit predominated over that of the light form, in mirror image of the situation found in the exocrine pancreas. When intact islets were preincubated with cholera toxin, the adenylate cyclase activity of a subcellular particulate fraction was increased. The responsiveness of adenylate cyclase to GTP was also augmented, but that to NaF was decreased. In intact islets, the production of cyclic AMP and the glucose-stimulated release of insulin were also enhanced after pretreatment with cholera toxin. These findings reveal the presence in pancreatic islets of the guanyl nucleotide regulatory protein of adenylate cyclase, with an unusual predominance of the heavy form of the Ns alpha-subunit.

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The differential detergent solubilization of adenylate cyclase and polypeptides ADP‐ribosylated with cholera toxin suggests an excess of G/F protein relative to adenylate cyclase in rat pancreatic plasma membranes

Cited by 8 publications

References 25 publications

Adenylate cyclase stimulation by VIP in rat and human parotid membranes

Adenylate cyclase stimulation by VIP in rat and human parotid membranes

Novel GTP‐binding proteins in plasma membranes and zymogen granule membranes from rat pancreas and in pancreatic AR 4‐2J cell membranes

Stimulation by cholera toxin of ADP‐ribosylation of membrane proteins, adenylate cyclase and insulilin release in pancreatic islets

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