GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxin

@article{Nagata1988GTPbindingPI,
  title={GTP‐binding proteins in human platelet membranes serving as the specific substrate of islet‐activating protein, pertussis toxin},
  author={Koh-ichi Nagata and Toshiaki Katada and Masahiro Tohkin and Hiroshi Itoh and Yoshito Kaziro and Michio Ui and Yoshinori Nozawa},
  journal={FEBS Letters},
  year={1988},
  volume={237}
}
View on Wiley
ncbi.nlm.nih.gov
30 Citations

30 Citations

Citation Type

Citation Type

Molecular heterogeneity of the subclasses of islet-activating protein (pertussis toxin)-sensitive GTP-binding proteins in porcine thyroid tissue.
Identification of the pertussis toxin-sensitive G proteins in platelets, megakaryocytes, and human erythroleukemia cells.
TLDR
The pertussis toxin substrates that have previously been detected in platelets and HEL cells are shown to be members of the Gi alpha family, all of which are candidates for interaction with receptors for thrombin and other agonists.
Immunochemical comparison of pertussis toxin substrates in brain and peripheral tissues.
A low Mr GTP‐binding protein, Rapl, in human platelets: localization, translocation and phosphorylation by cyclic AMP‐dependent protein kinase
TLDR
The results strongly suggest that Rapl in plasma membranes and the protein on a‐granules are regulated by different mechanisms, and have different functions.
Evidence for the Presence of a Low Mr GTP-binding Protein, ram p25, in Human Platelet Membranes.
TLDR
The ram gene was isolated from a rat megakaryocyte cDNA library and encodes a GTP-binding protein that was observed to be present in membrane fractions of human platelets.
Purification and identification of two pertussis-toxin-sensitive GTP-binding proteins of bovine spleen.
Purification and separation of closely related members of pertussis toxin-substrate G proteins.
Purification and characterization of five different alpha subunits of guanine-nucleotide-binding proteins in bovine brain membranes. Their physiological properties concerning the activities of adenylate cyclase and atrial muscarinic K+ channels.
TLDR
The results suggest that alpha and beta gamma subunits might activate the K+ channels by mechanisms different from each other.
Characterization of four GO‐type proteins purified from bovine brain membranes
Purification and characterization of a low M(r) GTP-binding protein, c25KG, from human platelet membranes.
...
...

References

SHOWING 1-10 OF 23 REFERENCES
A new GTP‐binding protein in brain tissues serving as the specific substrate of islet‐activating protein, pertussis toxin
Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. Interaction of the alpha-subunits with beta gamma-subunits in development of their biological activities.
Two proteins serving as substrates for ADP-ribosylation catalyzed by islet-activating protein (IAP), pertussis toxin, and binding guanosine 5'-(3-O-thio)triphosphate (GTP gamma S) with high…
The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Properties and function of the purified protein.
Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain.
Mechanisms for inhibition of the catalytic activity of adenylate cyclase by the guanine nucleotide-binding proteins serving as the substrate of islet-activating protein, pertussis toxin.
TLDR
The direct inhibition of the catalyst by beta gamma or GTP gamma S-bound alpha 41 is a likely mechanism involved in receptor-mediated inhibition of adenylate cyclase, in addition to the previously proposed indirect inhibition due to the reduction of the concentration of the active alpha-subunit of Ns by reassociation with beta gamma.
Stimulation by GTP-binding proteins (Gi, Go) of partially purified phospholipase C activity from human platelet membranes.
Interactions in platelets between G proteins and the agonists that stimulate phospholipase C and inhibit adenylyl cyclase.
Primary structure of the α-subunit of transducin and its relationship to ras proteins
TLDR
The complementary DNA encoding the α-subunit of bovine retinal transducin is cloned and sequenced and from this the complete amino-acid sequence is deduced.
Identification of three pertussis toxin substrates (41, 40 and 39 kDa proteins) in mammalian brain Comparison of predicted amino acid sequences from G‐protein α‐subunit genes and cDNAs with partial amino acid sequences from purified proteins
Primary structure of the α‐subunit of bovine adenylate cyclase‐inhibiting G‐protein deduced from the cDNA sequence
...
...