PMID: 2125207Dec 1, 1990Paper

A novel 100 kDa protein, localized to receptor-enriched endosomes, is immunologically related to the signal-transducing guanine-nucleotide-binding proteins Gt and Gi

The Biochemical Journal
L M TraubR Sagi-Eisenberg

Abstract

Antisera raised against the C-terminus decapeptide of the alpha-subunit of the retinal guanine-nucleotide-binding protein (G-protein) transducing (Gt) cross-reacted with the alpha-subunit of the inhibitory G-protein Gi. The same antisera also reacted with a 100 kDa protein (p100) found in rat liver homogenates. The immunoreactivity of both Gt and p100 was specifically inhibited by the immunizing peptide with similar dose-dependencies [concn. causing 50% inhibition (IC50) = 300 ng/ml]. This similarity in inhibition profiles implies that p100 contains within its structure the C-terminal sequence shared by both alpha t and alpha i. Tissue distribution studies demonstrated that p100 was particularly enriched in the liver and kidney, but was also present in other rat tissues, as well as in a number of cell lines tested. In the liver, p100 was found in both the soluble and membrane fractions. The membrane-associated form of p100 was specifically localized to an endosomal fraction (termed D-R), previously shown to be a ligand-free but receptor-enriched subfraction of liver endosomal vesicles. Two-dimensional gel electrophoresis revealed that both the cytosolic and membrane-bound forms of p100 occurred as a series of 100 kDa polypeptid...Continue Reading

Citations

Dec 22, 1994·Nature·R H KehlenbachW B Huttner
Jan 26, 1996·Molecular and Cellular Biochemistry·S JoshiD K Agrawal
Oct 10, 1998·Biochimica Et Biophysica Acta·T A KassessinoffR Sagi-Eisenberg
May 9, 1998·Molecular and Biochemical Parasitology·D J GrabO K ole-MoiYoi
Dec 1, 1994·Journal of Pharmacological and Toxicological Methods·N Ali, D K Agrawal

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