Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01350 (gastrin)
 9,683 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The precursor of the acid-stimulating hormone gastrin contains a phosphorylation site which is immediately adjacent to a functionally important cleavage site, and which occurs in a sequence resembling the phosphorylation sites in casein. We have examined phosphorylation of human preprogastrin 93-101 with [gamma-32P]ATP by a Triton-solubilized Golgi membrane preparation from mammary glands of lactating rats. The activity of solubilized Golgi membranes was approx. an order of magnitude greater than that of intact vesicles suggesting a luminal orientation of the kinase. Incorporation of 32P was linear for up to 12 min at 30 degrees C, and the half-maximal rate of phosphorylation at 1 mM ATP was observed at peptide concentrations of 0.2 mM. The Km for ATP was 0.12 mM and the maximal velocity was 2.17 nmol of peptide per min per mg Golgi protein. Proteinase inhibitors (leupeptin, pepstatin, benzamidine) and p-nitrophenyl phosphate did not influence phosphorylation. The incorporation of 32P was inhibited by poly-L-lysine but not by heparin. We conclude that the phosphorylation site in progastrin is a substrate for a Golgi membrane kinase and that a similar enzyme might act on endogenous progastrin in vivo.
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PMID:Phosphorylation of human preprogastrin 93-101 by a Golgi membrane kinase from rat mammary gland. 814 83

The fibroblast growth factor (FGF) family is composed of polypeptides with sequence identity which signal through transmembrane tyrosine kinase receptors. We report here the purification from bovine brain microsomes of an FGF-2-binding complex composed of three proteins of apparent molecular masses 150 kDa, 79 kDa and 46 kDa. Only the 150 kDa and 79 kDa proteins bound FGF-2 in cross-linking and ligand-blotting experiments. Binding of FGF-2 to p79 is enhanced in the presence of calcium. Peptide sequences allowed the identification of p150 and the cloning of the cDNAs encoding p79 and p46. The deduced amino acid sequence of p79 reveals high similarity to those of gastrin-binding protein and mitochondrial enoyl-CoA hydratase/hydroxyacyl-CoA dehydrogenase. p46 is similar to mitochondrial ketoacyl-CoA thiolase. Stable transfection of FR3T3 rat fibroblast cells with p79 cDNA analysed by electron microscopy following immunolabelling of ultra-thin cryosections revealed a localization of p79 in the secretory pathway, mainly in the endoplasmic reticulum and the Golgi region, where it is specifically associated with the molecular chaperone calnexin. In vivo a protein similar to the Golgi protein MG-160 forms a complex with FGF-2 and p79.
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PMID:Identification and characterization of an intracellular protein complex that binds fibroblast growth factor-2 in bovine brain. 1041 36