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)

This work describes the acid phosphatase activity in supramedullary neurons of Coris julis, analyzed by a cytochemical method. The presence of both acid phosphatase-positive and -negative membrane bound granules indicates that only a part of the numerous electrodense granules in the supramedullary neurons can be interpreted as lysosomes. The great number of lysosomes in these large neurons of young animals is indicative of the rapid turnover of cell structures, which may be correlated with the high rate of synthesis. The electrodense granules showing no acid phosphatase activity are postulated to be vesicles containing gastrin/CCK-like peptide or precursors of this neuromediator.
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PMID:Acid phosphatase activity in the supramedullary neurons of Coris julis (L.). 138 Aug 57

The yeast Saccharomyces cerevisiae expresses the cloned cDNA (Amy) encoding human salivary alpha-amylase (Amy) under control of the yeast PHO5 promoter, and secretes the active enzyme into the culture medium. Two approaches were utilized to define the moiety of Amy, which is required for proper secretion and glycosylation. In one approach, chimeras were constructed with a variety of secretion signal sequences (yeast mating factor precursor sequence, yeast acid phosphatase signal sequence and human gastrin signal sequence) fused to the secretion signal-deleted Amy cDNA. The other approach involved analysis of a set of deletion series and a set of point mutations in the Amy-encoding region. The results showed that heterologous signal sequences were sufficient for proper secretion in yeast, irrespective of the insertion of some extra amino acids. In most cases, enzymes with deletions and Cys-465 substitution were not secreted, even though they had complete secretion signal sequences. Instead, they accumulated in the cell in a glycosylated form. Thus, proper secretion seems to require an appropriate conformation in the polypeptide moiety to be secreted.
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PMID:The conformation of mature human alpha-amylase conditions its secretion from yeast. 268 91

In Wistar rats kept for 15, 30 and 60 days in a hypokinetic state in special cages, alteration of some gastrointestinal glands was studied by means of histochemical and electron microscopic methods. After 15-30 days of hypokinesia, a decrease was found in the muco-polysaccharide content of the submaxillary, gastric and duodenal glands. The intestinal goblet cells appeared vacuolated. The oxyntic cells, which secrete HCl, as well as the G antral cells, which secrete gastrin, were in an active state. The hypokinetic rats exhibited increased gastric secretion. The electron microscopic aspect of the principal cells corresponded to augmented pepsin secretion. The enterocytes showed an increase in their leucine aminopeptidase, acid phosphatase and glucose-6-phosphatase content. In the submucosa of the fundus of the stomach an accumulation of eosinophils was observed. These modifications were more striking after 15 than after 30 days, and disappeared after 60 days of hypokinesia. These morphological and functional changes may be explained by glucocorticoid hypersecretion corresponding to a stress reaction.
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PMID:The gastrointestinal tract in hypokinetic rats. 1200 6

A protein tyrosine phosphatase (PTPase) with acid phosphatase activity was purified (500-fold) from the fluid of boar seminal vesicles. Preparative purification was performed with a 3-step procedure, employing FPLC S-Sepharose Fast Flow, Mono Q and Superdex 75 column. Protein tyrosine acid phosphatase (PTAPase) was homogeneous by polyacrylamide gel electrophoresis (PAGE, SDS-PAGE). PTAPase is a glycoprotein which has a molecular weight of about 41-42 kDa. This enzyme was maximally active at pH 5.5, and its thermostability was less than 80 degrees C. The K(m) value for p-nitrophenylphosphate, a specific synthetic substrate, was 0.87 x 10(-3)M, however, higher substrate specificity was shown when phosphotyrosine (K(m)=0.37 x 10(-3)M) and protein fragments, such as gastrin (K(m)=0.0032 x 10(-3)M) and hirudin (K(m)=0.0075 x 10(-3)M), were used as substrates. Activity of PTAPase was inhibited by dephostatin, molybdate and orthovanadate by 100, 95 and 70%, respectively, when phosphotyrosine was used as the substrate. Immunofluorescence study has shown that the seminal vesicles are the only source of PTAPase in boar seminal plasma.
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PMID:Purification and characterization of a protein tyrosine acid phosphatase from boar seminal vesicle glands. 1251 1