Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.3.1.28 (chloramphenicol acetyltransferase)
 5,100 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A physiologically relevant response to insulin, stimulation of prolactin promoter activity in GH4 pituitary cells, was used as an assay to study the specificity of protein-tyrosine phosphatase function. Receptor-like protein-tyrosine phosphatase alpha (RPTPalpha) blocks the effect of insulin to increase prolactin gene expression but potentiates the effects of epidermal growth factor and cAMP on prolactin promoter activity. RPTPalpha was the only protein-tyrosine phosphatase tested that did this. Thus, the effect of RPTPalpha on prolactin-chloramphenicol acetyltransferase (CAT) promoter activity is specific by two criteria. A number of potential RPTPalpha targets were ruled out by finding (a) that they are not affected or (b) that they are not on the pathway to insulin-increased prolactin-CAT activity. The negative effect of RPTPalpha on insulin activation of the prolactin promoter is not due to reduced phosphorylation or kinase activity of the insulin receptor or to reduced phosphorylation of insulin receptor substrate-1 or Shc. Inhibitor studies suggest that insulin-increased prolactin gene expression is mediated by a Ras-like GTPase but is not mitogen-activated protein kinase dependent. Experiments with inhibitors of phosphatidylinositol 3-kinase suggest that insulin-increased prolactin-CAT expression is phosphatidylinositol 3-kinase-independent. These results suggest that RPTPalpha may be a physiological regulator of insulin action.
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PMID:Receptor-like protein-tyrosine phosphatase alpha specifically inhibits insulin-increased prolactin gene expression. 946 45

Human prostatic acid phosphatase (PAcP) is a prostate epithelium-specific differentiation antigen. The cellular form of PAcP functions as a neutral protein-tyrosine phosphatase, and is involved in regulating prostate cell growth. Although some information on the PAcP gene structure has been obtained, little is known regarding the cis- and trans-acting factors that regulate its expression. Due to the biological importance of PAcP, we investigated the regulation of its expression. A region upstream of the PAcP gene from -2899 to +87 base pairs was linked to the coding sequence of the chloramphenicol acetyltransferase (CAT) gene. Sequential deletions of the sequence between -2899 and -205 revealed that, in addition to the basic promoter, the region between -1258 and -779 represents a positive regulatory element. This -1258/-779 fragment could enhance the PAcP promoter activity in PC-3 and DU 145 human prostate cancer cells, but not in non-prostate cancer cells, including WI-38 lung diploid cells, A-431 epidermoid carcinoma cells, and HeLa cervix epitheloid carcinoma cells. Furthermore, this cis-element together with the promoter sequence could drive a high level of expression of green fluorescent protein (GFP) in PC-3 cells, but not in HeLa cells. The prostate-specific expression was further examined by injecting naked plasmid DNA into the prostate and the hamstring muscle of mice. The fluorescence pattern clearly showed that the level of GFP expression is consistently higher in prostate cells than in muscle cells of the intact animal. The data collectively indicate that region between -1258 and -779 is involved in governing the cell type-specific expression of the PAcP gene.
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PMID:Identification and characterization of regulatory elements of the human prostatic acid phosphatase promoter. 1203 38