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

Salivary-specific and cAMP-inducible expression of the rat proline-rich protein gene RP4 is dependent on a 28-base pair sequence of a salivary-specific cAMP response element (SCRE) (Lin, H. H., and Ann, D. K. (1992) Gene Expression 2, 365-377). To unravel its trans-acting factor(s), we used double-stranded oligoprobes corresponding to the SCRE to screen a randomly primed lambda gt11 cDNA expression library made from RNA of rat salivary cells. In this report, we describe the cDNA cloning of these helix-loop-helix SCRE-binding proteins (SCBPs) and demonstrate that there are at least three isoforms in salivary cells, namely SCBP alpha, SCBP beta, and SCBP gamma. RNA polymerase chain reaction and sequence analyses further confirmed the existence of these three different SCBP isoforms, which code for putative proteins of 707, 706, and 682 amino acids, respectively. Expression of the cloned SCBP cDNAs in salivary cells stimulates the expression of a cotransfected reporter construct containing multicopies of the SCRE cloned upstream of the thymidine kinase promoter and the chloramphenicol acetyltransferase structural gene. This stimulation is much more pronounced in transfections in which SCBP alpha and SCBP beta are cotransfected than when they are transfected individually. Furthermore, when low concentrations of SCBP alpha and SCBP beta are cotransfected with the SCRE reporter gene, coexpression of the catalytic subunit of protein kinase A is required to efficiently activate the expression of the reporter gene. These results strongly suggest that the observed stimulation of the SCRE is achieved through the coordinated expression of the SCBP alpha, SCBP beta, and protein kinase A activities, perhaps via a direct association of the two SCBPs and their phosphorylation by protein kinase A. We conclude that the isolated SCBP alpha and SCBP beta cDNAs encode transcription activators that participate in the control of the inducible RP4 gene expression in salivary cells.
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PMID:The helix-loop-helix proteins (salivary-specific cAMP response element-binding proteins) can modulate cAMP-inducible RP4 gene expression in salivary cells. 768 70

Transgenic mice were used to locate the cis-acting DNA elements that are essential for tissue-specific and inducible expression of the rat proline-rich protein gene, R15. Chimeric genes with up to 10 kb of R15 5'-flanking region fused to chloramphenicol acetyltransferase (CAT) or polyomaviral large T-antigen (PyLT) reporter genes were tested. Our results demonstrate that (1) the isoproterenol/tannin-inducible, parotid-specific transgene expression requires an upstream cis-regulatory domain, namely the parotid control region, which extends from -6 to -1.7 kb of the R15 gene; (2) this parotid control region functions with a heterologous promoter and is indispensable for achieving a reproducible chromosomal position-independent transgene expression; (3) deletion of the R15 5'-flanking region up to -1.7 kb results in a pleiotropic effect on the transgene expression, which includes ectopic (nonsalivary) reporter expression and lack of inducibility by either the beta-agonist isoproterenol or dietary tannin stimulation; (4) when the -10 to -6 kb region from the R15 gene is deleted in the construct, the inducible expression in the parotid glands of the transgenic mice decreases by over 30-fold, but position-independent and tissue-specific transgene expression is retained. Moreover, the mechanism of induction by either catecholamine isoproterenol or dietary tannin appears to be through a beta 1-adrenergic receptor-mediated pathway for both normal (non-transgenic) and transgenic animals.
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PMID:Isoproterenol/tannin-dependent R15 expression in transgenic mice is mediated by an upstream parotid control region. 801 29