Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT01586 (G418)
 2,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The sequence of a Saccharomyces cerevisiae cDNA encoding a novel 61-kDa protein serine/threonine phosphatase, termed PPQ1, is presented. The protein consists of two distinct domains: the carboxy-terminal phosphatase domain is approximately 60% identical to either PP1 or the carboxy-terminal domains of PPZ1 and PPZ2, while the amino-terminal region is rich in serine and asparagine. Deletion of the gene encoding PPQ1 reduces cell growth on several carbon sources, and lowers cell density in the stationary phase. Cells in which PPQ1 gene has been deleted show altered morphology from wild-type cells in the stationary phase in the absence of an essential amino acid and a reduced rate of protein synthesis in the exponential phase. They are hypersensitive to the protein synthesis inhibitors, cycloheximide and G418, implicating PPQ1 in the regulation of translation.
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PMID:PPQ, a novel protein phosphatase containing a Ser + Asn-rich amino-terminal domain, is involved in the regulation of protein synthesis. 826 60

Protein kinase Cdelta (PKCdelta) is a member of protein kinase C family, which possess phospholipid-dependent serine and threonine kinase activity. PKCdelta is a potential drug target of diabetes and some cancers. The abnormal activation of PKCdelta can arouse diabetes and some cancers. Therefore the specific inhibitors of PKCdelta can be applied in the research and development of the drug candidate of these diseases. The present aim is to obtain active recombinant PKCdelta from COS1 cells. For cloning of mouse PKCdelta a pair of specific primers were designed based on the published sequence of this gene. The cDNA of full coding region was obtained by RT-PCR. The amplified cDNA was subsequently cloned into FLAG-tagged pcDNA3.0 and its sequence was confirmed by DNA sequencing analysis. FLAG-tagged pcDNA3.0-PKCdelta was transfected into COS1 cells. A cell strain which can stably express PKCdelta was obtained by G418 screening. FLAG-tagged PKCdelta in the supernant of COS1 cells extracts was absorbed by anti-FLAG resin and eluted by FLAG peptide. The purified protein appeared as a single band on both SDS-PAGE and western blotting, indicating that it was chemical and antigenic pure. By kinase assay, the recombinant PKCdelta was active. Positive inhibitor, staurosporine, was used to prove the enzyme could be greatly inhibited. Several compounds have been found to inhibit the enzyme, which indicates the preliminary application in drug lead compounds screening.
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PMID:[Cloning, expression, purification of protein kinase Cdelta and its preliminary application in drug lead compounds screening]. 1601 94