| pubmed-article:9539713 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C0085080 | lld:lifeskim |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C1157383 | lld:lifeskim |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:9539713 | lifeskim:mentions | umls-concept:C0136824 | lld:lifeskim |
| pubmed-article:9539713 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:9539713 | pubmed:dateCreated | 1998-5-13 | lld:pubmed |
| pubmed-article:9539713 | pubmed:abstractText | Phosphatidylserine (PtdSer) synthesis in Chinese hamster ovary (CHO) cells occurs through the exchange of L-serine with the base moiety of phosphatidylcholine or phosphatidylethanolamine. The synthesis is depressed on the addition of PtdSer to the culture medium. A CHO cell mutant named mutant 29, whose PtdSer biosynthesis is highly resistant to this depression by exogenous PtdSer, has been isolated from CHO-K1 cells. In the present study, the PtdSer-resistant PtdSer biosynthesis in the mutant was traced to a point mutation in the PtdSer synthase I gene, pssA, resulting in the replacement of Arg-95 of the synthase by lysine. Introduction of the mutant pssA cDNA, but not the wild-type pssA cDNA, into CHO-K1 cells induced the PtdSer-resistant PtdSer biosynthesis. In a cell-free system, the serine base-exchange activity of the wild-type pssA-transfected cells was inhibited by PtdSer, but that of the mutant pssA-transfected cells was resistant to the inhibition. Like the mutant 29 cells, the mutant pssA-transfected cells grown without exogenous PtdSer exhibited an approximately 2-fold increase in the cellular PtdSer level compared with that in CHO-K1 cells, although the wild-type pssA-transfected cells did not exhibit such a significant increase. These results indicated that the inhibition of PtdSer synthase I by PtdSer is essential for the maintenance of a normal PtdSer level in CHO-K1 cells and that Arg-95 of the synthase is a crucial residue for the inhibition. | lld:pubmed |
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| pubmed-article:9539713 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9539713 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9539713 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9539713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9539713 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9539713 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9539713 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9539713 | pubmed:author | pubmed-author:SaitoKK | lld:pubmed |
| pubmed-article:9539713 | pubmed:author | pubmed-author:NishijimaMM | lld:pubmed |
| pubmed-article:9539713 | pubmed:author | pubmed-author:HasegawaKK | lld:pubmed |
| pubmed-article:9539713 | pubmed:author | pubmed-author:KugeOO | lld:pubmed |
| pubmed-article:9539713 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9539713 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:9539713 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9539713 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9539713 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9539713 | pubmed:pagination | 4199-203 | lld:pubmed |
| pubmed-article:9539713 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9539713 | pubmed:meshHeading | pubmed-meshheading:9539713-... | lld:pubmed |
| pubmed-article:9539713 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9539713 | pubmed:articleTitle | Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells. | lld:pubmed |
| pubmed-article:9539713 | pubmed:affiliation | Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162, Japan. kuge@nih.go.jp | lld:pubmed |
| pubmed-article:9539713 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9539713 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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