pubmed-article:8391439 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0193398 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0010734 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0311989 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:8391439 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:8391439 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8391439 | pubmed:dateCreated | 1993-8-3 | lld:pubmed |
pubmed-article:8391439 | pubmed:abstractText | Regulation of CTP:choline-phosphate cytidylyltransferase activity was studied in regenerating rat liver. The formation of phosphatidylcholine from [14C]choline in hepatocytes isolated from regenerating liver at 22 h after surgery was increased 1.9-fold when compared with hepatocytes from sham-operated animals. This effect was accompanied by a 1.4-fold increase in cytosolic cytidylyltransferase activity as well as by a 1.5-fold increase in the amount of immunoreactive cytidylyltransferase protein, and a 1.7-fold increase in [35S]methionine incorporation into cytidylyltransferase protein. Northern blot analysis of cytidylyltransferase mRNA showed two signals at 1.5 and 5.0 kb. Partial hepatectomy caused a significant 2-3-fold increase in the 1.5-kb and 5.0-kb messengers at 12 h after surgery. During the next 10 h after partial hepatectomy cytidylyltransferase mRNA levels slightly decreased, although they were still elevated in comparison with sham-operated rats 20-22 h after surgery. In contrast to the elevated cytidylyltransferase mRNA levels, the amount of acetyl-CoA carboxylase mRNA did not increase between 12 and 22 h after surgery, which is in line with the unchanged activity of this enzyme. In conclusion, our data demonstrate that in regenerating liver phosphatidylcholine biosynthesis and cytidylyltransferase activity are regulated at a pretranslational level. | lld:pubmed |
pubmed-article:8391439 | pubmed:language | eng | lld:pubmed |
pubmed-article:8391439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391439 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8391439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8391439 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8391439 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8391439 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8391439 | pubmed:issn | 0014-2956 | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:VaartjesW JWJ | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:BatenburgJ... | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:Van GoldeL... | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:TijburgL BLB | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:HouwelingMM | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:CornellR BRB | lld:pubmed |
pubmed-article:8391439 | pubmed:author | pubmed-author:KalmarG BGB | lld:pubmed |
pubmed-article:8391439 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8391439 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8391439 | pubmed:volume | 214 | lld:pubmed |
pubmed-article:8391439 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8391439 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8391439 | pubmed:pagination | 927-33 | lld:pubmed |
pubmed-article:8391439 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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pubmed-article:8391439 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8391439 | pubmed:articleTitle | Evidence that CTP:choline-phosphate cytidylyltransferase is regulated at a pretranslational level in rat liver after partial hepatectomy. | lld:pubmed |
pubmed-article:8391439 | pubmed:affiliation | Laboratory of Veterinary Biochemistry, Utrecht University, The Netherlands. | lld:pubmed |
pubmed-article:8391439 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8391439 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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