| pubmed-article:10801907 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0205054 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0019878 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0036725 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0087162 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0597297 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C1521828 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C1150952 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C1156853 | lld:lifeskim |
| pubmed-article:10801907 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:10801907 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10801907 | pubmed:dateCreated | 2000-6-7 | lld:pubmed |
| pubmed-article:10801907 | pubmed:abstractText | Vitamin B-6 deficiency causes mild elevation in plasma homocysteine, but the mechanism has not been clearly established. Serine is a substrate in one-carbon metabolism and in the transsulfuration pathway of homocysteine catabolism, and pyridoxal phosphate (PLP) plays a key role as coenzyme for serine hydroxymethyltransferase (SHMT) and enzymes of transsulfuration. In this study we used [(2)H(3)]serine as a primary tracer to examine the remethylation pathway in adequately nourished and vitamin B-6-deficient rats [7 and 0.1 mg pyridoxine (PN)/kg diet]. [(2)H(3)]Leucine and [1-(13)C]methionine were also used to examine turnover of protein and methionine pools, respectively. All tracers were injected intraperitoneally as a bolus dose, and then rats were killed (n = 4/time point) after 30, 60 and 120 min. Rats fed the low-PN diet had significantly lower growth and plasma and liver PLP concentrations, reduced liver SHMT activity, greater plasma and liver total homocysteine concentration, and reduced liver S-adenosylmethionine concentration. Hepatic and whole body protein turnover were reduced in vitamin B-6-deficient rats as evidenced by greater isotopic enrichment of [(2)H(3)]leucine. Hepatic [(2)H(2)]methionine production from [(2)H(3)]serine via cytosolic SHMT and the remethylation pathway was reduced by 80.6% in vitamin B-6 deficiency. The deficiency did not significantly reduce hepatic cystathionine-beta-synthase activity, and in vivo hepatic transsulfuration flux shown by production of [(2)H(3)]cysteine from the [(2)H(3)]serine increased over twofold. In contrast, plasma appearance of [(2)H(3)]cysteine was decreased by 89% in vitamin B-6 deficiency. The rate of hepatic homocysteine production shown by the ratio of [1-(13)C]homocysteine/[1-(13)C]methionine areas under enrichment vs. time curves was not affected by vitamin B-6 deficiency. Overall, these results indicate that vitamin B-6 deficiency substantially affects one-carbon metabolism by impairing both methyl group production for homocysteine remethylation and flux through whole-body transsulfuration. | lld:pubmed |
| pubmed-article:10801907 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10801907 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10801907 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10801907 | pubmed:month | May | lld:pubmed |
| pubmed-article:10801907 | pubmed:issn | 0022-3166 | lld:pubmed |
| pubmed-article:10801907 | pubmed:author | pubmed-author:MartinezMM | lld:pubmed |
| pubmed-article:10801907 | pubmed:author | pubmed-author:WilliamsonJJ | lld:pubmed |
| pubmed-article:10801907 | pubmed:author | pubmed-author:GregoryJ... | lld:pubmed |
| pubmed-article:10801907 | pubmed:author | pubmed-author:TothJ PJP | lld:pubmed |
| pubmed-article:10801907 | pubmed:author | pubmed-author:CuskellyG JGJ | lld:pubmed |
| pubmed-article:10801907 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10801907 | pubmed:volume | 130 | lld:pubmed |
| pubmed-article:10801907 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10801907 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10801907 | pubmed:pagination | 1115-23 | lld:pubmed |
| pubmed-article:10801907 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
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| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:meshHeading | pubmed-meshheading:10801907... | lld:pubmed |
| pubmed-article:10801907 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10801907 | pubmed:articleTitle | Vitamin B-6 deficiency in rats reduces hepatic serine hydroxymethyltransferase and cystathionine beta-synthase activities and rates of in vivo protein turnover, homocysteine remethylation and transsulfuration. | lld:pubmed |
| pubmed-article:10801907 | pubmed:affiliation | Food Science and Human Nutrition Department, University of Florida, Gainesville, FL 32611-0370, USA. | lld:pubmed |
| pubmed-article:10801907 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10801907 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10801907 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| entrez-gene:24962 | entrezgene:pubmed | pubmed-article:10801907 | lld:entrezgene |
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