Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-21
pubmed:abstractText
Synthesis of glucose from 10 mM D-glycerate by hepatocytes isolated from rats fasted 24 h was inhibited by 3-aminopicolinate (3AP), 3-mercaptopicolinate (3MP), and aminoxyacetate (AOA). The inhibition by AOA can be exerted over that caused by either of the picolinates. The effects of 3AP and 3MP were not additive, and cannot be ascribed totally to inhibition of reducing equivalent transfer by their inhibitory effect on phosphoenolpyruvate carboxykinase. The time course and dependence on substrate concentration of gluconeogenesis from L-glycerate was similar to those from D-glycerate, even though the cellular content of D-glycerate was markedly less when L-glycerate was the substrate. Gluconeogenesis from L-glycerate was not significantly affected by 3AP or 3MP, but was inhibited by AOA. The degree of inhibition by AOA of glucose synthesis from L-glycerate was greater than that from D-glycerate. Studies employing [14C]paraformaldehyde revealed that hydroxypyruvate may be converted to dihydroxyacetone in the hepatocyte. A hitherto unknown inhibition site of 3AP and 3MP is inferred and a dual pathway of D- and L-glycerate gluconeogenesis consistent with these results is proposed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
433-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Pathway of gluconeogenesis from D- and L-glycerate in rat hepatocytes.
pubmed:affiliation
Institute for Enzyme Research, University of Wisconsin, Madison 53705.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.