Linked Life Data

2031869

Source:http://linkedlifedata.com/resource/pubmed/id/2031869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1991-6-27
pubmed:abstractText
Propionyl-CoA is formed principally during amino acid catabolism. It is then converted chiefly to succinate in a described three-step sequence. Free propionate is formed from propionyl-CoA to a very limited extent, but this anion can participate in a futile cycle of activation and hydrolysis, which can significantly deplete mitochondrial ATP. Free CoA and propionyl-CoA cannot enter or leave mitochondria, but propionyl groups are transferred between separate CoA pools by prior conversion to propionyl-L-carnitine. This reaction requires carnitine and carnitine acetyl transferase, an enzyme abundant in heart tissue. Propionyl-L-carnitine traverses both mitochondrial and cell membranes. Within the cell, this mobility helps to maintain the mitochondrial acyl-CoA/CoA ratio. When this ratio is increased, as in carnitine deficiency states, deleterious consequences ensue, which include deficient metabolism of fatty acids and urea synthesis. From outside the cell (in blood plasma), propionyl-L-carnitine can either be excreted in the urine or redistributed by entering other tissues. This process apparently occurs-without prior hydrolysis and reformation. It is suggested that heart tissue utilizes such exogenous propionyl-L-carnitine to stimulate the tricarboxylic acid cycle (via succinate synthesis) and that this may explain its known protective effect against ischemia.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0920-3206
pubmed:author
pubmed:issnType
Print
pubmed:volume
5 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-5
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Propionyl-L-carnitine: biochemical significance and possible role in cardiac metabolism.
pubmed:affiliation
Dipartimento di Chimica Biologica, Università di Padova, Italy.
pubmed:publicationType
Journal Article, Review