Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-4-7
pubmed:abstractText
A concerted function of purine nucleotide (PN) binding and fatty acid (FA) release from the uncoupling protein (UP) resulting in the maximum coupling (potential) of brown adipose tissue (BAT) mitochondria was demonstrated. The uncoupling effect of FA was studied (at 4 mM MgCl2): 17 nmol oleate per mg protein caused a slight uncoupling with 8.9 mM ATP but with ATP below 3.6 mM almost total uncoupling was achieved. This shows that the PN-controlled gate can be stabilized in the closed conformation (with 8.9 mM ATP), also when FA is bound to UP. The sensitivity of the FA effect to ATP proves that oleate directly interacts with UP. The closed conformation of the H+ channel of UP is then abolished by oleate when a lower free ATP concentration is maintained outside.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carnitine, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Nonesterified, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Oleic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Uncoupling Agents, http://linkedlifedata.com/resource/pubmed/chemical/mitochondrial uncoupling protein
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:2920823-Adenosine Diphosphate, pubmed-meshheading:2920823-Adenosine Triphosphate, pubmed-meshheading:2920823-Adipose Tissue, Brown, pubmed-meshheading:2920823-Animals, pubmed-meshheading:2920823-Carnitine, pubmed-meshheading:2920823-Carrier Proteins, pubmed-meshheading:2920823-Cricetinae, pubmed-meshheading:2920823-Fatty Acids, Nonesterified, pubmed-meshheading:2920823-Guanosine Diphosphate, pubmed-meshheading:2920823-Homeostasis, pubmed-meshheading:2920823-Ion Channels, pubmed-meshheading:2920823-Kinetics, pubmed-meshheading:2920823-Membrane Proteins, pubmed-meshheading:2920823-Mitochondria, pubmed-meshheading:2920823-Mitochondrial Proteins, pubmed-meshheading:2920823-Oleic Acid, pubmed-meshheading:2920823-Oleic Acids, pubmed-meshheading:2920823-Oxygen Consumption, pubmed-meshheading:2920823-Uncoupling Agents
pubmed:year
1989
pubmed:articleTitle
Carnitine cycle in brown adipose tissue mitochondria as a tool for studying the regulatory role of fatty acids in the uncoupling protein function.
pubmed:affiliation
Institute of Physiology, Czechoslovak Academy of Sciences, Prague.
pubmed:publicationType
Journal Article