Modulation of pyruvate dehydrogenase kinase activity in cultured hepatocytes by glucagon and n-octanoate.
The activity of pyruvate dehydrogenase kinase in extracts of mitochondria from rat hepatocytes cultured for 21 h in medium 199 was increased 2.5-fold by the presence of 55 nM-glucagon and 1 mM-sodium n-octanoate in the culture medium. The change was comparable with that induced in vivo by 48 h starvation. The potential contribution of branched-chain complex to estimates of PDH-complex activity in rat liver mitochondria has been defined.
H R
HR
Fatania
T C
TC
Vary
P J
PJ
Randle
D000818:Animals; D002210:Caprylates / Q000494:pharmacology*; D002478:Cells, Cultured; D005934:Glucagon / Q000494:pharmacology*; D008099:Liver / Q000166:cytology; D008297:Male; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D000081382:Pyruvate Dehydrogenase Acetyl-Transferring Kinase; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D002210:Caprylates; D000081382:Pyruvate Dehydrogenase Acetyl-Transferring Kinase; D011768:Pyruvate Dehydrogenase Complex; D005934:Glucagon; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; C031492:octanoic acid