Different mechanisms underlie the long-term regulation of pyruvate dehydrogenase kinase (PDHK) by tri-iodothyronine in heart and liver

Antibodies to purified recombinant PDHKII were used for ELISAs of PDHKII in mitochondrial extracts. In liver, hyperthyroidism elicited a 2.3-fold increase in PDHK activity ( P<0.01) which was accompanied by a significant 1.5-fold ( P<0.001) increase in the amount of mitochondrial immunoreactiv...

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Published inFEBS letters Vol. 419; no. 1; pp. 55 - 57
Main Authors Priestman, David A, Donald, Elaine, Holness, Mark J, Sugden, Mary C
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 08.12.1997
Subjects
Animals
Cell Extracts
ELISA
Enzyme-Linked Immunosorbent Assay - methods
Female
Hyperthyroidism - enzymology
Mitochondria, Heart - enzymology
Mitochondria, Liver - enzymology
PDHKII
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases
Pyruvate dehydrogenase
Rats
Rats, Wistar
Triiodothyronine - pharmacology
PDHKII
Pyruvate dehydrogenase
ELISA
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Summary:Antibodies to purified recombinant PDHKII were used for ELISAs of PDHKII in mitochondrial extracts. In liver, hyperthyroidism elicited a 2.3-fold increase in PDHK activity ( P<0.01) which was accompanied by a significant 1.5-fold ( P<0.001) increase in the amount of mitochondrial immunoreactive PDHKII. In contrast, despite a stable 2.0-fold increase in cardiac PDHK activity ( P<0.001), the amount of mitochondrial immunoreactive PDHKII in heart was unaffected by hyperthyroidism. The mechanisms for long-term regulation of PDHK activity by thyroid hormones therefore differ fundamentally between heart and liver.
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ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01430-0