Abstract:
:Branched-chain alpha-keto acid dehydrogenase (BCKDH) complex catalyzes the committed step of branched-chain amino acid catabolism, and its activity is regulated by the phosphorylation-dephosphorylation cycle. BCKDH kinase is responsible for inactivation of the complex by phosphorylation. In the present study, we examined acute exercise on the activity state of the complex as well as the amounts of bound and free forms of the kinase in rat liver and skeletal muscle. Acute exercise activated the complex in association with a decrease in the bound form of kinase in both liver and muscle. The free form of kinase in both tissues was slightly increased but the total amount of the kinase was not affected by acute exercise. The protein amount ratio of bound kinase to E1beta component of the complex was much higher in muscle than in the liver of rats, reflecting the low activity state of the complex in muscle. These results suggest that the amount of the bound kinase plays an important role in regulation of the activity state of the complex. We propose that the alteration in the amount of bound BCKDH kinase is a short-term regulatory mechanism for determining the activity of BCKDH complex.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Xu M,Nagasaki M,Obayashi M,Sato Y,Tamura T,Shimomura Ydoi
10.1006/bbrc.2001.5647subject
Has Abstractpub_date
2001-09-28 00:00:00pages
752-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(01)95647-5journal_volume
287pub_type
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