No relationship between enzyme activity and structure of nucleotide binding site in sarcoplasmic reticulum Ca2+-ATPase from short-term stimulated rat muscle

Aim:  We examined whether structural alterations to the adenine nucleotide binding site (ANBS) within sarcoplasmic (endo) reticulum Ca2+‐ATPase (SERCA) would account for contraction‐induced changes in the catalytic activity of the enzyme as assessed in vitro. Methods:  Repetitive contractions were i...

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Bibliographic Details
Published in:Acta Physiologica 2009-08, Vol.196 (4), p.401-409
Main Authors: Mishima, T., Kuratani, M., Kanzaki, K., Yamada, T., Matsunaga, S., Wada, M.
Format: Article
Language:English
Subjects:
adenine nucleotide binding site
Biological and medical sciences
calcium handling
Fundamental and applied biological sciences. Psychology
muscle fatigue
structural modification
Vertebrates: anatomy and physiology, studies on body, several organs or systems
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Summary:Aim:  We examined whether structural alterations to the adenine nucleotide binding site (ANBS) within sarcoplasmic (endo) reticulum Ca2+‐ATPase (SERCA) would account for contraction‐induced changes in the catalytic activity of the enzyme as assessed in vitro. Methods:  Repetitive contractions were induced in rat gastrocnemius by electrical nerve stimulation. Measurements of sarcoplasmic reticulum properties were performed on control and stimulated muscles immediately after or at 30 min after the cessation of 5‐min stimulation. In order to examine the properties at the ANBS, the binding capacity of SERCA to fluorescence isothiocyanate (FITC), a competitive inhibitor at the ANBS, was analysed in microsomes. Results:  Short‐term electrical stimulation evoked a 23.9% and 32.6% decrease (P 
ISSN:1748-1708
1748-1716
DOI:10.1111/j.1748-1716.2009.01986.x