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Papers In Press, published online ahead of print February 8, 2001
Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106-4970
Corresponding Author: jxj12{at}po.cwru.edu
In a tail-suspension rat model, we investigated changes in myofilament protein during cardiac adaptation in simulated microgravity. Contractile force and velocity of cardiac muscle were decreased in the tail-suspension rats as compared with the control. Ca2+-dependent actomyosin ATPase activity was also decreased however sensitivity of cardiac muscle to Ca2+ activation was unchanged. There was no change in expression of myosin heavy chain, tropomyosin, troponin T or troponin I isoform protein in hearts of tail-suspension rats. A novel finding is a fragment of cardiac troponin I (cTnI) which had increased amounts in heart of tail-suspension rats. Binding of this cTnI fragment by a monoclonal antibody that specifically recognizes the COOH terminus indicates an intact COOH terminus. NH2-terminal sequence analysis of the cTnI fragment revealed truncations primarily of amino acids 1-26 and 1-27 and smaller amounts of 1-30, including Ser23 and Ser24, which are substrates of protein kinase A phosphorylation. This cTnI fragment is present in normal cardiac muscle and incorporated into myofibrils, indicating a role in regulating contractility. This proteolytic modification of cTnI up-regulated during simulated microgravity suggests a potential role of the NH2-terminal segment of cTnI in functional adaptations of cardiac muscle.
J. Biol. Chem, 10.1074/jbc.M011048200
Submitted on December 7, 2000
Revised on January 26, 2001
Accepted on February 8, 2001
A Proteolytic NH2-Terminal Truncation of Cardiac Troponin IThat is Up-Regulated in Simulated Microgravity
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