Cardiac troponin C (TnC) and a site I skeletal TnC mutant alter Ca2+versuscrossbridge contribution to force in rabbit skeletal fibres
نویسندگان
چکیده
منابع مشابه
The low-affinity Ca2(+)-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: site I alone cannot trigger contraction.
Both troponin C (TnC) and calmodulin share a remarkably similar tertiary motif that may be common to other Ca2(+)-binding proteins with activator activity. TnC plays a critical role in regulating muscle contraction and is particularly well-suited for structural analysis by site-directed mutation. Fast-twitch skeletal muscle TnC has two low-affinity Ca2(+)-binding sites (sites I and II), while i...
متن کاملSynthetic analog of a high affinity calcium binding site in rabbit skeletal troponin C.
A 21-residue peptide analog of the Ca2+ binding Site 3 in rabbit skeletal troponin C has been synthesized by the solid phase method. CD studies as well as uv difference spectroscopy did not show any changes upon addition of Ca2+ to this peptide in aqueous solution. Acetylation of the NH2-terminal residue of the analog resulted in Ca2+-induced CD and uv difference spectral changes and these chan...
متن کاملCalcium-induced structural transition in the regulatory domain of human cardiac troponin C.
While calcium binding to troponin C (TnC) triggers the contraction of both skeletal and cardiac muscle, there is clear evidence that different mechanisms may be involved. For example, activation of heart myofilaments occurs with binding to a single regulatory site on TnC, whereas activation of fast skeletal myofilaments occurs with binding to two regulatory sites. The physiological difference b...
متن کاملMutation of the high affinity calcium binding sites in cardiac troponin C.
Fast skeletal and cardiac troponin C (TnC) contain two high affinity Ca2+/Mg2+ binding sites within the C-terminal domain that are thought to be important for association of TnC with the troponin complex of the thin filament. To test directly the function of these high affinity sites in cardiac TnC they were systematically altered by mutagenesis to generate proteins with a single inactive site ...
متن کاملDeveloping Cardiac and Skeletal Muscle Share Fast-Skeletal Myosin Heavy Chain and Cardiac Troponin-I Expression
Skeletal muscle derived stem cells (MDSCs) transplanted into injured myocardium can differentiate into fast skeletal muscle specific myosin heavy chain (sk-fMHC) and cardiac specific troponin-I (cTn-I) positive cells sustaining recipient myocardial function. We have recently found that MDSCs differentiate into a cardiomyocyte phenotype within a three-dimensional gel bioreactor. It is generally ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Physiology
سال: 2005
ISSN: 0022-3751
DOI: 10.1113/jphysiol.2004.077891