Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/38361
標題: Changes in thiol reactivity and extractability of myofibril bound cardiac troponin C in porcine malignant hyperthermia
作者: Liou, Y.M.
劉英明
Jiang, M.J.
Wu, M.C.
關鍵字: conformational changes in cardiac troponin C (cTnC)
cysteine residues
(Cys-35 and Cys-84)
fluorescent label
malignant hyperthermia (MH)
myofibril incorporation
skeletal-muscle
ryanodine receptor
regulatory domain
susceptible
swine
calcium-binding
striated-muscle
contraction
extraction
filament
ca2+
期刊/報告no:: Journal of Biochemistry, Volume 132, Issue 2, Page(s) 317-325.
摘要: We recently showed that a shift (similar to44%) in cardiac myosin isozyme from V3 to V1 occurs in the hearts of malignant hyperthermia (MH)-susceptible pigs and may be important in the disease. To follow up this finding, we investigated whether this myosin isozyme shift results in conformational changes in cardiac troponin C (cTnC). The two cysteine residues (Cys-35 and Cys-84) in the regulatory domain of cTnC make it possible to attach conformational probes to this region. Incorporation of a fluorescent probe, 7-diethylamino-3-(4'maleimidylphenyl)-4-methylcoumairin (CPM), into myofibril-bound cTnC was measured by alkaline urea gel electrophoresis, followed by quantification of the protein and the fluorescent label on the gels. The structural stability of cTnC incorporated into cardiac myofibrils was compared between normal and MH-susceptible pigs by selective cTnC extraction and re-incorporation. Changes were detected in both the reactivity of cTnC with CPM in rigor myofibrils and cTnC incorporation into myofibrils from the hearts of MH-susceptible pigs. These changes are very likely to be a consequence of the cardiac myosin isozyme shift in the hearts of MH-susceptible pigs, which may contribute to the changes in the myofilament response to Ca2+ binding and to the modulation of cardiac contractility seen in this disease.
URI: http://hdl.handle.net/11455/38361
ISSN: 0021-924X
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