Structure and proteolytic susceptibility of the inhibitory C-terminal tail of cardiac troponin I

• Published in: Biochimica et biophysica acta. General subjects Vol. 1863; no. 4; pp. 661 - 671
• Main Authors: Mahmud, Zabed, Zahran, Somaya, Liu, Philip B., Reiz, Bela, Chan, Brandon Y.H., Roczkowsky, Andrej, McCartney, Christian-Scott E., Davies, Peter L., Li, Liang, Schulz, Richard, Hwang, Peter M.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2019
• Subjects: actin; biomarkers; calcium; Calpain; cardiomyocytes; Escherichia coli; gelatinase A; Intrinsically disordered protein; Ischemia-reperfusion injury; liquid chromatography; Mass spectrometry; Matrix metalloproteinase-2; muscle contraction; Myocardial infarction; Myocardial stunning; Nuclear magnetic resonance (NMR) spectroscopy; nuclear magnetic resonance spectroscopy; proteolysis; troponin C; troponin I; Myocardial infarction; Ischemia-reperfusion injury; Myocardial stunning; Nuclear magnetic resonance (NMR) spectroscopy; Matrix metalloproteinase-2; Calpain; Intrinsically disordered protein; Mass spectrometry

Cardiac troponin I (cTnI) has two flexible tails that control the cardiac cycle. The C-terminal tail, cTnI135–209, binds actin to shut off cardiac muscle contraction, whereas the competing calcium-dependent binding of the switch region, cTnI146–158, by cardiac troponin C (cTnC) triggers contraction....