The amino acid sequence of human cardiac troponin-C

1986 ◽  
Vol 9 (1) ◽  
pp. 73-77 ◽  
Author(s):  
Alex Roher ◽  
Norman Lieska ◽  
Werner Spitz
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cardiac Troponin ◽  
Troponin C ◽  
Cardiac Troponin C ◽  
Human Cardiac Troponin C

Sequence mutations in teleost cardiac troponin C that are permissive of high Ca2+ affinity of site II

2003 ◽  
Vol 284 (5) ◽  
pp. C1176-C1184 ◽  
Author(s):  
Todd E. Gillis ◽  
Chris D. Moyes ◽  
Glen F. Tibbits
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cardiac Troponin ◽  
Troponin C ◽  
Fluorescent Reporter ◽  
Cardiac Troponin C ◽  
The Difference ◽  
Higher Sensitivity

Cardiac myofibrils isolated from trout heart have been demonstrated to have a higher sensitivity for Ca2+ than mammalian cardiac myofibrils. Using cardiac troponin C (cTnC) cloned from trout and mammalian hearts, we have previously demonstrated that this comparatively high Ca2+ sensitivity is due, in part, to trout cTnC (ScTnC) having twice the Ca2+ affinity of mammalian cTnC (McTnC) over a broad range of temperatures. The amino acid sequence of ScTnC is 92% identical to McTnC. To determine the residues responsible for the high Ca2+ affinity, the function of a number of ScTnC and McTnC mutants was characterized by monitoring an intrinsic fluorescent reporter that monitors Ca2+ binding to site II (F27W). The removal of the COOH terminus (amino acids 90–161) from ScTnC and McTnC maintained the difference in Ca2+ affinity between the truncated cTnC isoforms (ScNTnC and McNTnC). The replacement of Gln29 and Asp30 in ScNTnC with the corresponding residues from McNTnC, Leu and Gly, respectively, reduced Ca2+ affinity to that of McNTnC. These results demonstrate that Gln29 and Asp30 in ScTnC are required for the high Ca2+ affinity of site II.

Increasing mammalian cardiomyocyte contractility with residues identified in trout troponin C

2005 ◽  
Vol 22 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Todd E. Gillis ◽  
Bo Liang ◽  
Franca Chung ◽  
Glen F. Tibbits
Keyword(s):  
Amino Acid ◽  
Cardiac Myocytes ◽  
Cardiac Troponin ◽  
Troponin C ◽  
Force Generation ◽  
Wild Type ◽  
Cardiac Troponin C ◽  
Cardiomyocyte Contractility

The Ca2+ sensitivity of force generation in trout cardiac myocytes is significantly greater than that from mammalian hearts. One mechanism that we have suggested to be responsible, at least in part, for this high Ca2+ sensitivity is the isoform of cardiac troponin C (cTnC) found in trout hearts (ScTnC), which has greater than twice the Ca2+ affinity of mammalian cTnC (McTnC). Here, through a series of mutations, the residues in ScTnC responsible for its high Ca2+ affinity have been identified as being Asn2, Ile28, Gln29, and Asp30. When these residues in McTnC were mutated to the trout-equivalent amino acid, the Ca2+ affinity of the molecule, determined by monitoring the fluorescence of a Trp inserted for a Phe at residue 27, is comparable to that of ScTnC. To determine how a McTnC mutant containing Asn2, Ile28, Gln29, and Asp30 (NIQD McTnC) affects the Ca2+ sensitivity of force generation, endogenous cTnC in single, chemically skinned rabbit cardiomyocytes was replaced with either wild-type McTnC or NIQD McTnC. Our results demonstrate that the cardiomyocytes containing NIQD McTnC were approximately twice as sensitive to Ca2+, illustrating that a McTnC mutant with similar Ca2+ affinity as ScTnC can be used to sensitize mammalian cardiac myocytes to Ca2+.

Calcium-Induced Structural Transition in the Regulatory Domain of Human Cardiac Troponin C†,‡

Biochemistry ◽  
1997 ◽  
Vol 36 (40) ◽  
pp. 12138-12146 ◽  
Author(s):  
Leo Spyracopoulos ◽  
Monica X. Li ◽  
Samuel K. Sia ◽  
Stéphane M. Gagné ◽  
Murali Chandra ◽  
...  
Keyword(s):  
Cardiac Troponin ◽  
Structural Transition ◽  
Troponin C ◽  
Regulatory Domain ◽  
Cardiac Troponin C ◽  
Human Cardiac Troponin C

A peptide hydrogel derived from a fragment of human cardiac troponin C

2016 ◽  
Vol 52 (21) ◽  
pp. 4056-4059 ◽  
Author(s):  
Luis M. De Leon-Rodriguez ◽  
Meder Kamalov ◽  
Yacine Hemar ◽  
Alok K. Mitra ◽  
Valeria Castelletto ◽  
...  
Keyword(s):  
Cardiac Troponin ◽  
Troponin C ◽  
Peptide Fragment ◽  
C Peptide ◽  
Cardiac Troponin C ◽  
Β Sheets ◽  
Human Cardiac Troponin C ◽  
Peptide Hydrogel

The human cardiac troponin C peptide fragment H-V9EQLTEEQKNEFKAAFDIFVLGA31-OH self assembles into β-sheets fibrils that further entangle to give a hydrogels.

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