A cardiac troponin T epitope conserved across phyla.

Malouf, Nadia N.; Mcmahon, Debra K.; Oakeley, A. E.; Anderson, Page A.W.

doi:10.1016/s0021-9258(19)50418-5

Cited by 52 publications

(3 citation statements)

References 35 publications

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“…The cardiac troponins are found in high concentrations in the myocardium of most vertebrates. Epitopes of these proteins are conserved in the troponin structure across a number of phyla (Malouf et al, 1992). Investigations by Berson et al (1978) also showed that cTnI appeared to have similar molecular weights but different isoeletric points among mammalian species.…”

Section: Bridge Between Speciesmentioning

confidence: 97%

“…However, the subsequent 28 amino acid residues are unique to cTnT. Studies in a variety of different mammals have found that the epitopes of the cTnT and cTnI proteins are strongly conserved across a broad range of animal species, including species that are commonly employed in nonclinical toxicity testing (Berson et al, 1978;Malouf et al, 1992;O'Brien et al, 1998).…”

Section: Distribution and Intracellular Turnover Of Cardiac Troponin T And Imentioning

confidence: 99%

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Serum Troponins as Biomarkers of Drug-Induced Cardiac Toxicity

et al. 2004

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Section: Bridge Between Speciesmentioning

confidence: 97%

Section: Distribution and Intracellular Turnover Of Cardiac Troponin T And Imentioning

confidence: 99%

Serum Troponins as Biomarkers of Drug-Induced Cardiac Toxicity

et al. 2004

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“…This higher-than-expected MW may reflect cTnT having a highly acidic N-terminal region which has been suggested to alter the binding of negatively charged SDS. Western blots, using a cTnT-specific monoclonal antibody (26), demonstrated a single band (results not shown).…”

Section: Resultsmentioning

confidence: 92%

Cardiac Troponin T Forms a Tetramer in Vitro

et al. 2008

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Cardiac troponin T (cTnT) is a myofibrillar protein essential for calcium-dependent contraction. This property has led to functional studies of developmentally expressed cTnT isoforms and mutants identified in patients with hypertrophic cardiomyopathy. The release of cTnT into the serum following myocardial infarction has led to the development of antibody-based assays for measuring cTnT serum concentration. We examined the behavior of cTnT in solution. Recombinant human cTnT3, the dominant isoform in the adult human heart, was used. The protein was pure and functional, as demonstrated by SDS-PAGE and surface plasmon resonance. cTnT3 was found to bind specifically and in a concentration-dependent manner to cTnC. Routine size exclusion chromatography suggested a higher-than-expected MW for cTnT. Using analytical ultracentrifugation, we found cTnT3 in solution to be mainly in the form of a tightly bound tetramer at concentrations as low as 4 micromol/L. Our sedimentation velocity and transmission electron microscopy results indicate that the tetramer's shape is elongated rather than globular. CTnT's self-association in solution is an important consideration in the design and interpretation of experiments with the aim of understanding the biochemical and biophysical properties of cTnT, its isoforms, and its mutants.

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Comparative studies on the expression patterns of three troponin T genes during mouse development

et al. 2001

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In vertebrates, three troponin T (TnT) genes, cardiac TnT (cTnT), skeletal muscle fast-twitch TnT (fTnT), and slow-twitch TnT (sTnT), have evolved for the regulation of striated muscle contraction. To understand the mechanism for muscle fiber-specific expression of the TnT genes, we compared their expression patterns during mouse development. Our data revealed that the TnT expression in the developing embryo was not as restricted as that in the adult. In addition to a strong expression in the developing heart beginning at day 7.5 p.c (postcoitum), the cTnT transcript was detected at later stages in some skeletal muscles, where beginning at day 11.75 p.c. the fTnT and sTnT genes were also expressed. Only sTnT but not fTnT was found transiently in the developing heart. At day 13.5 p.c., expressions of all three genes were detected in the developing tongue and this co-expression continued to day 16.5 p.c. with the fTnT isoform being predominant. At this stage, overlapping and distinct expression patterns of both sTnT and fTnT genes were also evident in many developing skeletal muscles. These data suggest that different muscles during development undergo a complex change in TnT isoforms resulting in different contractile properties. Unexpectedly, the cTnT transcript was persistently found in the developing bladder, where presumably smooth muscle is present. In transgenic mice, expression of a LacZ gene driven by a rat cTnT promoter (Ϫ497 to ϩ192 bp) was very similar to that of the endogenous cTnT gene, suggesting that this promoter contained regulatory elements sufficient for the control of tissue-specific cTnT expression during development. Anat Rec 263: [72][73][74][75][76][77][78][79][80][81][82][83][84] 2001.

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A cardiac troponin T epitope conserved across phyla.

Cited by 52 publications

References 35 publications

Serum Troponins as Biomarkers of Drug-Induced Cardiac Toxicity

Serum Troponins as Biomarkers of Drug-Induced Cardiac Toxicity

Cardiac Troponin T Forms a Tetramer in Vitro

Comparative studies on the expression patterns of three troponin T genes during mouse development

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