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Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
Gene References into Functions
Rationally engineered TnC constructs corrected the abnormal Ca(2+) sensitivities of the thin filament, reconstituted actomyosin ATPase activityPMID:22511780
Molecular effects of cardiac troponin C mutations present in hypertrophic cardiomyopathy on calcium sensitivity and myofilament activation have been reported.PMID:27133568
Study shows that over-expression of MFAP5 and TNNC1 is correlated with cervical lymph node metastasis (CLNM), metastasis relapse-free survival and overall survival. These results propose that MFAP5 and TNNC1 may be potential markers for predicting occult cervical lymphatic metastasis and prognosis of oral tongue carcinoma.PMID:27713166
Our results (i) confirm that genetic backgrounds of hypertrophic cardiomyopathy and restrictive cardiomyopathy overlap and (ii) indicate that TNNC1 is a likely novel gene for autosomal recessive restrictive cardiomyopathy.PMID:27604170
Data suggest that modulation of structural dynamics far from the regulatory Ca2+-binding site is the underlying molecular mechanism for many TNNC1 mutations in patients with hypertrophic cardiomyopathies or familial hypertrophic cardiomyopathies; many mutations affect balance between open and closed conformations; troponin I switch peptide [TnI(SW)] switch peptide binds to TNNC1 and stabilizes the open TNNC1 conformation.PMID:28533433
Data suggest that mutations in troponin C (TnC) found in patients with hypertrophic cardiomyopathy (A8V, C84Y, and D145E) stabilize the active state of regulated actin (the actin-tropomyosin-troponin complex) to various extents; at a saturating Ca2+ concentration, all TnC mutants investigated increase the level of active M state compared to the wild type.PMID:28530094
There was no difference in the test characteristics of the HEART Pathway whether using cTnI or hs-cTnI, with both achieving 100% sensitivity and NPV. Use of hs-cTnT with the HEART Pathway was associated with one missed major adverse cardiac events.PMID:28087371
contractility is constantly above normal in hearts made hypertrophic by TnC with the A8V mutationPMID:26976709
We used nuclear magnetic resonance and circular dichroism to solve the structure and characterize the backbone dynamics and stability of the regulatory domain of cTnC with the L29Q mutation.PMID:26341255
conclusive evidence that TNNC1 is an uncommon but definitive HCM-susceptibility genePMID:26304555
Troponin C (TnC) and the N-terminal helix of Troponin I (TnI N-helix), which occurs in vivo during muscle contraction.PMID:26111167
FAK/CREB/TNNC1 has a role in mediating the effect of stromal MFAP5 on ovarian cancer metastatic potentialPMID:25277212
Mutations in cTnC have been associated with hypertrophic or dilated cardiomyopathy.[review]PMID:26232335
Data suggest that mutation A162H in switch region of troponin I induces transitory curved conformation and promotes contraction of troponin I bound to regulatory domain of troponin C; this is countered by residue E164 to ensure proper relaxation.PMID:25996354
in vitro characterisation of six cardiac Troponin C mutations causing hypertrophic and dilated cardiomyopathies (Review)PMID:24744096
The conformational dynamics of N-terminal lobe of TnC plays an important role in the regulation of cardiac muscle contraction.PMID:25101951
Data indicate that domain positioning impacts the effective concentration of cardiac isoform of troponin I (cTnI) presented to cardiac troponin C (cTnC).PMID:25246568
Toponin I, T, and C play crucial roles in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction. [review]PMID:24490734
Central helix point mutations decreased affinity of Ca2+ saturated cardiac TNC for TnI128-180.PMID:24650606
The structure of cardiac troponin C regulatory domain with bound Cd2+ reveals a closed conformation and unique ion coordination.PMID:23633581
Calcium induced regulation of skeletal troponin--computational insights from molecular dynamics simulations.PMID:23554884
calcium binding to the regulatory site of human cardiac troponin CPMID:23111626
Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy.PMID:23066014
a novel mutation in the TNNC1 gene is associated with HCM pathogenesis and may predispose to the pathogenesis of a fatal arrhythmogenic subtype of HCMPMID:22815480
The study examines TNC for its ability of binding Ca2+ and furthermore determines the molecular contributions to Ca2+ binding kinetics.PMID:22329450
The L48Q mutation enhanced binding of both Ca(2+) and troponin I to cardiac troponin C.PMID:22591429
The disease-related protein modifications alter Ca(2+) binding by influencing both the association and dissociation rates of thin filament Ca(2+) exchange.PMID:22675533
Cardiomyopathy-linked TnC mutations affect the response of reconstituted thin filaments to calcium upon cardiac troponin (Tn)I phosphorylation.PMID:22489623
Functional characterization of TNNC1 rare variants identified in dilated cardiomyopathy.PMID:21832052
strong cross-bridges potentiate the Ca(2+)-sensitizing effect of hypertrophic cardiomyopathy-cTnC mutants on the myofilamentPMID:21056975
analysis of order and disorder in troponin C, T and IPMID:20889975
A region in cTnC associated with increased Ca(2+) sensitivity in skinned fibers was identified, an the F27W reporter mutation affected Ca(2+) sensitivity, maximal force, and ATPase activation of some mutants.PMID:20566645
plasma levels are associated with degree of vascular obstruction in patients with pulmonary embolismPMID:19492165
Calcium binding properties of the carboxy terminal-domain sites might be important for the proper regulatory function of cardiac troponin C.PMID:20459070
Four private protein-altering variants were identified in troponin C type 1 in 4 probands.PMID:20215591
After acute myocardial infarction, cTnI is present in serum as the ternary cTnT-cTnI-TnC (TIC) complex and binary cTnI-TnC (IC) complex.PMID:20378771
the dilated cardiomyopathy troponin C mutation lowers contractile force by reducing strong myosin-actin bindingPMID:20371872
The intrinsic properties of TnC and its interactions with other contractile proteins play a crucial role in modulating the binding of calcium to TnC in increasingly complex biochemical systems.PMID:20128626
cardiac troponin switches between alternative sets of intramolecular interactions, similar to previous intermediate resolution x-ray data of skeletal muscle troponinPMID:19920153
Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I.PMID:12732641
Data suggest that activation of cardiac myofilaments is tightly coupled to the open state of the N-domain of cardiac troponin C, and that pathological effects of phosphorylation are influenced by mutations in cardiac troponin I.PMID:15147183
CTnI mutations mainly alter myocardial performance via changes in the Ca2+ -sensitivity of force development and in some cases alter the muscle relaxation kinetics. Review.PMID:15524171
C helix moves away from the D helix in a distinct Ca(2+)-dependent manner, while the B helix does not.PMID:15628883
Results describe the in situ structure of human cardiac troponin C.PMID:15808858
The crystal structure of troponin suggests that the Ca2+-binding to the regulatory TnC site displaces the N-terminal portion of TnI from actin/tropomyosin, thereby altering mobility/flexibility of the troponin/tropomyosin strand on the actin filament.PMID:16157639
Spin dipole-dipole interaction showed that in reconstituted muscle fibers both skeletal and cardiac TnC undergo Ca2+-induced structural change that is thought to be TnIreg movement.PMID:16157641
Results imply a hindered transduction of the protein kinase A phosphorylation signal from cardiac troponin I to troponin C.PMID:16302972
the mutation Gly159Asp causes a significant decrease in the rate of force production and a change in the relationship between the rate of force production and generated force in musclePMID:17021793
in the presence of phosphorylated cTnI, cTnC-G159D specifically blunted phosphorylation induced decrease in Ca(2+)-sensitive tension development without altering cross-bridge cycling in cardiac myofilamentPMID:17446435
Suggest that TnC Ca(2+) binding properties modulate the rate of cardiac muscle contraction at submaximal levels of Ca(2+) activation.PMID:17693547