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The first step of hypertrophic cardiomyopathy pathogenesis with E99K is increased calcium sensitivity and decreased calcium cooperativity, which result in larger tension during partial activation to cause a diastolic problem.
over-inhibition of the actomyosin interaction by E40K and E54K Tm mutants leads to a decreased force-generating ability at systole, which is the main mechanism underlying the early pathogenesis of DCM.
The tendency of smooth muscle tropomyosin to form semi-rigid polymers with continuous and undampened rigidity may compensate for the lack of troponin-based structural support in smooth muscles.
Deletion of regions 2-3 in tropomyosin alpha resulted in an 60 % decrease in both isometric tension and stiffness of tropomyosin-reconstituted myocardium.
Tropomyosin is primarily responsible for the change in the kinetic constants of the elementary steps of the cross bridge cycle.
Tm affects the conformation of actin so as to increase the area of hydrophobic interaction between actin and myosin molecules
Stress fibre formation and up-regulation of alpha-smooth muscle actin (alphaSMA) induced by TGFbeta2 could be reversed by Tpm1/2 knock-down by siRNA.
The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin position.
three-dimensional structure of F-actin at a resolution of 3.7 A in complex with tropomyosin at a resolution of 6.5 A, determined by electron cryomicroscopy
data also identify a novel alphaTM1/Tmod1-based pathway stabilizing F-actin at cell-cell junctions, which may be required for maintenance of cell shapes during embryonic cardiac morphogenesis.
This is the first study to demonstrate that decreasing phosphorylation of tropomyosin can rescue a hypertrophic cardiomyopathic phenotype.
the link between flexibility of TM and its function in ejecting hearts.
Tm pseudo-phosphorylation slows deactivation of the thin filament and muscle force relaxation dynamics in the absence of dynamic and steady-state effects on muscle activation.
Tropomyosin dephosphorylation results in myocyte hypertrophy with increases in SERCA2a expression.
The results identify a novel mode of myofilament desensitization to Ca(2+) associated with a DCM linked switch in TPM1-kappa.
signaling by alpha-tropomyosin may have a role in familial hypertrophic cardiomyopathy
A point mutation in alpha-TM causes a disease similar to familial hypertophic cardiomyopahy.
PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing.
the N terminus is a critical determinant of TM1 functions, which in turn determines the organization of stress fibers.
charge changes at the carboxy-terminal of alpha-TM alter the functional characteristics of the heart at both the whole organ and myofilament levels.
Two transgenic lines of mutated alpha-TM demonstrated alterations in myocardial contractility differently.
Chronic activation of p38alpha MAPK directly depresses sarcomeric function in association with decreased phosphorylation of alpha-tropomyosin.
Developed mouse model of familial hypertrophic cardiomyopathy with a mutation in the thin filament protein alpha-tropomyosin.
M127A/I130A and M141A/Q144A do not influence the thermal unfolding and domain structure of Tpm or its actin-binding properties. They increase sliding velocity of regulated actin filaments in vitro and cause an oversensitivity of the velocity to Ca(2+). These substitutions increase bending stiffness of the coiled-coil structure of Tpm probably due to closure of the interhelical gap in the area of the substitutions.
TPM1 expression was significantly downregulated in intrahepatic cholangiocarcinoma tissues at mRNA and protein levels (P<0.001 for both). Downregulated TPM1 mRNA was negatively associated with tumor size (P=0.001) and TNM stage (P=0.007).
Missense variant (p.Leu113Val) in TPM1 causes left ventricular non-compaction with Ebstein anomaly in five members of the family.
miR-107 overexpression promoted U2OS cell viability, migration, and invasion via downregulation of TPM1 and might be through activating the MEK/ERK and NF-kappaB signaling pathways.
Functional effects of substitutions I92T and V95A in actin-binding period 3 of tropomyosin.
This study demonstrated that sarcomeric TPM1 plays vital roles in cardiogenesis and is a suitable candidate gene for screening individuals with isolated congenital heart defects .
Tpm isoforms 1.8/9 are enriched in the lamellipodium of fibroblasts as detected with a novel isoform-specific monoclonal antibody. RNAi-mediated silencing of Tpm1.8/9 led to an increase of Arp2/3 accumulation at the cell periphery and a decrease in the persistence of lamellipodia and cell motility.
TPM1-AS regulates the alternative splicing of TPM1 through an interaction with RBM4 and involves in TPM1-mediated filopodium formation and migration of cancer cells
The impact of tropomyosins on actin filament assembly is isoform specific.
TPM1 is the second gene linked to EA with LVNC in humans, implicating overlap in the molecular basis of structural and myopathic heart disease.
data demonstrate that the K15N mutation alters pointed end dynamics by affecting molecular interactions between Tpm1.1, Lmod2 and Tmod1.
Results report evidence for the existence of variants in LHFPL2 and TPM1 with low allele frequencies and large effects on age-at-onset of familial Parkinson's disease.
In diabetes, expression of high molecular weight (HMW) isoforms from tropomyosin 1 (TPM1) were markedly decreased but HMW isoforms from tropomyosin 4 (TPM4) were not significantly different.
results suggest that TPM1 can suppress tumors in oral squamous cell carcinoma, and the TPM1 expression level is related to oral squamous cell carcinoma patient prognosis
Data suggest that the tropomyosin overlap region structure and function are affected differentially by a point mutation in cardiac tropomyosin (TPM1, D230N) that is associated with dilated cardiomyopathy as compared to a point mutation in cardiac troponin T (TNNT2, R92L) that is associated with hypertrophic cardiomyopathy.
Data indicate that various hypertrophic cardiomyopathy (HCM) mutations can differently affect the structural and functional properties of tropomyosin (Tpm) and cause HCM by different molecular mechanisms.
Promoter variants in HOXA9, TPM1, and TPM2, alter promoter expression suggesting that they have a functional role in clubfoot.
The TPM1 mutations D175N and E180G increased the sliding velocity and its calcium sensitivity of the actin-myosin Interaction, while mutation E40K reduced both these parameters.
No association was observed between the remaining three markers (rs11071720, rs3803499, and rs12148828) and NSOC as well as its subgroups. TPM1 polymorphisms might contribute to the etiology ofnonsyndromic orofacial clefts (NSOC), , and more emphasis should be placed on TPM1 during craniofacial development
We show that the phosphorylation of cTnI and alphaTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not.
The results indicate that cross-linking significantly affects properties of Tpm and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm in human heart diseases.
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1
We propose that TR100 acts to compromise the integrity of Tpm cables rather than prevent overlap complex formation. Our data suggests that TR100 is incorporated into the growing actin-Tpm co-polymer given that its effects cannot be observed on pre-formed Tpm3.1/actin filaments
Maximal Ca(2+) activated force was the same in alphaalphaTm versus betabetaTm myofibrils, but betabetaTm myofibrils showed a marked slowing of relaxation and an impairment of regulation under resting conditions
Tmod1 and Tmod3 showed somewhat different tropomyosin-binding site utilization.
Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin, showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another.
The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin, was measured.
a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed.
This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy.
, alpha-tropomyosin 2
, alpha-tropomyosin of skeletal fast muscle
, tropomyosin (CTm4)
, tropomyosin (CTm7)
, tropomyosin alpha-1 chain
, tropomyosin 1 alpha chain
, alpha tropomyosin
, hepatoma alpha tropomyosin
, smooth muscle alpha-tropomyosin
, striated muscle alpha-tropomyosin
, tropomyosin 3 alpha
, alpha-skeletal tropomyosin
, cardiomyopathy, hypertrophic 3
, sarcomeric tropomyosin kappa
, tropomyosin 1 (alpha) isoform 1
, tropomyosin 1 (alpha) isoform 2
, tropomyosin 1 (alpha) isoform 3
, tropomyosin 1 (alpha) isoform 4
, tropomyosin 1 (alpha) isoform 5
, tropomyosin 1 (alpha) isoform 6
, tropomyosin 1 (alpha) isoform 7
, tropomyosin 1-1
, tropomyosin 1 (alpha)