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Myopathy-inducing mutation H40Y in ACTA1 hampers actin filament structure and function.
Our study demonstrates that high ActA level is an independent prognosis factor of survival in cancer patients. More than a basic marker of the severity of the neoplastic disease or of the inflammatory process, ActA seems to influence survival by contributing to the development of cachexia and loss of skeletal muscle mass.
The study confirmed ACTA1 mutations in four patients, including one with intranuclear rods, one with large intracytoplasmic aggregates, and two with nemaline intracytoplasmic rods.
Study shows that clinically severe ACTA1-related myopathy can present with muscle morphological findings suggestive of cytoplasmic body myopathy in the absence of definite nemaline rods.
Shorter than normal thin filament length contributes to the impaired force generation in patients with thin filament myopathy, but only in those who harbor specific mutations in NEB or ACTA1.
Over-expression of TNC, SMA, and vimentin were significantly correlated with the lower overall survival in prostate cancer patients.
ANA and ASMA evaluation in patients with liver transplantation and no history of autoimmune disease has no clinical relevance, since it varies in time and is not related to any risk factors or liver injury. Routine autoimmunity evaluation should be avoided.
Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the vinculin tail helical bundle to mediate actin bundling.
This study reported the new information on the frequency and phenotypes of congenital myopathy caused by ACTA1 mutations in subjects >/=5 years of age.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Mutations in ACTA1 can cause pathologic features consistent with myofibrillar myopathy.
TIMP-1 significantly increased levels of alpha-SMA.
novel homozygous recessive missense variant (c.460G>C, P.(Val154Leu)) was found in two brothers with infantile-onset congenital muscular dystrophy with rigid spine.
Myopathy associated with zebra bodies is part of the spectrum of myopathies associated with the ACTA1 gene.
New scapuloperoneal phenotype associated with an ACTA1 mutation.
Antisynthetase syndrome-associated myositis is characterized by distinctive myonuclear actin filament inclusions.
The predominant pathway mediated by Australian bat lyssavirus G envelope for internalization into HEK293T cells is clathrin-and actin-dependent also requiring Rab5.
Data show that the width and speed of the waves depend counter-intuitively on parameters, negative feedback, and the F-actin time scale.
Although most cases of severe infantile form of nemaline myopathy caused by ACTA1 mutations are sporadic and have no family history
These findings suggest that the direct contact of Dengue virus 2 E protein with 43 kDa actin protein may have a crucial function in Dengue virus 2 infection of ECV304 cells.
Titin-actin interaction: PEVK-actin-based viscosity in a large animal.
alpha smooth muscle actin (alphaSMA) was identified as a marker of osteoprogenitor cells in bone and periodontium.
WIP is a link between membrane lipid composition and actin cytoskeleton at dendritic spines.
ACTA1(Asp286Gly) mouse model of nemaline myopathy provide evidence of impaired in vivo muscle function, altered muscle structure and disturbed energy metabolism.
Combined MRI and (3)(1)P-MRS investigations of the ACTA1(H40Y) mouse model of nemaline myopathy show impaired muscle function and altered energy metabolism.
Data indicate roles for linkers of nucleus to cytoskeleton (LINC) molecules nesprin2giant and nesprin3, which anchor actin cap fibers to the nucleus.
Asp286Gly acts as a "poison-protein" and according to the computational analysis it modifies the actin-actin interface. This phenomenon is likely to prevent proper myosin cross-bridge binding.
Data show that upon actin binding, the two domains of utrophin become dramatically separated and ordered, indicating a transition to a single open and extended conformation.
Data indicated that CacyBP/SIP could simultaneously interact with tubulin and actin, suggesting that CacyBP/SIP might link actin and tubulin cytoskeletons.
Results provide the genetic proof that platelet production from megakaryocytes strictly requires dynamic changes in the actin cytoskeleton.
Data show that while increases in cardiac and vascular smooth-muscle actin can partially compensate for the lack of skeletal actin in null mice, this is not sufficient to support adequate skeletal muscle growth and/or function.
alpha-skeletal-muscle actin mutations have roles in development of myopathies
myotome pairs are transiently left-right asymmetric, with higher expression of alpha-skeletal actin and myosin light chain 3F (MLC3F) on the left side between embryonic day 9.5-10.25.
K+-depolarization increased Tnni1 and Acta1 mRNA levels in both differentiated C2C12 and rat skeletal muscle cells in primary culture
Myotubes are a suitable system to study the capacity of a mutant to incorporate into actin structures or to form or induce pathological changes.
Val163Met mutation in alpha-skeletal actin can affect the dynamics of other actin isoforms and severely disrupt sarcomeric structure, processes that can contribute to muscle weakness.
F- and G-actin concentrations in lamellipodia are about 500 microM & 150 microM, respectively. The excess of G-actin shows that the polymerization rate is not limited by diffusion & is tightly controlled by polymerization/depolymerization modulators.
A genetic actc1b mutant exhibits mild muscle defects and is unaffected by injection of the actc1b targeting morpholino. The milder phenotype results from a compensatory transcriptional upregulation of an actin paralogue providing a novel approach to be explored for the treatment of actin myopathy. These findings provide further evidence that genetic compensation may influence the penetrance of disease-causing mutations.
Data show that local actin monomer depletion and network architecture can tune the rate of network growth to impose steering during motility.
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.
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
Structure of a Bud6/Actin complex reveals a novel wh2-like actin monomer recruitment motif.
Data suggest that toxofilin has two actin binding sites, and and the affinities of these actin binding sites are identical or very close to each other.
The activation of vinculin by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin association.
The product encoded by this gene belongs to the actin family of proteins, which are highly conserved proteins that play a role in cell motility, structure and integrity. Alpha, beta and gamma actin isoforms have been identified, with alpha actins being a major constituent of the contractile apparatus, while beta and gamma actins are involved in the regulation of cell motility. This actin is an alpha actin that is found in skeletal muscle. Mutations in this gene cause nemaline myopathy type 3, congenital myopathy with excess of thin myofilaments, congenital myopathy with cores, and congenital myopathy with fiber-type disproportion, diseases that lead to muscle fiber defects.
actin, alpha skeletal muscle
, nemaline myopathy type 3
, alpha actin 1
, skeletal alpha actin
, alpha 1 skeletal muscle actin
, actin alpha 1
, actin, alpha 1, skeletal muscle
, actin, alpha, cardiac muscle 1
, Actin, alpha skeletal muscle
, LOW QUALITY PROTEIN: actin, alpha skeletal muscle
, cytoplasmic beta-actin
, actin, muscle
, skeletal alpha-actin
, skeletal muscle alpha-actin