A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.
A form of creatine kinase found in the BRAIN.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.

Gamma-Actinin, a new regulatory protein from rabbit skeletal muscle. I. Purification and characterization. (1/917)

A new regulatory protein which we have designated as gamma-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40--60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified gamma-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of gamma-actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of gamma-actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of gamma-actinin with F-actin showed that gamma-actinin binds to F-action.  (+info)

Polypyrimidine tract binding protein functions as a repressor to regulate alternative splicing of alpha-actinin mutally exclusive exons. (2/917)

The smooth muscle (SM) and nonmuscle (NM) isoforms of alpha-actinin are produced by mutually exclusive splicing of an upstream NM exon and a downstream SM-specific exon. A rat alpha-actinin genomic clone encompassing the mutually exclusive exons was isolated and sequenced. The SM exon was found to utilize two branch points located 382 and 386 nucleotides (nt) upstream of the 3' splice site, while the NM exon used a single branch point 191 nt upstream. Mutually exclusive splicing arises from the proximity of the SM branch points to the NM 5' splice site, and this steric repression could be relieved in part by the insertion of spacer elements. In addition, the SM exon is repressed in non-SM cells and extracts. In vitro splicing of spacer-containing transcripts could be activated by (i) truncation of the transcript between the SM polypyrimidine tract and exon, (ii) addition of competitor RNAs containing the 3' end of the actinin intron or regulatory sequences from alpha-tropomyosin (TM), and (iii) depletion of the splicing extract by using biotinylated alpha-TM RNAs. A number of lines of evidence point to polypyrimidine tract binding protein (PTB) as the trans-acting factor responsible for repression. PTB was the only nuclear protein observed to cross-link to the actinin RNA, and the ability of various competitor RNAs to activate splicing correlated with their ability to bind PTB. Furthermore, repression of alpha-actinin splicing in the nuclear extracts depleted of PTB by using biotinylated RNA could be specifically restored by the addition of recombinant PTB. Thus, alpha-actinin mutually exclusive splicing is enforced by the unusual location of the SM branch point, while constitutive repression of the SM exon is conferred by regulatory elements between the branch point and 3' splice site and by PTB.  (+info)

Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: evidence that thin filaments rearrange to form striated myofibrils. (3/917)

Actin filament lengths in muscle and nonmuscle cells are believed to depend on the regulated activity of capping proteins at both the fast growing (barbed) and slow growing (pointed) filament ends. In striated muscle, the pointed end capping protein, tropomodulin, has been shown to maintain the lengths of thin filaments in mature myofibrils. To determine whether tropomodulin might also be involved in thin filament assembly, we investigated the assembly of tropomodulin into myofibrils during differentiation of primary cultures of chick skeletal muscle cells. Our results show that tropomodulin is expressed early in differentiation and is associated with the earliest premyofibrils which contain overlapping and misaligned actin filaments. In addition, tropomodulin can be found in actin filament bundles at the distal tips of growing myotubes, where sarcomeric alpha-actinin is not always detected, suggesting that tropomodulin caps actin filament pointed ends even before the filaments are cross-linked into Z bodies by alpha-actinin. Tropomodulin staining exhibits an irregular punctate pattern along the length of premyofibrils that demonstrate a smooth phalloidin staining pattern for F-actin. Strikingly, the tropomodulin dots often appear to be located between the closely spaced, dot-like Z bodies that are stained for (&agr;)-actinin. Thus, in the earliest premyofibrils, the pointed ends of the thin filaments are clustered and partially aligned with respect to the Z bodies (the location of the barbed filament ends). At later stages of differentiation, the tropomodulin dots become aligned into regular periodic striations concurrently with the appearance of striated phalloidin staining for F-actin and alignment of Z bodies into Z lines. Tropomodulin, together with the barbed end capping protein, CapZ, may function from the earliest stages of myofibrillogenesis to restrict the lengths of newly assembled thin filaments by capping their ends; thus, transitions from nonstriated to striated myofibrils in skeletal muscle are likely due principally to filament rearrangements rather than to filament polymerization or depolymerization. Rearrangements of actin filaments capped at their pointed and barbed ends may be a general mechanism by which cells restructure their actin cytoskeletal networks during cell growth and differentiation.  (+info)

An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment. (4/917)

The LIM domain protein zyxin is a component of adherens type junctions, stress fibers, and highly dynamic membrane areas and appears to be involved in microfilament organization. Chicken zyxin and its human counterpart display less than 60% sequence identity, raising concern about their functional identity. Here, we demonstrate that human zyxin, like the avian protein, specifically interacts with alpha-actinin. Furthermore, we map the interaction site to a motif of approximately 22 amino acids, present in the N-terminal domain of human zyxin. This motif is both necessary and sufficient for alpha-actinin binding, whereas a downstream region, which is related in sequence, appears to be dispensable. A synthetic peptide comprising human zyxin residues 21-42 specifically binds to alpha-actinin in solid phase binding assays. In contrast to full-length zyxin, constructs lacking this motif do not interact with alpha-actinin in blot overlays and fail to recruit alpha-actinin in living cells. When zyxin lacking the alpha-actinin binding site is expressed as a fusion protein with green fluorescent protein, association of the recombinant protein with stress fibers is abolished, and targeting to focal adhesions is grossly impaired. Our results suggest a crucial role for the alpha-actinin-zyxin interaction in subcellular zyxin localization and microfilament organization.  (+info)

Viscoelastic properties of f-actin, microtubules, f-actin/alpha-actinin, and f-actin/hexokinase determined in microliter volumes with a novel nondestructive method. (5/917)

A nondestructive method to determine viscoelastic properties of gels and fluids involves an oscillating glass fiber serving as a sensor for the viscosity of the surrounding fluid. Extremely small displacements (typically 1-100 nm) are caused by the glass rod oscillating at its resonance frequency. These displacements are analyzed using a phase-sensitive acoustic microscope. Alterations of the elastic modulus of a fluid or gel change the propagation speed of a longitudinal acoustic wave. The system allows to study quantities as small as 10 microliters with temporal resolution >1 Hz. For 2-100 microM f-actin gels a final viscosity of 1.3-9.4 mPa s and a final elastic modulus of 2.229-2.254 GPa (corresponding to 1493-1501 m/s sound velocity) have been determined. For 10- to 100-microM microtubule gels (native, without stabilization by taxol), a final viscosity of 1.5-124 mPa s and a final elastic modulus of 2.288-2. 547 GPa (approximately 1513-1596 m/s) have been determined. During polymerization the sound velocity in low-concentration actin solutions increased up to +1.3 m/s (approximately 1.69 kPa) and decreased up to -7 m/s (approximately 49 kPa) at high actin concentrations. On polymerization of tubulin a concentration-dependent decrease of sound velocity was observed, too (+48 to -12 m/s approximately 2.3-0.1 MPa, for 10- to 100-microM tubulin). This decrease was interpreted by a nematic phase transition of the actin filaments and microtubules with increasing concentration. 2 mM ATP (when compared to 0.2 mM ATP) increased polymerization rate, final viscosity and elastic modulus of f-actin (17 microM). The actin-binding glycolytic enzyme hexokinase also accelerated the polymerization rate and final viscosity but elastic modulus (2.26 GPa) was less than for f-actin polymerized in presence of 0.2 mM ATP (2.28 GPa).  (+info)

Cardiac microvascular endothelial cells express alpha-smooth muscle actin and show low NOS III activity. (6/917)

We established a culture system of porcine coronary microvascular endothelial cells (MVEC) with high cellular yield and purity >98%. Endothelial origin was confirmed by immunostaining, immunoblotting and fluorescence-activated cell sorter (FACS) analysis using low-density lipoprotein uptake, CD31, von Willebrand factor, and the lectin Dolichos biflorus agglutinin. MVEC were positive for alpha-smooth muscle actin in culture and in myocardium, as confirmed by FACS. Of the primary MVEC, approximately 30% expressed nitric oxide synthase (NOS) III in numbers decreasing from the first passage (6 +/- 1%) to the second passage (4 +/- 1%; P < 0.001 vs. primary isolates), whereas approximately 100% of aortic endothelial cells (AEC) expressed NOS III. In AEC, NOS III activity (pmol citrulline. mg protein-1. min-1) was 80 +/- 10 and was nearly abolished in the absence of calcium (5 +/- 1, P < 0.001). In primary MVEC, however, NOS III activity in the presence and absence of calcium was 20 +/- 4 and 25 +/- 5, respectively. We conclude that cardiac MVEC, in contrast to AEC, contain alpha-smooth muscle actin, show low-grade NOS III activity, and provide a suitable in vitro system for the study of endothelial pathophysiology.  (+info)

Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy. (7/917)

The striated muscle sarcomeres are highly organized structures composed of actin (thin) and myosin (thick) filaments that slide past each other during contraction. The integrity of sarcomeres is controlled by a set of structural proteins, among which are titin, a giant molecule that contains several immunoglobulin (Ig)-like domains and associates with thin and thick filaments, and [alpha]-actinin, an actin cross-linking protein. Mutations in several sarcomeric and sarcolemmal proteins have been shown to result in muscular dystrophy and cardiomyopathy. On the other hand, the disease genes underlying several disease forms remain to be identified. Here we describe a novel 57 kDa cytoskeletal protein, myotilin. Its N-terminal sequence is unique, but the C-terminal half contains two Ig-like domains homologous to titin. Myotilin is expressed in skeletal and cardiac muscle, it co-localizes with [alpha]-actinin in the sarcomeric I--bands and directly interacts with [alpha]-actinin. The human myotilin gene maps to chromosome 5q31 between markers AFM350yB1 and D5S500. The locus of a dominantly inherited limb-girdle muscular dystrophy (LGMD1A) resides in an overlapping narrow segment, and a new type of distal myopathy with vocal cord and pharyngeal weakness (VCPMD) has been mapped to the same locus. The muscle specificity and apparent role as a sarcomeric structural protein raise the possibility that defects in the myotilin gene may cause muscular dystrophy.  (+info)

Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. (8/917)

The present experiment was conducted to determine whether calpastatin inhibits only the rate, or both the rate and extent, of calpain-induced postmortem proteolysis. Biceps femoris from normal (n = 6) and callipyge (n = 6) lamb was stored for 56 d at 4 degrees C. Calpastatin activity was higher (P < .05) in the callipyge muscle at 0 and 14 d postmortem, but not at 56 d postmortem. The activity of mu-calpain did not differ between normal and callipyge biceps femoris at 0 and 56 d postmortem (P > .05), but was higher at 14 d postmortem in the callipyge muscle (P < 0.05). The activity of m-calpain was higher in the callipyge muscle (P < 0.05). Western blot analyses of titin, nebulin, dystrophin, myosin heavy chain, vinculin, alpha-actinin, desmin, and troponin-T indicated that postmortem proteolysis was less extensive in callipyge than in normal biceps femoris at all postmortem times. The results of this experiment indicate that calpastatin inhibits both the rate and extent of postmortem proteolysis.  (+info)

alpha Actinin ELISA Kits für viele Reaktivitäten. Huhn, Rind (Kuh), Hund und weitere. alpha Actinin ELISA Kits vergleichen und bestellen.
购买alpha Actinin 4兔多克隆抗体(ab117411),alpha Actinin 4抗体经WB,ELISA验证,可与人,小鼠,大鼠,Monkey样本反应。中国现货速达。
University of Helsinki, Faculty of Biosciences, Department of Biological and Environmental Sciences, Division of genetics and Institute of Biotechnology. The actin cytoskeleton is essential for a large variety of cell biological processes. Actin exists in either a monomeric or a filamentous form, and it is very important for many cellular functions that the local balance between these two actin populations is properly regulated. A large number of proteins participate in the regulation of actin dynamics in the cell, and twinfilin, one of the proteins examined in this thesis, belongs to this category. The second level of regulation involves proteins that crosslink or bundle actin filaments, thereby providing the cell with a certain shape. α-Actinin, the second protein studied, mainly acts as an actin crosslinking protein. Both proteins are conserved in organisms ranging from yeast to mammals. In this thesis, the roles of twinfilin and α-actinin in development were examined using Drosophila ...
References for Abcams Recombinant Human Sarcomeric Alpha Actinin protein (ab92234). Please let us know if you have used this product in your publication
Anti-Sarcomeric Alpha Actinin antibody [EA-53] (ab9465) has been cited in 63 publications. References for Human, Mouse, Rat, Goat, Pig, Xl, Xp in Flow Cyt…
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Mouse Monoclonal Anti-Alpha Actinin 4 Antibody (4D10) [DyLight 488]. Validated: WB, ELISA, ICC/IF, IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat. 100% Guaranteed.
ウサギ・ポリクローナル抗体 ab59468 交差種: Ms,Hu 適用: WB,IHC-P,ICC/IF…alpha Actinin 4抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
Ni-NTA magnetic agarose beads (Qiagen, Valencia, CA) were used to immobilize histidine-tagged proteins in binding assays performed according to the manufacturers protocol. In brief, 30 μg of histidine-tagged recombinant proteins (His-N-RAP-SR, His-N-RAP-LIM, His-N-RAP-IB, His-CAT) were incubated with 100 μl of Ni-NTA magnetic agarose beads for 1.5 hours at room temperature under denaturing conditions (8 M urea, 0.1 M NaH2PO4, 0.01 M Tris-Cl, 0.005% Tween 20, pH 8.0). The recombinant proteins immobilized on the Ni-NTA matrix were renatured by sequential incubations in 4 M, 2 M, 1 M, and 0 M urea in phosphate buffer (0.1 M NaH2PO4, 0.01 M Tris-Cl, 0.005% Tween 20, pH 8.0) over a period of 2 hours. They were then incubated with potentially interacting biomolecules (Krp1, filamin or α-actinin) at final monomer concentrations of 2.5 μg/ml (0.037 μM), 33 μg/ml (0.13 μM) and 33μg/ml (0.33 μM), respectively. Purified chicken gizzard filamin was purchased from Research Diagnostics (Flanders, ...
Actinin alpha (pan), 0.1 mg. The spectrin gene family encodes a diverse group of cytoskeletal proteins that include spectrins, dystrophins and α-actinins.
Since Uzgiris and Kornberg showed that lipid monolayers formed excellent substrates for 2-D crystallization of proteins and macromolecular assemblies. We are using this technique to crystallize cytoskeletal proteins and their complexes. One of these molecules currently being studied is the actin crosslinking protein alpha-actinin. 2-D crystals of alpha-actinin have been formed on positively charged lipid monolayers. In addition, paracrystalline aggregates of F-actin and the complex between F-actin and α-actinin have also been formed on these same lipid monolayers. The technology for formation of 2-D paracrystalline bundles of F-actin on lipid monolayers makes it possible to study additional complexes between F-actin and its crosslinkers which hitherto had formed 3-D gels or bundles. The image to the right was published from Biophys. J. 67, 1976-1983 in 1994.. ...
高い抗原親和性、特異性と安定した品質を兼ね備えたアブカムのウサギ・モノクローナル抗体 RabMAb® ab68167 交差種: Ms,Rat,Hu 適用: WB,IP,IHC-P
ABP-120 and non-muscle α-actinin are members of a family of F-actin cross-linkers that are grouped based on the high degree of amino acid similarity of their actin-binding domains. Although these two proteins have been extensively characterized, little is known about whether they bind to different kinds of F-actin structures and what regulates their binding. GFP fusion proteins were constructed consisting of either the entire cross-linking protein or its actin-binding domain alone. The localization of these fluorescent proteins was examined in living cells under a variety of conditions known to involve actin. The localization patterns of ABP-120 (GFP120) and α-Actinin (GFPα-A) were overlapping but distinct. GFP120 localized to the cell cortex as well as to new pseudopods and to the cortex of polarized cells, but was observed to localize more to the rear of the cell during cAMP and under agarose folate chemotaxis. GFPα-A was enriched in new pseudopods and to the F-actin filled leading edge of
ACTN4 [ENSP00000252699]. Non-muscle alpha-actinin 4; F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA; Belongs to the alpha-actinin family.. Synonyms: ACTN4, ACTN4p, hACTN4, H7C144, K7EJH8 .... Linkouts: STRING Pharos UniProt OMIM ...
Histone lysine methylation is considered to be a relatively stable modification associated with important functions in epigenetic gene control and for organizing chromatin domains. Genes encoding mammalian homologues of the Drosophila suppressor of PEV Su(var)3-9 were the first shown to encode proteins with histone lysine methyl-transferase (HKMT) activity. A hallmark signature of this class of proteins is the evolutionary conserved SET-domain found in numerous chromatin regulators, and was named for its occurrence in genes encoding three such regulators in Drosophila, namely Su(var)3-9, E(z) and trithorax. Here we describe the characterization of a putative SET-domain gene in Drosophila melanogaster, G9a. The gene encodes a protein of 1637 amino acids with similar domain architecture as the mammalian homologue of same name. Whole mount in situ hybridization shows that the gene is maternal and immunostaining shows nuclear localization of DmG9a. A yeast two-hybrid screening revealed that DmG9a ...
Principal Investigator:AKASAKA Yoshikiyo, Project Period (FY):2006 - 2007, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Experimental pathology
The proband (II-15) was an 82-year-old man with mild, asymmetrical LV hypertrophy localized to the basal and midseptum, marked biatrial dilatation, and a restrictive LV filling pattern with preserved systolic function. He had been diagnosed with nonobstructive HCM almost 3 decades earlier and followed at our institution since 2005. Remarkably, he had a history of paroxysmal AF that presented at the age of 30, which subsequently evolved into permanent AF with advanced AV block, requiring VVI pacing at the age of 68 (Figure 2). In 2008, he proved to be negative for mutations in the coding regions and splice sites of the 8 most prevalent sarcomere genes. Despite his early onset of disease manifestations and adverse cardiac remodeling, consistent with restrictive evolution of HCM, he remained fully active with only mild functional limitation (functional class New York Heart Association class II). Furthermore, he remained free from cardioembolic complications although he repeatedly refused treatment ...
UniProtKB IDs are not shown, 1) if protein (or gene) isotypes are not specified in the referred articles, 2) if their IDs are not found in the UniprotKB database or by us ...
Deficiency of the fast-twitch muscle protein alpha-actinin-3 due to homozygosity for a nonsense polymorphism (R577X) in the ACTN3 gene is common in humans. alpha-Actinin-3 deficiency (XX) is associated with reduced muscle strength/power and enhanced endurance performance in elite athletes and in the general population. The association between R577X and loss in muscle mass and function (sarcopenia) has previously been investigated in a number of studies in elderly humans. The majority of studies report loss of ACTN3 genotype association with muscle traits in the elderly, however, there is some indication that the XX genotype may be associated with faster muscle function decline. To further explore these potential age-related effects and the underlying mechanisms, we examined the effect of alpha-actinin-3 deficiency in aging male and female Actn3 knockout (KO) mice (2, 6, 12, and 18 months). Our findings support previous reports of a diminished influence of ACTN3 genotype on muscle performance in the
Alpha-actinin (alpha-actinin-2) is a protein which links the NR1 and NR2B subunits of N-methyl-D-aspartate (NMDA) glutamate receptors to the actin cytoskeleton. Because of the importance of NMDA receptors in modulating the function of the striatum, we have examined the localization of alpha-actinin-2 protein and mRNA in striatal neurons, and its biochemical interaction with NMDA receptor subunits present in the rat striatum. Using an alpha-actinin-2-specific antibody, we found intense immunoreactivity in the striatal neuropil and within striatal neurons that also expressed parvalbumin, calretinin and calbindin. Conversely, alpha-actinin-2 immunoreactivity was not detected in neurons expressing choline acetyltransferase and neuronal nitric oxide synthase. Dual-label in situ hybridization revealed that the highest expression of alpha-actinin-2 mRNA is in substance P-containing striatal projection neurons. The alpha-actinin-2 mRNA is also present in enkephalinergic projection neurons and ...
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Dictyostelium alpha-actinin is a Ca(2+)-regulated F-actin cross-linking protein. To test the inhibitory function of the two EF hands, point mutations were introduced into either one or both Ca(2+)-binding sites. After mutations, the two EF hands were distinguishable with respect to their regulatory activities. Inactivation of EF hand I abolished completely the F-actin cross-linking activity of Dictyostelium discoideum alpha-actinin but Ca2+ binding by EF hand II was still observed in a 45Ca2+ overlay assay. In contrast, after mutation of EF hand II the molecule was still active and inhibited by Ca2+; however, approximately 500-fold more Ca2+ was necessary for inhibition and 45Ca2+ binding could not be detected in the overlay assay. These data indicate that EF hand I has a low affinity for Ca2+ and EF hand II a high affinity, implying a regulatory function of EF hand I in the inhibition of F-actin cross-linking activity. Biochemical data is presented which allows us to distinguish two functions ...
Clearly my myosin LC2 and my alpha actinin genes count as two (or is it 4, because I have two copies of each), but do we have 2 more if we add in those of the mouse? And how about the chimpanzee, if we discover that (unlike the mouse) their genes/alleles are absolutely identical to mine? Do we have 2 more when we add in the alleles of the mayor of my town (which, unbeknowst to her have synonomous substitions that make the protein-encoding portion of her DNA, but not the protein itself, different from mine)? Or how about those of the guy next door, who has a neutral mutation in an intron region? Or my third cousin, who has a neutral AA substition in his proteins ...
Recombinant protein from the full-length sequence of homo sapiens actinin alpha 1 (ACTN1), transcript variant 2 (NM_001102), with a His tag., from EUPROTEIN
The muscle protein, which covers the active sites on the actin filament at rest, is: a. Troponin-I b. Troponin-C c. Tropomyosin d. Myosin e. Actinin
Our previous series of studies have shown that l-afadin is essential for the colocalization and compact clustering of nectin with E-cadherin at cell-cell AJs and proper organization of E-cadherin-based cell-cell AJs (Ikeda et al. 1999; Takahashi et al. 1999; Miyahara et al. 2000). Extending these earlier observations, we have shown here that the COOH-terminal half of α-catenin is, furthermore, essential for this colocalization. This colocalization is not mediated through the cytoplasmic region of E-cadherin or β-catenin. α-Catenin directly interacts with vinculin and α-actinin through the NH2-terminal half (Knudsen et al. 1995; Nieset et al. 1997; Watabe-Uchida et al. 1998; Imamura et al. 1999) and with ZO-1 through the COOH-terminal half (Itoh et al. 1997; Imamura et al. 1999). All of these α-catenin-binding proteins directly interact with F-actin (Burridge and Feramisco 1982; Menkel et al. 1994; Johnson and Craig 1995; Itoh et al. 1997; Fanning et al. 1998). The present results show that ...
To examine the function of CRP2 in vivo, we generated Csrp2−/− mice by targeted mutation. The LIM domains of CRP2 mediate interactions with its binding partners including zyxin, α-actinin, and CRP2BP.12,19,30 Thus, we targeted the first LIM domain by disrupting exon 3, the largest coding exon. No message was detected in Csrp2−/− mouse RNA when exon 3 was used as a probe, although a smaller transcript was detected by RT-PCR. Nevertheless, no CRP2 was detected in protein isolated from Csrp2−/− mouse aorta by Western blot analysis using CRP2(91-98) antiserum. Furthermore, immunostaining of aortic sections with CRP2(93-108) antiserum did not detect CRP2 expression in Csrp2−/− mice. We cannot exclude the possibility that a truncated protein could be generated because the two antisera used in this study were against epitopes C-terminal to those encoded by exon 2. However, even if the truncated transcript were translated, it would not encode either LIM domain due to a frame shift. ...
apical plasma membrane, cell-cell adherens junction, focal adhesion, actinin binding, protein C-terminus binding, ubiquitin-protein transferase activity, cell-cell adhesion
This paper provides a comprehensive explanation of striated muscle mechanics and contraction on the basis of filament rotations. Helical proteins, particularly the coiled-coils of tropomyosin, myosin and α-actinin, shorten their H-bonds cooperatively and produce torque and filament rotations when the Coulombic net-charge repulsion of their highly charged side-chains is diminished by interaction with ions. The classical
Heterogeneity of SMC is a well-known phenomenon. The interpretation, however, of the morphologic phenotype as well as the functional implications of the expression of differentiation markers is subject to much debate. The data are derived from in vivo or in vitro studies. The material used varies from adult to neonatal to fetal vessels and cells from different animal species. The origin of the cultured cells can be from intima, inner or outer media, or the adventitia in both normal and diseased vessels.. The data from in vitro studies are largely reflected in in vivo studies. Proceeding from data in early fetal development, it has been shown that the SMC start to express SM α-actin17 followed by 1E12,20 an actinin marker, and smoothelin.21 Relative late differentiation markers are the already mentioned markers, such as SM22, calponin, h-caldesmon,7 and SM myosin.8 These are upregulated until the expression level of the mature vessel wall is reached.9 11 During this developmental period, there ...
Immunocytochemistry for confocal microscopy. Sections were blocked in 20% normal donkey serum (NDS; Jackson ImmunoResearch, West Grove, PA) in 0.05 m PBS, pH 7.4, then incubated in various combinations of primary antibodies for cortactin, α-actinin, synaptophysin, and VGLUT1 in PBS containing 2% NDS overnight at room temperature. After several washes, sections were incubated in secondary antibodies (anti-rabbit Cy3 for cortactin, anti-mouse FITC for synaptophysin and VGLUT1). Alexa Fluor-488 conjugated to phalloidin (Molecular Probes, Eugene, OR) was used for visualization of F-actin (Allison et al., 1998). For visualization of cell processes, we used the lipophilic dye 3,3′-dioctadecyloxacarbocyanidine perchlorate (DiO; Molecular Probes), which infiltrates the plasma membrane, labeling even the finest neuronal processes (for details, see Burette et al., 2002). After several washes, sections were mounted on glass slides, coverslipped in Vectashield (Vector Laboratories, Burlingame, CA) and ...
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity).
Loss of CH-ILKBP impairs the membrane translocation of PKB/Akt. (A-E) The CH-ILKBP siRNA-transfectants (lanes 1 and 2), the control transfectants (lanes 3 and
Things will be a lot different when we are older. Perhaps when your grandchild is born, right after they snip the umbilical cord, they will sequence their genome. Immediately, some computer will pick out genetic markers for specific disease states, and maybe a doctor (possibly some gene-ologist of sorts) will do a little bit of gene therapy to prevent the more serious diseases from developing. Perhaps for those really wealthy parents, a few more options may open for tweaking. If you dont like the hair colour your childs genes code for, just check the appropriate box and they can take care of that. What about sports? Would you prefer a power athlete, maybe a sprinter, or would you rather your child be tailored for endurance? For that option, perhaps they would look at tinkering with the ACTN3 gene, which encodes the muscle fiber protein alpha-actinin-3. As it turns out, you could probably already predict genetic predisposition of muscles for either power or endurance. There is evidence for certain
Mutations in 1-actinin-4 (Actn4), an actin crosslinking protein encoded by the human ACTN4 gene, cause an autosomal dominant form of focal segmental glomerulosc...
Complete information for ACTN1-AS1 gene (RNA Gene), ACTN1 Antisense RNA 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
BioMed Research International is a peer-reviewed, Open Access journal that publishes original research articles, review articles, and clinical studies covering a wide range of subjects in life sciences and medicine. The journal is divided into 55 subject areas.
The topographical relationship between stress fiber-like structures (SFLS) and nascent myofibrils was examined in cultured chick cardiac myocytes by immunofluorescence microscopy. Antibodies against muscle-specific light meromyosin (anti-LMM) and desmin were used to distinguish cardiac myocytes from fibroblastic cells. By various combinations of staining with rhodamine-labeled phalloidin, anti-LMM, and antibodies against chick brain myosin and smooth muscle alpha-actinin, we observed the following relationships between transitory SFLS and nascent and mature myofibrils: (a) more SFLS were present in immature than mature myocytes; (b) in immature myocytes a single fluorescent fiber would stain as a SFLS distally and as a striated myofibril proximally, towards the center of the cell; (c) in regions of a myocyte not yet penetrated by the elongating myofibrils, SFLS were abundant; and (d) in regions of a myocyte with numerous mature myofibrils, SFLS had totally disappeared. Spontaneously contracting ...
Skeletal muscle actin binding protein spin-down assay kit provides G- or F-actin plus positive (α-actinin ) and negative (Bovine Serum Albumin, BSA) binding control proteins. Kit contains skeletal muscle actin.
TY - JOUR. T1 - C3a receptor blockade protects podocytes from injury in diabetic nephropathy. AU - Morigi, Marina. AU - Perico, Luca. AU - Corna, Daniela. AU - Locatelli, Monica. AU - Cassis, Paola. AU - Carminati, Claudia Elisa. AU - Bolognini, Silvia. AU - Zoja, Carlamaria. AU - Remuzzi, Giuseppe. AU - Benigni, Ariela. AU - Buelli, Simona. PY - 2020/3/12. Y1 - 2020/3/12. N2 - Renal activation of the complement system has been described in patients with diabetic nephropathy (DN), although its pathological relevance is still ill-defined. Here, we studied whether glomerular C3a, generated by uncontrolled complement activation, promotes podocyte damage, leading to proteinuria and renal injury in mice with type 2 diabetes. BTBR ob/ob mice exhibited podocyte loss, albuminuria, and glomerular injury accompanied by C3 deposits and increased C3a and C3a receptor (C3aR) levels. Decreased glomerular nephrin and α-actinin4 expression, coupled with integrin-linked kinase induction, were also observed. ...
de Almeida Ribeiro E., Pinotsis N., Ghisleni A., Salmazo A., Konarev P. V., Kostan J., Sjöblom B., Schreiner C., Polyansky A., Gkougkoulia E. A., Holt M. R., Aachmann F. L., Žagrović B., Bordignon E., Pirker K. F., Svergun D. I., Gautel M., Djinović-Carugo K. (2014), The structure of human muscle α-actinin: Insight into the intramolecular regulation of ligand binding and Z-disk assembly, Cell 159(6):1447-60. ...
de Almeida Ribeiro E., Pinotsis N., Ghisleni A., Salmazo A., Konarev P. V., Kostan J., Sjöblom B., Schreiner C., Polyansky A., Gkougkoulia E. A., Holt M. R., Aachmann F. L., Žagrović B., Bordignon E., Pirker K. F., Svergun D. I., Gautel M., Djinović-Carugo K. (2014), The structure of human muscle α-actinin: Insight into the intramolecular regulation of ligand binding and Z-disk assembly, Cell 159(6):1447-60. ...
Many eukaryotes have long slender motile cytoplasmic projections, called flagella. These are composed mainly of tubulin and shorter cilia, both of which are variously involved in movement, feeding, and sensation. These are entirely distinct from prokaryotic flagella. They are supported by a bundle of microtubules arising from a basal body, also called a kinetosome or centriole, characteristically arranged as nine doublets surrounding two singlets. Flagella also may have hairs, or mastigonemes, and scales connecting membranes and internal rods. Their interior is continuous with the cells cytoplasm. Microfilamental structures composed by actin and actin binding proteins, e.g., α-actinin, fimbrin, filamin are present in submembraneous cortical layers and bundles, as well. Motor proteins of microtubules, e.g., dynein or kinesin and actin, e.g., myosins provide dynamic character of the network. Centrioles are often present even in cells and groups that do not have flagella. They generally occur in ...
Clone REA199 recognizes CD144 (VE-Cadherin), a 120 KDa type II cadherin. Cadherins are cell adhesion molecules and mediate Ca2+ dependent homophilic interactions. CD144 contains five extracellular cadherin (EC) domains and like other cadherins can interact directly via its C-terminus with cytoplasmic proteins such as β-catenin, plaktoglobin, and p120. Plaktoglobin und β-catenin bind to α-catenin, which in turn interacts with several actin-binding proteins, α-actinin, ajuba, zonula occludens-1 (ZO-1). Further indirect interactions of CD144 with partners such as SHP-2, VEGFR-2, Csk, and PAR-3, 6 allows CD144 to not only regulate the stability and strength of cell adhesion but also to serve functions such as sensing of shear forces, anti-proliferative, and anti-apoptotic effects. Additional information: Clone REA199 displays negligible binding to Fc receptors. - Ireland
Clone REA199 recognizes CD144 (VE-Cadherin), a 120 KDa type II cadherin. Cadherins are cell adhesion molecules and mediate Ca2+ dependent homophilic interactions. CD144 contains five extracellular cadherin (EC) domains and like other cadherins can interact directly via its C-terminus with cytoplasmic proteins such as β-catenin, plaktoglobin, and p120. Plaktoglobin und β-catenin bind to α-catenin, which in turn interacts with several actin-binding proteins, α-actinin, ajuba, zonula occludens-1 (ZO-1). Further indirect interactions of CD144 with partners such as SHP-2, VEGFR-2, Csk, and PAR-3, 6 allows CD144 to not only regulate the stability and strength of cell adhesion but also to serve functions such as sensing of shear forces, anti-proliferative, and anti-apoptotic effects. Additional information: Clone REA199 displays negligible binding to Fc receptors. - Schweiz
Myosin II is a motor protein found in the cytoskeleton in the cytoplasm of cells. It is responsible for enpowering actin to contract. In [[A quantitative analysis of contractility in active cytoskeletal protein networks]] by Weitz et al. Show the role of myosin in actin contraction. It was shown that without appropriate amounts of ,math>alpha,/math>-actinin, myosin cannot produce contraction. ==References== http://en.wikipedia.org/wiki/Myosin ...
Walikonis, Randall S. and Oguni, Asako and Khorosheva, Eugenia M. et al. (2001) Densin-180 forms a ternary complex with the α-subunit of Ca^(2+)/calmodulin-dependent protein kinase II and α-actinin. Journal of Neuroscience, 21 (2). pp. 423-433. ISSN 0270-6474. PMCID PMC6763799. https://resolver.caltech.edu/CaltechAUTHORS:20120424-150007753 ...
Methods and Results: Distribution of Islet-1+ cells in adult heart was investigated using transgenic mice with nuclear β-galactosidase inserted into the Islet-1 locus. nLacZ-positive cells were only present in 3 regions of the adult heart: clusters in the interatrial septum, scattered within the wall of the great vessels, and a strictly delimited cluster between right atrium and superior vena cava. Islet-1+ cells in the first type of clusters coexpressed markers for parasympathetic neurons. Positive cells in the great arteries coexpressed smooth muscle actin and β-myosin heavy chain, indicating a smooth muscle cell identity. Very few Islet-1+ cells within the outflow tract expressed the cardiomyocyte marker α-actinin. Islet-1+ cells in the right atrium coexpressed the sinoatrial node pacemaker cell marker HCN4. Cell number and localization remained unchanged between 1 to 18 months of age. Consistently Islet-1 mRNA was detected in human sinoatrial node. Islet-1+ cells could not be detected in ...
test were utilized. through ubiquitination. Over-expression of IQGAP1 in charge MEF phenocopied the migration and growing flaws of cells. On the other hand, siRNA-mediated knockdown of IQGAP1 rescued the flaws in cellular motion of cells. Conclusions The E3 ligase activity of Hectd1 regulates the protein degree of IQGAP1 through ubiquitination and for that reason mediates the dynamics of FXs like the recruitment of paxillin and actinin. IQGAP1 is among the effectors of HECTD1. Electronic supplementary materials The online edition of this content (doi:10.1186/s12964-016-0156-8) contains supplementary materials, which is open to authorized users. mice elevated the cranial mesenchyme cell migration [16, 17] however the results from Li and coworkers demonstrated that knockdown of HECTD1 inhibits TGFBR2 the migration of breasts cancer tumor MDA-MB-231 cells [18]. To solve this contradictory concern, we have utilized the Hectd1 homozygous mutant (mutation mice [33], the gene-trap mouse embryonic stem ...
Identification, characterization, and synthesis of peptide epitopes and a recombinant six-epitope protein for Trichomonas vaginalis serodiagnosis J F Alderete, Calvin J NeaceSchool of Molecular Biosciences, College of Veterinary Medicine, Washington State University, Pullman, WA, USAAbstract: There is a need for a rapid, accurate serodiagnostic test useful for both women and men infected by Trichomonas vaginalis, which causes the number one sexually transmitted infection (STI). Women and men exposed to T. vaginalis make serum antibody to fructose-1,6-bisphosphate aldolase (ALD), α-enolase (ENO), and glyceraldehyde-3-phosphate dehydrogenase (GAP). We identified, by epitope mapping, the common and distinct epitopes of each protein detected by the sera of women patients with trichomonosis and by the sera of men highly seropositive to the immunogenic protein α-actinin (positive control sera). We analyzed the amino acid sequences to determine the extent of identity of the epitopes of each protein
Connecting devices and elongated members for orthopedic medical use are disclosed. In certain embodiments, a connecting device may include a central portion that can accommodate part of an elongated member and wings for connecting to anchor members. Such central portions can be open or closed, and such wings can be solid, e.g. rod-type structures, or can be slotted. A T-shaped elongated member is also disclosed.
Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
This gene encodes a member of the IQGAP family. The encoded protein contains three IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. This protein interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. It also acts as a tumor suppressor and has been found to play a role in regulating innate antiviral responses. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Apr 2017 ...
... has been shown to interact with: AKAP9, Actinin, alpha 1, CCDC85B, NEFL, NEUROD2 Phosphoinositide-dependent ... "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740-6. doi:10.1074/jbc.272.8.4740. PMID 9030526. Matsuzawa K, ... "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX ...
... alpha-actinin. Xin, and XIRP2. Nebulette was identified in 1995 by Moncman and Wang using primary cultures of chicken embryonic ...
"An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol ... "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol ... Li B, Trueb B (2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328-35. doi:10.1074/jbc. ... Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328-35. doi: ...
CapZ interacts with α-actinin, nebulette, nebulin, HSC70. at the Z-disc. CAPZB is a member of the F-actin capping protein ... Papa I, Astier C, Kwiatek O, Raynaud F, Bonnal C, Lebart MC, Roustan C, Benyamin Y (February 1999). "Alpha actinin-CapZ, an ...
Maruyama K, Kurokawa H, Oosawa M, Shimaoka S, Yamamoto H, Ito M, Maruyama K (May 1990). "Beta-actinin is equivalent to Cap Z ...
... has been shown to interact with Keratin 18, Actinin alpha 4, Dystonin, Actinin, alpha 1, CTNND1 ... Gonzalez, A M; Otey C; Edlund M; Jones J C (December 2001). "Interactions of a hemidesmosome component and actinin family ...
They decided to compile their work on α-actinin and showed that α-actinin is distributed periodically along stress fibers. They ... Since these regions would several years later be named focal adhesions, α-actinin was the first protein found to be ... While developing a procedure to purify α-actinin from smooth muscle, Burridge co-purified another protein, vinculin, ... Lazarides E, Burridge K; Burridge (November 1975). "Alpha-actinin: immunofluorescent localization of a muscle structural ...
Liu Y, Belkina NV, Shaw S (2009). "HIV infection of T cells: actin-in and actin-out". Science Signaling. 2 (66): pe23. doi: ... For example, if the α-actinin or gelation factor gene has been removed in Dictyostelium individuals do not show an anomalous ... The contractile ring is composed of actin, myosin, anillin, and α-actinin. In the fission yeast Schizosaccharomyces pombe, ... Fujiwara K, Porter ME, Pollard TD (Oct 1978). "Alpha-actinin localization in the cleavage furrow during cytokinesis". The ...
TRPP3 is abundant in mouse brain where it associates with alpha-actinin-2. Alpha-actinin attaches TRPP3 to the cytoskeleton and ... Li Q, Dai XQ, Shen PY, Wu Y, Long W, Chen CX, Hussain Z, Wang S, Chen XZ (December 2007). "Direct binding of alpha-actinin ... Li Q, Dai XQ, Shen PY, Wu Y, Long W, Chen CX, Hussain Z, Wang S, Chen XZ (December 2007). "Direct binding of alpha-actinin ... Alpha-actinin is an actin-bundling protein known to regulate several types of ion channels. Planer lipid bilayer ...
Li B, Zhuang L, Reinhard M, Trueb B (2003). "The lipoma preferred partner LPP interacts with alpha-actinin". J. Cell Sci. 116 ( ...
... has been shown to interact with Actinin alpha 4. GRCh38: Ensembl release 89: ENSG00000058404 - Ensembl, May 2017 GRCm38 ... actinin". J. Neurosci. 21 (2): 423-33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423. Liao GY, Wagner DA, ... actinin". J. Neurosci. 21 (2): 423-33. doi:10.1523/JNEUROSCI.21-02-00423.2001. PMC 6763799. PMID 11160423. Yamamoto H (2002 ...
... has been shown to interact with Actinin, alpha 1. GRCh38: Ensembl release 89: ENSG00000171450 - Ensembl, May 2017 GRCm38 ... 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in ... 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in ...
Lan S, Wang H, Jiang H, Mao H, Liu X, Zhang X, Hu Y, Xiang L, Yuan Z (2003). "Direct interaction between α-actinin and ...
Yan Q, Sun W, Kujala P, Lotfi Y, Vida TA, Bean AJ (May 2005). "CART: an Hrs/actinin-4/BERP/myosin V protein complex required ... The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin ... TRIM3 has been shown to interact with Actinin alpha 4. TRIM3 binds to and ubiquitinates Estrogen receptor alpha (ERa) leading ... binds to alpha-actinin-4". Biochemical and Biophysical Research Communications. 267 (3): 906-911. doi:10.1006/bbrc.1999.2045. ...
2003). "Direct interaction between alpha-actinin and hepatitis C virus NS5B". FEBS Lett. 554 (3): 289-94. doi:10.1016/S0014- ...
... with alpha-actinin 2". J Cell Biochem. 78 (4): 558-65. doi:10.1002/1097-4644(20000915)78:4. 3.0.CO;2-I. PMID 10861853. S2CID ...
Namely, α-Actinin results in heightened pH sensitivity and desensitization recovery. They can also increase current flow ...
Wyszynski M, Lin J, Rao A, Nigh E, Beggs AH, Craig AM, Sheng M (January 1997). "Competitive binding of alpha-actinin and ... Actinin, alpha 2, DLG2, DLG3, DLG4, EXOC4, LIN7B, and RICS. NMDA receptor Glutamate receptor GRCh38: Ensembl release 89: ...
Immunostains for myotilin and α-actinin all but clinch the diagnosis. However, nemaline rods may still be visible post-mortem ...
... "alpha-Actinin localization in the junctional complex of intestinal epithelial cells". J Cell Biol. 80 (1): 203-210. doi:10.1083 ...
2005). "Involvement of palladin and alpha-actinin in targeting of the Abl/Arg kinase adaptor ArgBP2 to the actin cytoskeleton ... 2004). "Molecular analysis of the interaction between palladin and alpha-actinin". FEBS Lett. 566 (1-3): 30-4. doi:10.1016/j. ...
Vallenius T, Luukko K, Mäkelä TP (2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4 ... PDLIM1 has been shown to interact with: Actinin alpha 4, Actinin, alpha 1, Estrogen receptor alpha, and RNF12. GRCh38: Ensembl ... "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100-5. doi: ... with alpha-actinin 2". J Cell Biochem. 78 (4): 558-65. doi:10.1002/1097-4644(20000915)78:4. 3.0.CO;2-I. PMID 10861853. S2CID ...
The antiparallel arrangement of actin filaments within stress fibers is reinforced by α-actinin, an actin filament crosslinking ... Lazarides, Elias; Burridge, Keith (November 1975). "α-Actinin: Immunofluorescent localization of a muscle structural protein in ... such as α-actinin, to form a highly regulated actomyosin structure within non-muscle cells. Stress fibers have been shown to ... fibers in motile and non-motile cells are similar in that they both contain actin filaments which are cross-linked by α-actinin ...
There are no RNA binding motifs or actinin type actin binding motifs. There are no N-myristoylation pattern or prenylation ...
Harper BD, Beckerle MC, Pomiès P (2001). "Fine mapping of the alpha-actinin binding site within cysteine-rich protein". Biochem ...
Within the brain, dendrin interacts with α-actinin in postsynaptic dendritic spines. Together MAGI/S-SCAM, α-actinin, and ... Along with two other proteins, MAGI/S-SCAM and α-actinin, dendrin is linked to synaptic plasticity and memory formation in the ... The protein trio of MAGI/S-SCAM, α-actinin, and dendrin helps to connect postsynaptic density (PSD) to the cytoskeleton of the ...
These include spectrin, alpha-actinin, dystrophin and more recently the plakin family. The spectrin repeat forms a three-helix ...
Olski TM, Noegel AA, Korenbaum E (Feb 2001). "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily ... 2004). "Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial ...
Olski TM, Noegel AA, Korenbaum E (Feb 2001). "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily ...
Otey CA, Vasquez GB, Burridge K, Erickson BW (Oct 1993). "Mapping of the alpha-actinin binding site within the beta 1 integrin ... Otey CA, Pavalko FM, Burridge K (Aug 1990). "An interaction between alpha-actinin and the beta 1 integrin subunit in vitro". ...
Actinin is a microfilament protein. Alpha-actinin-1 is necessary for the attachment of actin myofilaments to the Z-lines in ... Both ends of the rod-shaped alpha-actinin dimer contain actin-binding domains. Mutations in ACTN4 can cause the kidney disease ... ISBN 978-0-08-092427-4. Actinin at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with ... The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. ACTN2 expression is found in both cardiac ...
alpha-actinin-1. Names. F-actin cross-linking protein. alpha actinin 1a. non-muscle alpha-actinin-1. ... actinin, alpha 1provided by MGI. Primary source. MGI:MGI:2137706 See related. Ensembl:ENSMUSG00000015143 AllianceGenome:MGI: ... XM_030246514.2 → XP_030102374.1 alpha-actinin-1 isoform X2. Conserved Domains (4) summary. cd00051. Location:507 → 596. EFh; EF ... XM_036157161.1 → XP_036013054.1 alpha-actinin-1 isoform X3. Conserved Domains (4) summary. cd00051. Location:475 → 564. EFh; EF ...
"α-actinin, an actin binding protein, plays a key role in cell migration, cross-links actin filaments in the Z-disk, and is a ... α-actinin, an actin binding protein, plays a key role in cell migration, cross-links actin filaments in the Z-disk, and is a ... α-actinin rod domain, α-spectrin, Steered Molecular Dynamics. Cite This Article. Zaman, M. H., Kaazempur-Mofrad, M. R. (2004). ... How flexible is α-actinins rod domain?. Muhammad H. Zaman1, Mohammad R. Kaazempur-Mofrad2 1. Whitehead Institute, 9 Cambridge ...
Similar to human α-actinin, calcium-binding occurs to the most N-terminal EF-hand motif in the calmodulin-like C-terminal ... Analysis of the primary sequence indicate that this protein has the same domain structure as other α-actinins, a N-terminal ... The results indicate that this Bigelowiella protein is a proper α-actinin, with all common characteristics of a typical α- ... The genome of the chlorarchiniophyte Bigelowiella natans codes for a protein annotated as an α-actinin-like protein. ...
α-Actinin-4, encoded by the gene ACTN4 on chromosome 19, cross-links actin filaments of the podocyte cytoskeleton and anchors ... Mutations in the α-actinin-4 gene (ACTN4) and the gene TRPC6 are associated with autosomal-dominant forms of familial FSGS. ...
Monoclonal Anti-α-Actinin antibody produced in mouse (monoclonal BM-75.2, ascites fluid); Suitable for indirect ... α-actinin is a 100kD actin binding protein found in muscle as well as non-muscle cells. In smooth muscle, α-actinin is ... The gene encoding α-actinin is mapped to the human chromosome 11q13.2. α-actinin belongs to the spectrin protein superfamily.[ ... Monoclonal anti-α-actinin antibody (diluted 1: 500) can be used in native protein binding assays[. 69. ]. It can also be used ...
Crucial functions of alpha-actinin 2 in the embryonic heart Gehmlich K., Jiang A., Wadmore K., Hooper C., Douglas G., Ehler E ...
... actinin antibody showed the presence of α-actinin in the immunoblot which was absent when GST-N terminus deleted annexin A6 was ... In overall, the present study demonstrated for the first time that annexin A6 physically interacts with sarcomeric α-actinin ... Double immunofluorescent staining of cardiomyocytes with anti annexin A6 and anti sarcomeric α-actinin antibodies showed ... as revealed by α-actinin immunostaining in shRNA treated cells. ... From: Interaction of annexin A6 with alpha actinin in ...
Alpha-actinin dynamically anchors PSD-95 and AMPARs at postsynaptic sites. Add to your list(s) Download to your calendar using ... University of Cambridge , Talks.cam , ihg21s list , Alpha-actinin dynamically anchors PSD-95 and AMPARs at postsynaptic sites ...
Purification and properties of [alpha]-actinin from rabbit striated ...
Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein alpha-actinin-4 for viral replicationExternal. ...
Procedure describing a suggested protocol for sarcomeric actinin, ANP, ER and ERb fluorescent staining of cardiomyocytes. ... The α-actinin stain is stable for quite some time but the ANP stain tends to bleach out within about 1-2 weeks. ... Treat cells with antibodies for α-actinin eg. alpha sarcomeric actin antibody [alpha Sr-1] (ab28052) and ANP diluted in the ... Treat cells with antibodies for α-actinin (1/200 dilution) diluted in the blocking buffer as above for 1 hour. ...
alpha-Actinin-4. O43707. 11. 72. assembly. Myosin-9. P35579. 11. 26. assembly. ...
Affixin interacts with a-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell- ... Affixin interacts with a-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell- ...
ORCID: 0000-0002-6956-9188 (2019) A "human knockout" model to investigate the influence of the α-actinin-3 protein on exercise- ... A "human knockout" model to investigate the influence of the α-actinin-3 protein on exercise-induced mitochondrial adaptations ...
... wild-type α-actinin-4, and (C) mutant α-actinin-4. Scale bar is ,math>40\mu m,/math>]] By performing rheological experiments, ... View source for Dynamic Viscoelasticity of Actin Cross-Linked with Wild-Type and Disease-Causing Mutant α-Actinin-4. ← Dynamic ... Of particular interest is a cross-linker called α-actinin-4. This cross-linker is present naturally in podocytes, the kidney ... By examining the relaxation frequency of the wild-type and mutant α-actinin-4 networks at various temperatures, the authors ...
Anti-Actinin α4. Application Data. Detection of rat ACTN4 by immunoblotting. Sample: Whole cell lysate from PC-12 cells. ... Anti-Actinin α4. Application. ELISA (see coments). Immunoblotting (1-5 µg/ml). Immunocytochemistry (20 µg/ml). Paraffin ... Alpha actinin is an actin-binding protein with multiple roles in different cell types. In non-muscle cells, the cytoskeletal ... Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the ...
α-Actinin Anchors PSD-95 at Postsynaptic Sites. Matt L, Kim K, Hergarden AC, Patriarchi T, Malik ZA, Park DK, Chowdhury D, ...
... α-actinin-2, mouse monoclonal (Sigma); calbindin D-28k, mouse monoclonal (Swant); GABA-A receptor α1 subunit, rabbit polyclonal ... and J72a for calbindin and α-actinin-2, which provide clear areal boundaries (Mercer et al., 2007). To delineate the area that ...
A variant in this gene, called R577X, leads to production of an abnormally short α-actinin-3 protein that is quickly broken ... The ACTN3 gene provides instructions for making a protein called alpha (α)-actinin-3, which is predominantly found in fast- ... These individuals have a complete absence of α-actinin-3, which appears to reduce the proportion of fast-twitch muscle fibers ...
The actin-ECM (extracellular matrix) linkage defects caused by mutations in the Kindlin1 gene are mediated by actinin alpha. / ... The actin-ECM (extracellular matrix) linkage defects caused by mutations in the Kindlin1 gene are mediated by actinin alpha. ... The actin-ECM (extracellular matrix) linkage defects caused by mutations in the Kindlin1 gene are mediated by actinin alpha. ... title = "The actin-ECM (extracellular matrix) linkage defects caused by mutations in the Kindlin1 gene are mediated by actinin ...
SASDJL6 - Sarcomeric F-actin crosslinking protein α-actinin-2 (spectrin repeat rod domain, rod-α-actinin-2) ... SASDJN6 - Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (rod-α-actinin-2/Δ91-FATZ-1) ... SASDJP6 - Sarcomeric fuzzy α-actinin-2/FATZ-1 complex (hd-α-actinin-2/Δ91-FATZ-1) ... Rod domain of α-actinin-2 dimer, 112 kDa Homo sapiens protein. Buffer:. 50 mM Tris-HCl 150 mM NaCl, pH: 7.5. ...
alpha-actinin ,α-actinin,. Alpha-Actinin {n}. ,α-Actinin, biochem.. alpha-actinin ,α-actinin,. Alpha-Aktinin {n}. ,α-Aktinin, ...
A-Actinin 4 (Tyr-4), phospho-specific. £458.00 SKU:. AP4241. Size:. 100 ul. Suppl:. ECM Biosciences. Appli:. Western Blot, ...
actinin alpha 3. involved_in. ISO. (MGI:5554485,PMID:24234654). RGD. PMID:24234654. MGI:5554485. NCBI chr 1:202,159,081... ...
Name: actinin alpha 4. Type: Gene. Species: Mus musculus (mouse). Chromosome: 7 ...
alpha-actinin ,α-actinin,. Alpha-Aktinin {n}. ,α-Aktinin, med.. alpha-synucleinopathies ,α-synucleinopathies,. Alpha- ... α-actinin. α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic. α-Aminobutyric. α-Aminobutyric acid. α-amylase. α-cells. α Cen. α ... alpha-actinin ,α-actinin,. Alpha-Actinin {n}. ,α-Actinin, biochem.. alpha-amylase ,α-amylase,. Alpha-Amylase {f}. ,α-Amylase, ...
  • The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. (wikipedia.org)
  • Orthologous to human ACTN1 (actinin alpha 1). (nih.gov)
  • The ACTN3 gene provides instructions for making a protein called alpha (α)-actinin-3, which is predominantly found in fast-twitch muscle fibers. (medlineplus.gov)
  • A common variant of the ACTN3 gene, R577X, results in complete deficiency of the α-actinin-3 protein in the fast skeletal muscle fibers of more than a billion humans worldwide. (lww.com)
  • One gene potentially associated with human physical performance is the ACTN3 gene, which encodes the protein α-actinin-3. (lww.com)
  • This variation creates two different versions of the ACTN3 gene, both of which are common in the general population: the 577R version (or allele) is the normal, functional version of the gene, whereas the 577X allele contains a sequence change that completely prevents the production of functional α-actinin-3 protein ( 12 ). (lww.com)
  • In its most common variation, which accounts for about 80% of the Australian population, ACTN3 encodes for a protein called alpha-actinin-3. (cavemanpower.com)
  • They found the muscle metabolism of the mice without the actinin protein was more efficient: the mice were able to run, on average, 33 per cent further before reaching exhaustion than mice with the normal ACTN3 gene. (cavemanpower.com)
  • Alpha-actinin-3 (ACTN3) is a protein found mainly in fast glycolytic muscle fibers. (gentrend.cz)
  • Picture this, individuals with a specific variant of the ACTN3 gene, which is one of the most studied fitnessgenes have muscles which contract powerfully at high speeds because they secrete a specific protein called alpha actinin. (xcode.life)
  • A special emphasis was placed on those candidate polymorphisms that have been more extensively studied, i.e. angiotensin-converting enzyme (ACE) gene I/D, α-actinin-3 (ACTN3) R577X, and myostatin (MSTN) K153R, among others. (universidadeuropea.com)
  • Treat cells with antibodies for α-actinin eg. (abcam.com)
  • Treat cells with antibodies for α-actinin (1/200 dilution) diluted in the blocking buffer as above for 1 hour. (abcam.com)
  • Pathogenic anti-DNA antibodies are able to interact at the tissue level with alpha actinin in the renal glomeruli. (immpact-international.org)
  • Cross-reactivity of human lupus anti-DNA antibodies with alpha-actinin and nephritogenic potential. (anapatterns.org)
  • Anti-alpha-actinin antibodies are part of the anti-cell membrane antibody spectrum that characterize patients with lupus nephritis. (anapatterns.org)
  • Anti-alpha-actinin antibodies in relation to new-onset systemic lupus erythematosus and lupus nephritis. (anapatterns.org)
  • Anti-alpha-actinin antibodies cross-react with anti-ssDNA antibodies in active autoimmune hepatitis. (anapatterns.org)
  • Anti-alpha actinin antibodies as new predictors of response to treatment in autoimmune hepatitis type 1. (anapatterns.org)
  • The differentiation potential of EBs into cardiomyocyte-like cells was confirmed by using antibodies against sarcomeric α-actinin, cardiac troponin T and connexin 43. (sciendo.com)
  • C) Immunolabeling of hiPSC-CMs with anti-cTNT (green) and anti-sarcomeric -actinin (reddish colored) antibodies with Hoechst 33342 staining. (cox2-inhibitor.com)
  • Staining indicates cardiac sarcomere proteins alpha actinin and cardiac troponin T, in addition to nuclear stain DAPI. (eurekalert.org)
  • Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). (embl.de)
  • A number of actin-binding proteins, including spectrin, alpha-actinin and fimbrin, contain a 250 amino acid stretch called the actin binding domain (ABD). (embl.de)
  • We found evidence that defined proteolytic cleavage results in various proteoforms of important podocyte proteins, including those of podocin, nephrin, neph1, alpha-actinin-4, and vimentin. (uni-koeln.de)
  • The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. (rcsb.org)
  • Specifically, Actin is assembled into contractile stress fibers, which are organized structures consisting of parallel Actin fibers with periodic cross-linking proteins such as alpha-Actinin and Myosin II motor proteins. (rndsystems.com)
  • Our approach is two-fold: first, we conducted biochemical studies focused on the interactions of actin filaments and the actin binding proteins ARP2/3, alpha-actinin, dynamin2, and cortactin and second, we developed a computational model to validate experimental hypotheses for actin filament crosslinking to promote filament bundling. (jmu.edu)
  • The sarcomeres contain a number of proteins, among them are alpha actinin, which is the major constituent of the Z-band, and actin and myosin, which are the major components of the thin and thick filaments, respectively. (medscape.com)
  • About half of the genes encode sarcomeric proteins including α- cardiac actin , myosin heavy chain , troponin , tropomyosin , metavinculin, α- actinin and therefore overlap with those in HCM. (dictionary.education)
  • It has been shown that this up-regulation of FA proteins, such as vinculin, talin, paxillin, and actin-crosslinking -actinin, causes astrocytes activation and increases the expression of intermediates filaments, including Glial Fibrillary Acidic Protein, vimentin, and nestin [176]. (aqualogy.org)
  • The abstract states, "Glutathione-S-transferase (GST) pulldown assays were used to show that RPTPrho interacts with several adherens junctional proteins in brain, including E-cadherin, N-cadherin, VE-cadherin (cadherin-5), desmoglein, alpha, beta [Ctnnb1] and gamma [Jup] catenin, p120(ctn) and alpha-actinin. (geneontology.org)
  • Alpha-actinin-1 is necessary for the attachment of actin myofilaments to the Z-lines in skeletal muscle cells, and to the dense bodies in smooth muscle cells. (wikipedia.org)
  • Both ends of the rod-shaped alpha-actinin dimer contain actin-binding domains. (wikipedia.org)
  • Alpha-actinin of the chlorarchiniophyte Bigelowiella natans. (scilifelab.se)
  • Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. (jimmunol.org)
  • alpha-actinin-3 and performance. (cdc.gov)
  • Among elite power athletes the alpha-actinin-3 protein is nearly always present. (cavemanpower.com)
  • Those with the variant form of the gene, about 20 per cent of the population, do not make the alpha-actinin-3 protein. (cavemanpower.com)
  • Researchers developed a strain of mice that were completely deficient in alpha-actinin-3. (cavemanpower.com)
  • Most Africans have alpha-actinin-3, it's the normal ancestral state. (cavemanpower.com)
  • Myotilin forms homodimers and binds to alpha-actinin, F-actin, and filamin C. (yeastrc.org)
  • Cultured chicken embryonic cardiomyocyte fixed and stained for alpha-actinin using a monoclonal antibody and Alexa-546 as a secondary fluorescent antibody. (cellimagelibrary.org)
  • In cardiac and skeletal muscle cells, Myozenin 2 binds calcineurin to alpha-actinin at the Z-line of the sarcomere. (fishersci.no)
  • Alpha-actinin was positively identified using electrophoretic techniques and confirmed by tandem mass spectroscopy. (canada.ca)
  • Additionally, cortactin decreases the association of alpha-actinin with bundled actin filaments. (jmu.edu)
  • We hypothesize that the transition from a branched to bundled F-actin network architecture involves balancing the activities of two competing filament crosslinkers: dynamin2 and cortactin vs. alpha-actinin. (jmu.edu)
  • We will test this hypothesis by creating an emergent Monte Carlo model in MATLAB that simulates filament crosslinking in the presence of alpha-actinin, cortactin and dynamin2. (jmu.edu)
  • e.g. anti-alpha-actinin, anti-vinculin. (anapatterns.org)
  • Double reactivity against actin and alpha-actinin defines a severe form of autoimmune hepatitis type 1. (anapatterns.org)
  • Interaction of alpha-actinin and nebulin in vitro. (mpg.de)
  • actinin alpha 1 [Source:HGNC Symbo. (gsea-msigdb.org)
  • Synaptopodin-2 has other known binding partners such as filamin and [alpha]-actinin (Weins, et al. (ecu.edu)
  • This genetic marker controls production of the Alpha-Actinin-3 protein in fast-twitch muscle fibers. (a7.co)
  • Actin/alpha-actinin-dependent transport of AMPA receptors in dendritic spines: role of the PDZ-LIM protein RIL. (mpg.de)
  • Here, it colocalises with metavinculin, vinculin and alpha-actinin, all of which have biochemically been identified as raver1 ligands. (helmholtz-hzi.de)
  • Research has shown that individuals with the gene type R produce a specific protein (alpha-actinin-3) that is exclusively found in the fast-twitch muscle fibers , used during explosive activities, such as sprinting or weight-lifting. (freeletics.com)
  • genetically encoded FRET-based force sensors inserted in F-actin and alpha-actinin are used to measure the propagation of mechanical signals to the cell cytoskeleton, while fluorescence microscopy with single-molecule sensitivity can be used with a huge array of biochemical and genetic sensors. (epj.org)
  • We describe the details of the setup implementation, the calibration of the basic components and preliminary characterization of actin and alpha-actinin FRET-based force sensors. (epj.org)
  • The apparent reason for this: the loss of ACNT3's protein was compensated by a different protein, called alpha-actinin-2, which shifted muscle metabolism towards a smoother, more efficient, aerobic pathway. (blogspot.com)
  • In the reanalysis of the National Cancer Institute Canadian Clinical Trial Group JBR.10, which led to the adoption of adjuvant cisplatin-based chemotherapy for patients with resected stages-IB to IIIA non-small cell lung cancer (NSCLC), we demonstrated a significant clinical benefit of adjuvant chemotherapy for overall survival only in the actinin-4 (ACTN4) high expression group. (nmsbiomarker.com)
  • α-actinin rod domain, α-spectrin, Steered Molecular Dynamics. (techscience.com)
  • α-actinin belongs to the spectrin protein superfamily. (sigmaaldrich.com)
  • 2] H. Lopez, J.F. Rodriguez, Microstructural model for cyclic hardening in F-actin networks crosslinked by -actinin. (polimi.it)
  • α-Actinin involvement in Z-disk assembly during skeletal muscle C2C12 cells in vitro differentiation. (nih.gov)
  • In smooth muscle, α-actinin is identified in dense bodies and plaques characteristic of tissues whereas it is associated with z-discs that define muscle sarcomas in normal skeletal muscle. (sigmaaldrich.com)
  • Remarkably, the remaining 18% of the healthy European population-and more than a billion people worldwide-have two copies of the nonfunctional 577X variant (the XX genotype), resulting in complete deficiency of α-actinin-3 protein in their skeletal muscle ( 9 ). (lww.com)
  • These individuals have a complete absence of α-actinin-3, which appears to reduce the proportion of fast-twitch muscle fibers and increase the proportion of slow-twitch fibers in the body. (medlineplus.gov)
  • Top row movies: Z-stacks of live hiPS cells expressing mEGFP-tagged ß-actin (left), α-actinin (center) and non-muscle myosin heavy chain IIB (right) imaged on a spinning-disk confocal microscope. (allencell.org)
  • Representative images of mEGFP tagged ß-actin (left), α-actinin (center) and non-muscle myosin heavy chain IIB (right) from the bottom (top row) and tops (bottom row) of cells. (allencell.org)
  • Myosin IIB localization is similar to that of actin and α -actinin, residing in prominent filaments primarily at the bottom and top of cells. (allencell.org)
  • In summary, α-actinin localizes to a subset of actin (e.g. the actin bundles) and myosin IIB to a yet smaller subset (actomyosin bundles) as expected. (allencell.org)
  • Monoclonal anti-α-actinin antibody can be used in immunoblotting to study the membrane anchorage sites and immunochemical identification of α-actinin. (sigmaaldrich.com)
  • Mouse anti-α-actinin antibody reacts specifically with chicken fibroblasts. (sigmaaldrich.com)
  • A variant in this gene, called R577X, leads to production of an abnormally short α-actinin-3 protein that is quickly broken down. (medlineplus.gov)
  • The gene for this protein occurs in two variants, R and X. Variant X (or more specifically, R577X) carries information for the cell causing muscle protein α-actinin-3 deficiency. (gentrend.cz)
  • The α-actinin-2 protein is present predominantly in the aerobically working muscle fibers, giving the muscle greater endurance. (gentrend.cz)
  • U.S. are exposed to attaching/effacing enteropathogens merized actin, -actinin, talin, and ezrin (2). (cdc.gov)
  • Immunofluorescence of cardiomyocytes from neonatal and adult mouse hearts was performed using monoclonal mouse anti-α actinin (clone EA-53) at 1:1000. (sigmaaldrich.com)
  • Quantitative mapping of N-termini demonstrated perturbation of protease action during podocyte injury in vitro, including diminished proteolysis of a-actinin-4. (uni-koeln.de)
  • Mutations in the α-actinin gene is observed in heterogeneous hypertrophic cardiomyopathy and in juvenile onset atrial fibrillation. (sigmaaldrich.com)
  • Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. (sasbdb.org)
  • Serologic evidence of a history of trichomonosis was assessed by a recombinant Trichomonas vaginalis α-actinin IgG ELISA. (aacrjournals.org)
  • It can also be used in immunofluorescence to study the localization of α-actinin in cultured cells and tissues. (sigmaaldrich.com)
  • α -actinin localization is almost identical to ß-actin. (allencell.org)
  • Figure 3: Frequency dependence of elastic modulus (solid) and viscous modulus (open) for different concentrations of (A) wild-type and (B) mutant α-actinin-4 for different molar concentrations of cross-linker. (harvard.edu)
  • actinin bound synthetic astaxanthin in a molar ratio of 1.11:1.00. (canada.ca)
  • using ApoE (pan) (D7I9N) Rabbit mAb (upper) and α-Actinin (D6F6) XP ® Rabbit mAb #6487 (lower). (cellsignal.com)
  • Western blot analysis of extracts from various cell lines using ARID1B/BAF250B (E9J4T) Rabbit mAb (upper) and α-Actinin (D6F6) Rabbit mAb #6487 (lower). (cellsignal.com)
  • Similar to human α-actinin, calcium-binding occurs to the most N-terminal EF-hand motif in the calmodulin-like C-terminal domain. (scilifelab.se)
  • The gene encoding α-actinin is mapped to the human chromosome 11q13.2. (sigmaaldrich.com)
  • The image shows a single isolated Wistar rat cardiomyocyte stained against α-actinin, displaying its periodic structure localized at the ends of sarcomeres (Z-discs). (tocris.com)
  • These rods contain the Z-line protein, α-actinin, that can be effectively stained in skeletal muscles using Gomori or Masson trichrome and negatively stained with periodic acid-Schiff. (scielo.org.za)
  • This is not a pathogenic issue as its deficiency is effectively compensated by the related protein α-actinin-2. (gentrend.cz)
  • Affixin interacts with a-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction. (nii.ac.jp)
  • α-actinin, an actin binding protein, plays a key role in cell migration, cross-links actin filaments in the Z-disk, and is a major component of contractile muscle apparatus. (techscience.com)
  • α-actinin is a 100kD actin binding protein found in muscle as well as non-muscle cells. (sigmaaldrich.com)
  • α−actinin regulates muscle contraction and cytoskeletal organization. (sigmaaldrich.com)
  • The precise functions of α-actinin-3 are still unknown but are likely to include a structural role in the maintenance of muscle mechanical integrity and possibly other functions related to muscle signaling and metabolism ( 8 ). (lww.com)
  • Additionally, I will be investigating the roles of focal adhesion molecule α-actinin in neutrophil recruitment and arrest. (brown.edu)
  • has been postulated that decreased mobilization of calcium actinin are distributed over the lateral cricoarytenoid m. (psm.edu)
  • α -actinin crosslinks actin filaments, forming actin bundles. (allencell.org)
  • The main difference is that α -actinin localizes less strongly to the lamellipodia at the protruding edges at the bottom of the cells, where there are fewer bundles. (allencell.org)
  • α-Actinin-1 promotes activity of the L-type Ca2+ channel Cav 1.2. (ucdavis.edu)
  • Analysis of the primary sequence indicate that this protein has the same domain structure as other α-actinins, a N-terminal actin-binding domain and a C-terminal calmodulin-like domain. (scilifelab.se)