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.
They are oval or bean shaped bodies (1 - 30 mm in diameter) located along the lymphatic system.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
The interstitial fluid that is in the LYMPHATIC SYSTEM.
The technique of placing cells or tissue in a supporting medium so that thin sections can be cut using a microtome. The medium can be paraffin wax (PARAFFIN EMBEDDING) or plastics (PLASTIC EMBEDDING) such as epoxy resins.
A hemoflagellate parasite affecting domestic and wild animals, as well as humans and invertebrates. Though it induces an immune response, it is non-pathogenic in humans and other vertebrates. It is cross-reactive with TRYPANOSOMA CRUZI and can thus cause false positives for CHAGAS DISEASE.
The use of instrumentation and techniques for visualizing material and details that cannot be seen by the unaided eye. It is usually done by enlarging images, transmitted by light or electron beams, with optical or magnetic lenses that magnify the entire image field. With scanning microscopy, images are generated by collecting output from the specimen in a point-by-point fashion, on a magnified scale, as it is scanned by a narrow beam of light or electrons, a laser, a conductive probe, or a topographical probe.
Surgical excision of one or more lymph nodes. Its most common use is in cancer surgery. (From Dorland, 28th ed, p966)

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)

Actinin is a protein that belongs to the family of actin-binding proteins. It plays an important role in the organization and stability of the cytoskeleton, which is the structural framework of a cell. Specifically, actinin crosslinks actin filaments into bundles or networks, providing strength and rigidity to the cell structure. There are several isoforms of actinin, with alpha-actinin and gamma-actinin being widely studied. Alpha-actinin is found in the Z-discs of sarcomeres in muscle cells, where it helps anchor actin filaments and maintains the structural integrity of the muscle. Gamma-actinin is primarily located at cell-cell junctions and participates in cell adhesion and signaling processes.

Creatine kinase (CK) is an enzyme found in various tissues in the body, including the heart, brain, and skeletal muscles. It plays a crucial role in energy metabolism by catalyzing the conversion of creatine and adenosine triphosphate (ATP) to phosphocreatine and adenosine diphosphate (ADP). This reaction helps regenerate ATP, which is the primary source of energy for cellular functions.

There are three main isoforms of CK in the human body: CK-MM, CK-MB, and CK-BB. The BB form of creatine kinase (CK-BB) is primarily found in the brain and is present in very low concentrations in other tissues. It is mainly located in the cytosol of neurons and glial cells.

An elevated level of CK-BB in the blood can indicate damage to the central nervous system, particularly in cases of stroke, traumatic brain injury, brain tumors, or neurodegenerative disorders like multiple sclerosis and Alzheimer's disease. However, it is essential to note that CK-BB levels alone are not considered a definitive diagnostic marker for these conditions, as other factors can influence its concentration in the bloodstream. Measurement of CK-BB, along with other biomarkers and clinical assessments, contributes to a more comprehensive understanding of the patient's condition.

Microfilament proteins are a type of structural protein that form part of the cytoskeleton in eukaryotic cells. They are made up of actin monomers, which polymerize to form long, thin filaments. These filaments are involved in various cellular processes such as muscle contraction, cell division, and cell motility. Microfilament proteins also interact with other cytoskeletal components like intermediate filaments and microtubules to maintain the overall shape and integrity of the cell. Additionally, they play a crucial role in the formation of cell-cell junctions and cell-matrix adhesions, which are essential for tissue structure and function.

Lymph nodes are small, bean-shaped organs that are part of the immune system. They are found throughout the body, especially in the neck, armpits, groin, and abdomen. Lymph nodes filter lymph fluid, which carries waste and unwanted substances such as bacteria, viruses, and cancer cells. They contain white blood cells called lymphocytes that help fight infections and diseases by attacking and destroying the harmful substances found in the lymph fluid. When an infection or disease is present, lymph nodes may swell due to the increased number of immune cells and fluid accumulation as they work to fight off the invaders.

Confocal microscopy is a powerful imaging technique used in medical and biological research to obtain high-resolution, contrast-rich images of thick samples. This super-resolution technology provides detailed visualization of cellular structures and processes at various depths within a specimen.

In confocal microscopy, a laser beam focused through a pinhole illuminates a small spot within the sample. The emitted fluorescence or reflected light from this spot is then collected by a detector, passing through a second pinhole that ensures only light from the focal plane reaches the detector. This process eliminates out-of-focus light, resulting in sharp images with improved contrast compared to conventional widefield microscopy.

By scanning the laser beam across the sample in a raster pattern and collecting fluorescence at each point, confocal microscopy generates optical sections of the specimen. These sections can be combined to create three-dimensional reconstructions, allowing researchers to study cellular architecture and interactions within complex tissues.

Confocal microscopy has numerous applications in medical research, including studying protein localization, tracking intracellular dynamics, analyzing cell morphology, and investigating disease mechanisms at the cellular level. Additionally, it is widely used in clinical settings for diagnostic purposes, such as analyzing skin lesions or detecting pathogens in patient samples.

Lymph is a colorless, transparent fluid that circulates throughout the lymphatic system, which is a part of the immune and circulatory systems. It consists of white blood cells called lymphocytes, proteins, lipids, glucose, electrolytes, hormones, and waste products. Lymph plays an essential role in maintaining fluid balance, absorbing fats from the digestive tract, and defending the body against infection by transporting immune cells to various tissues and organs. It is collected from tissues through lymph capillaries and flows through increasingly larger lymphatic vessels, ultimately returning to the bloodstream via the subclavian veins in the chest region.

Tissue embedding is a process in histology (the study of the microscopic structure of tissues) where biological tissue samples are encased in a supporting medium, typically paraffin wax or plastic resins, to maintain their shape and structural integrity during sectioning. This allows for thin slices of the embedded tissue to be cut using a microtome, mounted on slides, and then stained for further examination under a microscope. The embedding process ensures that the tissue remains intact and does not tear or compress during sectioning, providing clear and consistent samples for analysis.

Trypanosoma rangeli is a species of protozoan parasite that belongs to the family Trypanosomatidae. It is primarily found in various insects, particularly in triatomine bugs (also known as "kissing bugs"), which serve as its vectors. This parasite is closely related to another more well-known species called Trypanosoma cruzi, which causes Chagas disease in humans and other mammals.

Unlike T. cruzi, however, T. rangeli is not typically associated with causing severe or life-threatening diseases in humans. In fact, most human infections with T. rangeli are considered to be asymptomatic or mildly symptomatic. Some people may experience localized reactions, such as swelling and redness at the site of the insect bite, while a small number of cases might develop fever, headache, or muscle pain.

It is important to note that although T. rangeli infections are generally not harmful to humans, they can still have significant impacts on public health by complicating the diagnosis and treatment of Chagas disease, which can be caused by T. cruzi. The two species can co-infect both vectors and mammalian hosts, making it difficult to distinguish between them based on clinical symptoms or laboratory tests alone.

In summary, Trypanosoma rangeli is a protozoan parasite that primarily infects insects but can also be found in humans and other mammals. While it is not typically associated with severe disease in humans, its presence can complicate the diagnosis and management of Chagas disease caused by T. cruzi.

Microscopy is a technical field in medicine that involves the use of microscopes to observe structures and phenomena that are too small to be seen by the naked eye. It allows for the examination of samples such as tissues, cells, and microorganisms at high magnifications, enabling the detection and analysis of various medical conditions, including infections, diseases, and cellular abnormalities.

There are several types of microscopy used in medicine, including:

1. Light Microscopy: This is the most common type of microscopy, which uses visible light to illuminate and magnify samples. It can be used to examine a wide range of biological specimens, such as tissue sections, blood smears, and bacteria.
2. Electron Microscopy: This type of microscopy uses a beam of electrons instead of light to produce highly detailed images of samples. It is often used in research settings to study the ultrastructure of cells and tissues.
3. Fluorescence Microscopy: This technique involves labeling specific molecules within a sample with fluorescent dyes, allowing for their visualization under a microscope. It can be used to study protein interactions, gene expression, and cell signaling pathways.
4. Confocal Microscopy: This type of microscopy uses a laser beam to scan a sample point by point, producing high-resolution images with reduced background noise. It is often used in medical research to study the structure and function of cells and tissues.
5. Scanning Probe Microscopy: This technique involves scanning a sample with a physical probe, allowing for the measurement of topography, mechanical properties, and other characteristics at the nanoscale. It can be used in medical research to study the structure and function of individual molecules and cells.

Lymph node excision is a surgical procedure in which one or more lymph nodes are removed from the body for the purpose of examination. This procedure is often conducted to help diagnose or stage various types of cancer, as malignant cells may spread to the lymphatic system and eventually accumulate within nearby lymph nodes.

During a lymph node excision, an incision is made in the skin overlying the affected lymph node(s). The surgeon carefully dissects the tissue surrounding the lymph node(s) to isolate them from adjacent structures before removing them. In some cases, a sentinel lymph node biopsy may be performed instead, where only the sentinel lymph node (the first lymph node to which cancer cells are likely to spread) is removed and examined.

The excised lymph nodes are then sent to a laboratory for histopathological examination, which involves staining and microscopic evaluation of the tissue to determine whether it contains any malignant cells. The results of this examination can help guide further treatment decisions and provide valuable prognostic information.

... is a microfilament protein. Alpha-actinin-1 is necessary for the attachment of actin myofilaments to the Z-lines in ... ISBN 978-0-08-092427-4. Actinin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with ... Both ends of the rod-shaped alpha-actinin dimer contain actin-binding domains. Mutations in ACTN4 can cause the kidney disease ... The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. ACTN2 expression is found in both cardiac ...
... is a protein which in humans is encoded by the ACTN2 gene. This gene encodes an alpha-actinin isoform that is ... The high-resolution crystal structure of human alpha-actinin 2 at 3.5 Å was recently resolved. Alpha actinins belong to the ... Alpha-actinin-2 is a 103.8 kDa protein composed of 894 amino acids. Each molecule is rod-shaped (35 nm in length) and it ... Alpha-actinin 2 has been shown to interact with KCNA5, DLG1, DISC1, MYOZ1, GRIN2B, ADAM12, ACTN3, MYPN, PDLIM3, PKN, MYOT, TTN ...
... is a protein that in humans is encoded by the ACTN4 gene. Alpha actinins belong to the spectrin gene ... Vallenius T, Luukko K, Mäkelä TP (2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4 ... "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. UNITED STATES. 275 (15): ... Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal ...
... is a protein that in humans is encoded by the ACTN1 gene. Alpha actinins belong to the spectrin gene ... 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". ... "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100-5. doi: ... "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol ...
... , also known as alpha-actinin skeletal muscle isoform 3 or F-actin cross-linking protein, is a protein that in ... ACTN3 has been shown to interact with alpha-actinin-2. Actinin GRCh38: Ensembl release 89: ENSG00000248746 - Ensembl, May 2017 ... have no alpha-actinin-3 (16%-20% of the population), but they have a high level of alpha-actinin-2. There is an association ... The alpha-actinin-3 protein is found in type II muscle fibers. An allele (rs1815739; 577X) has been identified in the ACTN3 ...
... 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 ... Alpha-actinin is an actin-bundling protein known to regulate several types of ion channels. Planer lipid bilayer ... The TRPP3-alpha-actinin association was documented by co-immunoprecipitation using native cells and tissues, yeast two-hybrid, ...
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 ...
Actinin is a microfilament protein. Alpha-actinin-1 is necessary for the attachment of actin myofilaments to the Z-lines in ... ISBN 978-0-08-092427-4. Actinin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with ... Both ends of the rod-shaped alpha-actinin dimer contain actin-binding domains. Mutations in ACTN4 can cause the kidney disease ... The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. ACTN2 expression is found in both cardiac ...
Alpha-Actinin regulates nuclear actin bundling and nuclear size in early G1 Nuclear actin and its biological relevance raised ... We therefore decided to investigate non-muscle Alpha actinins and their roles in early G1 nuclei. We initially confirmed ... These nuclei further represented fewer actin filament bundles with reduced widths, suggesting that Alpha actinin-4 is a key ... Expression of a nuclear targeted dominant negative mutant of Alpha actinin-4 exhibited a significant reduction of phalloidin- ...
Actinin alpha 1) mouse monoclonal antibody, clone OTI7A4 (formerly 7A4) ... alpha-actinin (Actinin alpha 1) mouse monoclonal antibody, clone OTI7A4 (formerly 7A4) ...
Neutrophilia refers to a higher than normal number of neutrophils. Neutrophilia may result from a shift of cells from the marginal to the circulating pool (shift neutrophilia) without an increase in the total blood granulocyte pool (TBGP) or from a true increase in TBGP size (true neutrophilia).
Red indicates alpha-actinin, green indicates RyR , blue indicates DAPI. Scale bar: 200 µm. Download Figure 2-2, TIF file ... Intensity measurements of both alpha-actinin and Ryanodine Receptor (RyR) revealed an opposing stripe-like structure indicating ... α-actinin (Sigma-Aldrich, A5044; 1:400), Tau5 (Abcam, ab80579; 1:500) MAP2 (Millipore, ab5622; 1:500) were diluted in blocking ...
actinin alpha 4. involved_in. ISO. (PMID:25918384). UniProt. PMID:25918384. NCBI chrNW_004624794:12,042,627...12,113,762 ...
enables muscle alpha-actinin binding IBA Inferred from Biological aspect of Ancestor. more info ... Enables alpha-actinin binding activity; protein homodimerization activity; and protein phosphatase binding activity. Involved ...
Rob Partons lab contains the insert alpha actinin 2 and is published in Nat Commun. 2020 Jul 24;11(1):3711. doi: 10.1038/ ... Addgene NGS found R52H, S412T, R500K, S567P, V721A, and E770K amino acid mutations within the alpha actinin 2 translation that ...
α-Actinin is loading control. Representative images from three biological replicates shown. Raw unprocessed gel images are ... GAPDH and α-Actinin are loading controls. Representative images from three biological replicates shown. Raw unprocessed gel ...
IOD of α-actinin band at 103 kDa was quantified as loading control. IOD ratio (cMyBP-C/α-actinin) from one donor sample (blue ... cMyBP-C and α-actinin were detected by incubation with antibodies against the N-terminus of cMyBP-C or against α-actinin, ... In contrast, α-actinin (Figure 3C, middle column) or β-MyHC (Supplementary Figure 6) as markers for sarcomere alignment showed ... B) Relative protein amount of cMyBP-C was calculated from IOD of the cMyBP-C band divided by IOD of α-actinin for normalization ...
Among these proteins, 4 candidate markers actinin 1, actinin 4, protein DJ-1, and cathepsin B were validated by WB and IHC ... K. Honda, T. Yamada, R. Endo et al., "Actinin-4, a novel actin-bundling protein associated with cell motility and cancer ... overexpression of actinin 4 in cytoplasm is correlated to various clinicopathological parameters in certain human cancers [138 ... analysis [136]. α-actinin, an actin binding protein, is essential for remodeling of actin filament which promotes cell motility ...
Mouse monoclonal antibody raised against native actinin-alpha.. Application. WB, IHC-P, IHC-Fr ...
CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ. 1s35. Crystal Structure of Repeats 8 and 9 of Human ... Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin. 1u4q. Crystal Structure of Repeats 15, 16 and 17 of Chicken ... CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ. 1owa. Solution Structural Studies on Human Erythrocyte Alpha Spectrin N ... Solution structure of the third spectrin repeat of alpha-actinin-4. 2iak. Crystal Structure of a protease resistant fragment of ...
Visualisation and Quantification of Intracellular Interactions of Neisseria meningitidis and Human α-actinin by Confocal ... Visualisation and Quantification of Intracellular Interactions of Neisseria meningitidis and Human α-actinin by Confocal ...
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 ...
It is composed largely of the protein alpha actinin and anchors the thin filaments in the myofibril. A band is the longer ...
Front Physiol 2021; 12:725172 α-Actinin 4 Links Vasopressin Short-Term and Long-Term Regulation of Aquaporin-2 in Kidney ...
... and α-Actinin (D6F6) XP® Rabbit mAb #6487 (lower). Data were generated using the standard formulation of this product.. Show ... and α-Actinin (D6F6) XP® Rabbit mAb #6487 (lower). Data were generated using the standard formulation of this product.. ...
Immunostaining for alpha-actinin and myosin also showed more distinct striations and myofiber organization in anti-miR-133 BAMs ...
Alpha-Actinin-4 Supports B Cell Survival by Limiting Lateral BCR Mobility  Alsouri, Saed (2023-10-17) ...
Picture of light fixture 2 x 96W Actinin PCs & 2x 250 W MH will also add some LED stunner strips for moonlights.. ... Picture of light fixture 2 x 96W Actinin PCs & 2x 250 W MH will also add some LED stunner strips for moonlights.. ...
Actinin_actin-bd_CS. IPR001589. InterPro. CH-domain. IPR001715. InterPro. Ig-like_fold. IPR013783. InterPro. ...
1beta actin actinin blocks coactivator cytosol defective fails filtration focal fsgs glomerular glomerulosclerosis ikappabalpha ... 1beta actin actinin blocks coactivator cytosol defective fails filtration focal fsgs glomerular glomerulosclerosis ikappabalpha ... actinin, alpha 4. integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12). ...
ACTN1 Actinin, alpha 1. ACTN2 Actinin alpha 2. ACTN3 Actinin alpha 3. ACTN4 Actinin alpha 4. AJAP1 Adherens junction associated ...
GO:0051393 [alpha-actinin binding]. GO:0071805 [potassium ion transmembrane transport]. GO:0098914 [membrane repolarization ... GO:0051393 [alpha-actinin binding]. GO:0071805 [potassium ion transmembrane transport]. GO:0098914 [membrane repolarization ... GO:0051393 [alpha-actinin binding]. GO:0071805 [potassium ion transmembrane transport]. GO:0098914 [membrane repolarization ... GO:0051393 [alpha-actinin binding]. GO:0071805 [potassium ion transmembrane transport]. GO:0098914 [membrane repolarization ...
  • 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)
  • For instance, nucleocytoplasmic shuttling of the actin-bundling protein Alpha actinin-4 was associated with invasive cancer phenotypes. (uni-marburg.de)
  • We initially confirmed cytoplasmic and nuclear localization of Alpha actinin-4 in interphase and early G1 cells and its interaction with nuclear F-actin by immunostaining and phalloidin pulldown experiments. (uni-marburg.de)
  • These nuclei further represented fewer actin filament bundles with reduced widths, suggesting that Alpha actinin-4 is a key regulator of nuclear F-actin bundling and proper nuclear volume expansion in early G1. (uni-marburg.de)
  • U.S. are exposed to attaching/effacing enteropathogens merized actin, -actinin, talin, and ezrin (2). (cdc.gov)
  • The sarcomeres contain a number of proteins, including 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)
  • Mouse monoclonal antibody raised against native actinin-alpha. (abnova.com)
  • The non-sarcomeric alpha-actinins, encoded by ACTN1 and ACTN4, are widely expressed. (wikipedia.org)
  • Alpha-Actinin regulates nuclea. (uni-marburg.de)
  • G.O.4 α-Actinin-3 regulates muscle glycogen phosphorylase: A potential mechanism for the metabolic consequences of the common human null allele of ACTN3. (edu.au)
  • Actinin is a microfilament protein. (wikipedia.org)
  • 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 variant in this gene, called R577X, leads to production of an abnormally short α-actinin-3 protein that is quickly broken down. (medlineplus.gov)
  • Mutational analysis of ACTN4, encoding a-actinin 4, in patients with focal segmental glomerulosclerosis using HRM method. (cdc.gov)
  • We therefore decided to investigate non-muscle Alpha actinins and their roles in early G1 nuclei. (uni-marburg.de)
  • Subcellular fractionations and subsequent Co-immunoprecipitations revealed the presence of Alpha actinin-1 SNAP Flag in the nuclear compartment. (uni-marburg.de)
  • Imaging of histone 2B mCherry expressing cells during early G1 and following 3D reconstructions allowed for nuclear volume analysis and revealed that Alpha actinin-4, but not Alpha actinin-1 was required for proper nuclear volume expansion. (uni-marburg.de)
  • Expression of a nuclear targeted dominant negative mutant of Alpha actinin-4 exhibited a significant reduction of phalloidin-AlexaFluor647 localizations per nucleus compared to the wild-type construct. (uni-marburg.de)
  • Further investigations revealed an additional involvement of nuclear Alpha actinin-4 in other cellular processes such as proliferation. (uni-marburg.de)
  • Together, this work provides information about crucial functions of Alpha actinin-4 in the nuclear compartment of postmitotic mammalian cells and might therefore aid future investigations into its role for tumorigenesis and metastasis. (uni-marburg.de)
  • α - Actinins belong to the spectrin superfamily and are divided in four isoforms, encoded by different genes. (hypermol.com)
  • From NCBI Gene: Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. (nih.gov)
  • Alpha actinin is an actin-binding protein with multiple roles in different cell types. (nih.gov)
  • In an Actn3 knockout mouse model, alpha-actinin-3 deficiency is associated with a shift in the characteristics of fast, glycolytic 2B muscle fibers towards a slow phenotype, with decreased muscle mass and fiber diameter, slower contractile properties, increased fatigue resistance, and an increase in oxidative enzyme activity. (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)
  • The p.R577X polymorphism (rs1815739) in the ACTN3 gene causes individuals with the ACTN3 XX genotype to be deficient in functional α-actinin-3. (ufv.es)
  • Actinin-4, an isoform of non-muscular α-actinin, enhances cell motility by bundling the actin cytoskeleton. (medscape.com)
  • Isoform 2 and 3 - the so called 'muscle' α - actinins are constituents of sarcomeres in the cross-striated skeletal and cardiac muscle. (hypermol.com)
  • Isoform 1 and 4 are 'non-muscle' α - actinins and present in practically every tissue. (hypermol.com)
  • This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes. (nih.gov)
  • 5. Alpha-actinin 4 is associated with cancer cell motility and is a potential biomarker in non-small cell lung cancer. (nih.gov)
  • These include spectrin alpha and beta subunits [ ( PUBMED:12672815 ) ( PUBMED:15062087 ) ], alpha-actinin [ ( PUBMED:10481917 ) ] and dystrophin. (embl.de)
  • In turn, the shift towards a 'slow' muscle phenotype in fast muscle fibers likely explains why loss of alpha-actinin-3 is detrimental to sprint performance. (nih.gov)
  • the frequency of the XX genotype is significantly lower than controls in sprint athletes, and it appears that alpha-actinin-3 deficiency is detrimental to sprint performance. (nih.gov)
  • Why is alpha-actinin-3 deficiency so common in the general population? (nih.gov)
  • Exploring the relationship between α-actinin-3 deficiency and obesity in mice and humans. (edu.au)
  • The actinin-4 gene may be a target of the 19q amplicon, acting as a candidate oncogene, and serve as a predictor of poor outcome and tumor chemoresistance in patients with advanced-stage ovarian cancers. (medscape.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)
  • phosphorylation strongly inhibits interaction of GluR4 with α-Actinin-1 but has little effect on its interaction with IQGAP1. (elsevierpure.com)
  • Our findings strongly suggest an association between [Formula see text]- actinin -4 and AA-I nephrotoxic activity. (bvsalud.org)
  • 2. Serum Actinin-4 Levels as a Potential Diagnostic and Prognostic Marker in Cervical Cancer. (nih.gov)
  • [ 13 ] Multivariate analysis indicated that high actinin-4 expression can be a prognostic indicator that is independent of clinical stage and histologic subtype. (medscape.com)
  • 4. Increased expression of α-actinin-4 is associated with unfavorable pathological features and invasiveness of bladder cancer. (nih.gov)
  • These results suggest that α-Actinin-1 and IQGAP1 regulate GluR4 functions via their specific associations with GluR4. (elsevierpure.com)
  • Native α -actinin 1 from smooth muscle has a molecular mass of 200kDa and forms homodimers (2x100kDa). (hypermol.com)
  • α-Actinin-1 and IQGAP1 were identified to be GluR4-specific binding partners. (elsevierpure.com)
  • Single Nucleotide Polymorphism rs9277336 Controls the Nuclear Alpha Actinin 4-Human Leukocyte Antigen-DPA1 Axis and Pulmonary Endothelial Pathophenotypes in Pulmonary Arterial Hypertension. (ucdavis.edu)
  • Mapping experiments revealed that α-Actinin-1 and IQGAP1 bind to the same region within the C-terminus of GluR4 that contains a previously identified PKA phosphorylation site, Ser842, phosphorylation of which is regulated by synaptic activity. (elsevierpure.com)