An intermediate filament protein found predominantly in smooth, skeletal, and cardiac muscle cells. Localized at the Z line. MW 50,000 to 55,000 is species dependent.
Cytoplasmic filaments intermediate in diameter (about 10 nanometers) between the microfilaments and the microtubules. They may be composed of any of a number of different proteins and form a ring around the cell nucleus.
An intermediate filament protein found in most differentiating cells, in cells grown in tissue culture, and in certain fully differentiated cells. Its insolubility suggests that it serves a structural function in the cytoplasm. MW 52,000.
Filaments 7-11 nm in diameter found in the cytoplasm of all cells. Many specific proteins belong to this group, e.g., desmin, vimentin, prekeratin, decamin, skeletin, neurofilin, neurofilament protein, and glial fibrillary acid protein.
Acquired, familial, and congenital disorders of SKELETAL MUSCLE and SMOOTH MUSCLE.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.
The long cylindrical contractile organelles of STRIATED MUSCLE cells composed of ACTIN FILAMENTS; MYOSIN filaments; and other proteins organized in arrays of repeating units called SARCOMERES .
A sarcoma containing large spindle cells of smooth muscle. Although it rarely occurs in soft tissue, it is common in the viscera. It is the most common soft tissue sarcoma of the gastrointestinal tract and uterus. The median age of patients is 60 years. (From Dorland, 27th ed; Holland et al., Cancer Medicine, 3d ed, p1865)
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.

Specific and innervation-regulated expression of the intermediate filament protein nestin at neuromuscular and myotendinous junctions in skeletal muscle. (1/763)

The intermediate filament proteins nestin, vimentin, and desmin show a specific temporal expression pattern during the development of myofibers from myogenic precursor cells. Nestin and vimentin are actively expressed during early developmental stages to be later down-regulated, vimentin completely and nestin to minimal levels, whereas desmin expression begins later and is maintained in mature myofibers, in which desmin participates in maintaining structural integrity. In this study we have analyzed the expression levels and distribution pattern of nestin in intact and denervated muscle in rat and in human. Nestin immunoreactivity was specifically and focally localized in the sarcoplasm underneath neuromuscular junctions (NMJs) and in the vicinity of the myotendinous junctions (MTJs), ie, in regions associated with acetylcholine receptors (AChRs). This association prompted us to analyze nestin in neurogenically and myogenically denervated muscle. Immunoblot analysis disclosed a marked overall increase of accumulated nestin protein. Similar to the extrajunctional redistribution of AChRs in denervated myofibers, nestin immunoreactivity extended widely beyond the NMJ region. Re-innervation caused complete reversion of these changes. Our study demonstrates that the expression levels and distribution pattern of nestin are regulated by innervation, ie, signal transduction into myofibers.  (+info)

Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. (2/763)

Plectin is a versatile linker protein which is associated with various types of cytoskeletal components and/or filaments including intermediate filaments, and its deficiency causes the disruption of myofibrils, or muscular dystrophy. To better understand the functional role of plectin in skeletal muscle fibers, we have examined the topological and structural relationships of plectin to intermediate filaments and Z-discs in rat diaphragm muscles by confocal and immunoelectron microscopy. Immunofluorescence analysis revealed that plectin was colocalized with desmin at the periphery of Z-discs. This plectin localization around Z-discs was constantly maintained irrespective of the contracted or extended state of the muscle fibers, suggesting either direct or indirect association of plectin with Z-discs. Immunogold labeling in skinned muscle fibers clearly demonstrated that plectin-labeled fine threads linked desmin intermediate filaments to Z-discs and connected intermediate filaments to each other. These results indicate that through plectin threads desmin intermediate filaments form lateral linkages among adjacent Z-discs, preventing individual myofibrils from disruptive contraction and ensuring effective force generation.  (+info)

Myogenic signaling of phosphatidylinositol 3-kinase requires the serine-threonine kinase Akt/protein kinase B. (3/763)

The oncogene p3k, coding for a constitutively active form of phosphatidylinositol 3-kinase (PI 3-kinase), strongly activates myogenic differentiation. Inhibition of endogenous PI 3-kinase activity with the specific inhibitor LY294002, or with dominant-negative mutants of PI 3-kinase, interferes with myotube formation and with the expression of muscle-specific proteins. Here we demonstrate that a downstream target of PI 3-kinase, serine-threonine kinase Akt, plays an important role in myogenic differentiation. Expression of constitutively active forms of Akt dramatically enhances myotube formation and expression of the muscle-specific proteins MyoD, creatine kinase, myosin heavy chain, and desmin. Transdominant negative forms of Akt inhibit myotube formation and the expression of muscle-specific proteins. The inhibition of myotube formation and the reduced expression of muscle-specific proteins caused by the PI 3-kinase inhibitor LY294002 are completely reversed by constitutively active forms of Akt. Wild-type cellular Akt effects a partial reversal of LY294002-induced inhibition of myogenic differentiation. This result suggests that Akt can substitute for PI 3-kinase in the stimulation of myogenesis; Akt may be an essential downstream component of PI 3-kinase-induced muscle differentiation.  (+info)

A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin. (4/763)

BHK-21 fibroblasts contain type III vimentin/desmin intermediate filament (IF) proteins that typically co-isolate and co-cycle in in vitro experiments with certain high molecular weight proteins. Here, we report purification of one of these and demonstrate that it is in fact the type VI IF protein nestin. Nestin is expressed in several fibroblastic but not epithelioid cell lines. We show that nestin forms homodimers and homotetramers but does not form IF by itself in vitro. In mixtures, nestin preferentially co-assembles with purified vimentin or the type IV IF protein alpha-internexin to form heterodimer coiled-coil molecules. These molecules may co-assemble into 10 nm IF provided that the total amount of nestin does not exceed about 25%. However, nestin does not dimerize with types I/II keratin IF chains. The bulk of the nestin protein consists of a long carboxyl-terminal tail composed of various highly charged peptide repeats. By analogy with the larger neurofilament chains, we postulate that these sequences serve as cross-bridgers or spacers between IF and/or other cytoskeletal constituents. In this way, we propose that direct incorporation of modest amounts of nestin into the backbone of cytoplasmic types III and IV IFs affords a simple yet flexible method for the regulation of their dynamic supramolecular organization and function in cells.  (+info)

Dynamic distribution and formation of a para-sarcomeric banding pattern of prosomes during myogenic differentiation of satellite cells in vitro. (5/763)

Myogenesis proceeds by fusion of proliferating myoblasts into myotubes under the control of various transcription factors. In adult skeletal muscle, myogenic stem cells are represented by the satellite cells which can be cultured and differentiate in vitro. This system was used to investigate the subcellular distribution of a particular type of prosomes at different steps of the myogenic process. Prosomes constitute the MCP core of the 26S proteasomes but were first observed as subcomplexes of the untranslated mRNPs; recently, their RNase activity was discovered. A monoclonal antibody raised against the p27K subunit showed that the p27K subunit-specific prosomes move transiently into the nucleus prior to the onset of myoblast fusion into myotubes; this represents possibly one of the first signs of myoblast switching into the differentiation pathway. Prior to fusion, the prosomes containing the p27K subunit return to the cytoplasm, where they align with the gradually formed lengthwise-running desmin-type intermediate filaments and the microfilaments, co-localizing finally with the actin bundles. The prosomes progressively form discontinuous punctate structures which eventually develop a pseudo-sarcomeric banding pattern. In myotubes just formed in vitro, the formation of this pattern seems to preceed that produced by the muscle-specific sarcomeric (alpha)-actin. Interestingly, this pattern of prosomes of myotubes in terminal in vitro differentiation was very similar to that of prosomes observed in vivo in foetal and adult muscle. These observations are discussed in relation to molecular myogenesis and prosome/proteasome function.  (+info)

Transcriptional activity of MEF2 during mouse embryogenesis monitored with a MEF2-dependent transgene. (6/763)

The four members of the MEF2 family of MADS-box transcription factors, MEF2-A, MEF2-B, MEF2-C and MEF2-D, are expressed in overlapping patterns in developing muscle and neural cell lineages during embryogenesis. However, during late fetal development and postnatally, MEF2 transcripts are also expressed in a wide range of cell types. Because MEF2 expression is controlled by translational and post-translational mechanisms, it has been unclear whether the presence of MEF2 transcripts in the embryo reflects transcriptionally active MEF2 proteins. To define the temporospatial expression pattern of transcriptionally active MEF2 proteins during mouse embryogenesis, we generated transgenic mice harboring a lacZ reporter gene controlled by three tandem copies of the MEF2 site and flanking sequences from the desmin enhancer, which is active in cardiac, skeletal and smooth muscle cells. Expression of this MEF2-dependent transgene paralleled expression of MEF2 mRNAs in developing myogenic lineages and regions of the adult brain. However, it was not expressed in other cell types that express MEF2 transcripts. Tandem copies of the MEF2 site from the c-jun promoter directed expression in a similar pattern to the desmin MEF2 site, suggesting that transgene expression reflects the presence of transcriptionally active MEF2 proteins, rather than other factors specific for DNA sequences flanking the MEF2 site. These results demonstrate the presence of transcriptionally active MEF2 proteins in the early muscle and neural cell lineages during embryogenesis and argue against the existence of lineage-restricted MEF2 cofactors that discriminate between MEF2 sites with different immediate flanking sequences. The discordance between MEF2 mRNA expression and MEF2 transcriptional activity in nonmuscle cell types of embryos and adults also supports the notion that post-transcriptional mechanisms regulate the expression of MEF2 proteins.  (+info)

Activated stellate (Ito) cells possess voltage-activated calcium current. (7/763)

We previously reported stellate (Ito) cells possess voltage-activated Ca2+ current. The activation of stellate cells has been indicated to contribute to liver fibrosis and the regulation of hepatic hemodynamics. The aim of this study was to investigate the relationship between voltage-activated Ca2+ current and activation of stellate cells. Voltage-activated Ca2+ current in stellate cells isolated from rats were studied using whole-cell patch clamp technique. L-type voltage-activated Ca2+ current was hardly detected in stellate cells cultured for less than 9 days. Ca2+ current was detected 12.5 and 69% of cells at the 10th and 14th day of culture, respectively. BrdU incorporation indicated cell proliferation was recognized over 50% of cells at the 3rd and 5th day of culture, respectively, then decreased significantly in a time-dependent manner. On the other hand, the expression of alpha-smooth muscle actin indicated cell activation increased from 7th day of culture and collagen type I mRNA appeared remarkably in cells cultured for more than 10 days. In this study, we concluded L-type voltage-activated Ca2+ current was recognized in activated stellate (myofibroblast-like) cells.  (+info)

Cardiac microvascular endothelial cells express alpha-smooth muscle actin and show low NOS III activity. (8/763)

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)

Desmin is a type of intermediate filament protein that is primarily found in the cardiac and skeletal muscle cells, as well as in some types of smooth muscle cells. It is an important component of the cytoskeleton, which provides structural support to the cell and helps maintain its shape. Desmin plays a crucial role in maintaining the integrity of the sarcomere, which is the basic contractile unit of the muscle fiber. Mutations in the desmin gene can lead to various forms of muscular dystrophy and other inherited muscle disorders.

Intermediate filaments (IFs) are a type of cytoskeletal filament found in the cytoplasm of eukaryotic cells, including animal cells. They are called "intermediate" because they are smaller in diameter than microfilaments and larger than microtubules, two other types of cytoskeletal structures.

Intermediate filaments are composed of fibrous proteins that form long, unbranched, and flexible filaments. These filaments provide structural support to the cell and help maintain its shape. They also play a role in cell-to-cell adhesion, intracellular transport, and protection against mechanical stress.

Intermediate filaments are classified into six types based on their protein composition: Type I (acidic keratins), Type II (neutral/basic keratins), Type III (vimentin, desmin, peripherin), Type IV (neurofilaments), Type V (lamins), and Type VI (nestin). Each type of intermediate filament has a specific function and is expressed in different cell types. For example, Type I and II keratins are found in epithelial cells, while vimentin is expressed in mesenchymal cells.

Overall, intermediate filaments play an essential role in maintaining the structural integrity of cells and tissues, and their dysfunction has been implicated in various human diseases, including cancer, neurodegenerative disorders, and genetic disorders.

Vimentin is a type III intermediate filament protein that is expressed in various cell types, including mesenchymal cells, endothelial cells, and hematopoietic cells. It plays a crucial role in maintaining cell structure and integrity by forming part of the cytoskeleton. Vimentin is also involved in various cellular processes such as cell division, motility, and intracellular transport.

In addition to its structural functions, vimentin has been identified as a marker for epithelial-mesenchymal transition (EMT), a process that occurs during embryonic development and cancer metastasis. During EMT, epithelial cells lose their polarity and cell-cell adhesion properties and acquire mesenchymal characteristics, including increased migratory capacity and invasiveness. Vimentin expression is upregulated during EMT, making it a potential target for therapeutic intervention in cancer.

In diagnostic pathology, vimentin immunostaining is used to identify mesenchymal cells and to distinguish them from epithelial cells. It can also be used to diagnose certain types of sarcomas and carcinomas that express vimentin.

Intermediate filament proteins (IFPs) are a type of cytoskeletal protein that form the intermediate filaments (IFs), which are one of the three major components of the cytoskeleton in eukaryotic cells, along with microtubules and microfilaments. These proteins have a unique structure, characterized by an alpha-helical rod domain flanked by non-helical head and tail domains.

Intermediate filament proteins are classified into six major types based on their amino acid sequence: Type I (acidic) and Type II (basic) keratins, Type III (desmin, vimentin, glial fibrillary acidic protein, and peripherin), Type IV (neurofilaments), Type V (lamins), and Type VI (nestin). Each type of IFP has a distinct pattern of expression in different tissues and cell types.

Intermediate filament proteins play important roles in maintaining the structural integrity and mechanical strength of cells, providing resilience to mechanical stress, and regulating various cellular processes such as cell division, migration, and signal transduction. Mutations in IFP genes have been associated with several human diseases, including cancer, neurodegenerative disorders, and genetic skin fragility disorders.

Muscular diseases, also known as myopathies, refer to a group of conditions that affect the functionality and health of muscle tissue. These diseases can be inherited or acquired and may result from inflammation, infection, injury, or degenerative processes. They can cause symptoms such as weakness, stiffness, cramping, spasms, wasting, and loss of muscle function.

Examples of muscular diseases include:

1. Duchenne Muscular Dystrophy (DMD): A genetic disorder that results in progressive muscle weakness and degeneration due to a lack of dystrophin protein.
2. Myasthenia Gravis: An autoimmune disease that causes muscle weakness and fatigue, typically affecting the eyes and face, throat, and limbs.
3. Inclusion Body Myositis (IBM): A progressive muscle disorder characterized by muscle inflammation and wasting, typically affecting older adults.
4. Polymyositis: An inflammatory myopathy that causes muscle weakness and inflammation throughout the body.
5. Metabolic Myopathies: A group of inherited disorders that affect muscle metabolism, leading to exercise intolerance, muscle weakness, and other symptoms.
6. Muscular Dystonias: Involuntary muscle contractions and spasms that can cause abnormal postures or movements.

It is important to note that muscular diseases can have a significant impact on an individual's quality of life, mobility, and overall health. Proper diagnosis and treatment are crucial for managing symptoms and improving outcomes.

Muscle proteins are a type of protein that are found in muscle tissue and are responsible for providing structure, strength, and functionality to muscles. The two major types of muscle proteins are:

1. Contractile proteins: These include actin and myosin, which are responsible for the contraction and relaxation of muscles. They work together to cause muscle movement by sliding along each other and shortening the muscle fibers.
2. Structural proteins: These include titin, nebulin, and desmin, which provide structural support and stability to muscle fibers. Titin is the largest protein in the human body and acts as a molecular spring that helps maintain the integrity of the sarcomere (the basic unit of muscle contraction). Nebulin helps regulate the length of the sarcomere, while desmin forms a network of filaments that connects adjacent muscle fibers together.

Overall, muscle proteins play a critical role in maintaining muscle health and function, and their dysregulation can lead to various muscle-related disorders such as muscular dystrophy, myopathies, and sarcopenia.

Alpha-Crystallin B chain is a protein that is a component of the eye lens. It is one of the two subunits of the alpha-crystallin protein, which is a major structural protein in the lens and helps to maintain the transparency and refractive properties of the lens. Alpha-Crystallin B chain is produced by the CRYAB gene and has chaperone-like properties, helping to prevent the aggregation of other proteins and contributing to the maintenance of lens clarity. Mutations in the CRYAB gene can lead to various eye disorders, including cataracts and certain types of glaucoma.

Myofibrils are the basic contractile units of muscle fibers, composed of highly organized arrays of thick and thin filaments. They are responsible for generating the force necessary for muscle contraction. The thick filaments are primarily made up of the protein myosin, while the thin filaments are mainly composed of actin. Myofibrils are surrounded by a membrane called the sarcolemma and are organized into repeating sections called sarcomeres, which are the functional units of muscle contraction.

Leiomyosarcoma is a type of cancer that arises from the smooth muscle cells, which are responsible for the involuntary contractions of various organs and blood vessels. It most commonly occurs in the uterus, soft tissues (such as muscles and fat), and the gastrointestinal tract.

Leiomyosarcomas can vary in their aggressiveness and may spread to other parts of the body (metastasize) through the bloodstream or lymphatic system. The prognosis for leiomyosarcoma depends on several factors, including the location and size of the tumor, the patient's age and overall health, and the extent of metastasis. Treatment typically involves surgical removal of the tumor, along with radiation therapy and/or chemotherapy to help prevent recurrence or spread of the cancer.

Actin is a type of protein that forms part of the contractile apparatus in muscle cells, and is also found in various other cell types. It is a globular protein that polymerizes to form long filaments, which are important for many cellular processes such as cell division, cell motility, and the maintenance of cell shape. In muscle cells, actin filaments interact with another type of protein called myosin to enable muscle contraction. Actins can be further divided into different subtypes, including alpha-actin, beta-actin, and gamma-actin, which have distinct functions and expression patterns in the body.

The cytoskeleton is a complex network of various protein filaments that provides structural support, shape, and stability to the cell. It plays a crucial role in maintaining cellular integrity, intracellular organization, and enabling cell movement. The cytoskeleton is composed of three major types of protein fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. These filaments work together to provide mechanical support, participate in cell division, intracellular transport, and help maintain the cell's architecture. The dynamic nature of the cytoskeleton allows cells to adapt to changing environmental conditions and respond to various stimuli.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

... is a protein that in humans is encoded by the DES gene. Desmin is a muscle-specific, type III intermediate filament that ... In cardiac muscle, desmin is present in Z-discs and intercalated discs. Desmin has been shown to interact with desmoplakin and ... The function of desmin has been deduced through studies in knockout mice. Desmin is one of the earliest protein markers for ... However desmin knockout mice develop normally and only experience defects later in life. Since desmin is expressed at a low ...
"Desmin Borges-Resume". Retrieved October 6, 2016. Desmin Borges at IMDb Desmin Borges at the Internet Broadway Database v t e ( ... Desmin Borges (born 1983/1984) is an American actor. He is best known for playing Edgar Quintero on the FX/FXX comedy-drama ... "Desmin Borges returns to Teatro Vista in Freedom, NY". Time Out. May 10, 2011. Retrieved June 6, 2022. "FX Rounds Out Cast For ... Adams, Erik (October 1, 2015). "When the zombie apocalypse comes, expect to see You're the Worst's Desmin Borges in his ...
... , is a subgroup of the myofibrillar myopathy diseases and is the result of a mutation in ... Bär H, Strelkov SV, Sjöberg G, Aebi U, Herrmann H (November 2004). "The biology of desmin filaments: how do mutations affect ... Goldfarb LG, Vicart P, Goebel HH, Dalakas MC (April 2004). "Desmin myopathy". Brain. 127 (Pt 4): 723-34. doi:10.1093/brain/ ... the gene that codes for desmin which prevents it from forming protein filaments, instead forming aggregates of desmin and other ...
Desmin-Related Myopathy; DRM. Myofibrillar Myopathy With Arrhythmogenic Right Ventricular Cardiomyopathy. Desmin-Related ... The condition now called Desmin-related myofibrillar myopathy (also called myofibrillar myopathy-1) was formerly known as ... Alternative names: Myopathy, Myofibrillar, Desmin-Related. Desminopathy, Primary. ...
Sonavane, Sushilkumar K.; Milner, Desmin M.; Singh, Satinder P.; Abdel Aal, Ahmed Kamel; Shahir, Kaushik S.; Chaturvedi, ...
Actin, desmin, myosin, and tropomyosin". Am. J. Pathol. 142 (1): 221-30. PMC 1886840. PMID 8424456. v t e (Articles with short ...
Actin, desmin, myosin, and tropomyosin". The American Journal of Pathology. 142 (1): 221-30. PMC 1886840. PMID 8424456. Tiso N ...
... desmin-related, cardioskeletal; 601419; DES Myopathy, distal 2; 606070; MATR3 Myopathy, distal, with anterior tibial onset; ... desmin-related, with cataract; 608810; CRYAB Myopathy, centronuclear; 160150; DNM2 Myopathy, centronuclear; 160150; MYF6 ...
Actin, desmin, myosin, and tropomyosin". Am. J. Pathol. 142 (1): 221-30. PMC 1886840. PMID 8424456. New L, Jiang Y, Zhao M, et ...
Actin, desmin, myosin, and tropomyosin". The American Journal of Pathology. 142 (1): 221-30. PMC 1886840. PMID 8424456. Lalwani ...
Actin, desmin, myosin, and tropomyosin". The American Journal of Pathology. 142 (1): 221-30. PMC 1886840. PMID 8424456. ...
Actin, desmin, myosin, and tropomyosin". Am. J. Pathol. 142 (1): 221-30. PMC 1886840. PMID 8424456. Xu XR, Huang J, Xu ZG, et ...
Actin, desmin, myosin, and tropomyosin". The American Journal of Pathology. 142 (1): 221-30. PMC 1886840. PMID 8424456. Nakao K ...
... desmin protein in 22% of cases; ACTA2 (also termed α-SMA), CD34, and STAT6 proteins in 10% or fewer cases, and S100 and ...
Immunohistochemically, the tumour cells show positive staining for vimentin and smooth muscle actin (SMA). Focal desmin ...
Langley RC, Cohen CM (1986). "Association of spectrin with desmin intermediate filaments". J. Cell. Biochem. 30 (2): 101-9. doi ...
N'Duka, Amanda (May 8, 2017). "Manuel Garcia-Rulfo Cast In 'Widows'; Desmin Borges Joins Netflix Film 'Private Life'". Deadline ...
N'Duka, Amanda (8 May 2017). "Manuel Garcia-Rulfo Cast In 'Widows'; Desmin Borges Joins Netflix Film 'Private Life'". Deadline ...
Mabuchi K, Li B, Ip W, Tao T (1997). "Association of calponin with desmin intermediate filaments". The Journal of Biological ... Wang P, Gusev NB (1996). "Interaction of smooth muscle calponin and desmin". FEBS Letters. 392 (3): 255-8. doi:10.1016/0014- ... Calponin also binds tropomyosin, tubulin, desmin, Ca2+-calmodulin, Ca2+-S100, myosin, and phospholipids. Calponin also ...
Denis O'Hare and Desmin Borges subsequently joined the film as well. The film had its world premiere at the Sundance Film ... Dordick Emily Robinson as Charlotte Grimes John Carroll Lynch as Charlie Grimes Desmin Borges as Sam Francesca Root-Dodson as ... N'Duka, Amanda (May 8, 2017). "Manuel Garcia-Rulfo Cast In 'Widows'; Desmin Borges Joins Netflix Film 'Private Life'". Deadline ... Desmin Borges, and Denis O'Hare in supporting roles. The film focuses on Richard and Rachel, a middle-aged married couple of ...
... desmin, which suggests that a mutation in syncoilin might affect the bond between desmin and the sarcolemma. This may result in ... When there is a lack of either α-dystrobrevin or desmin, the expression of syncoilin is changed in order to compensate for the ... Later, a yeast two-hybrid method was used to demonstrate that syncoilin is a binding partner of desmin. These binding partners ... Syncoilin is found in skeletal and cardiac muscle which is similar to its binding protein desmin. The region of skeletal muscle ...
They are both vimentin and desmin positive. There are five known functions of intraglomerular mesangial cells: structural ...
Identification proteins for tumors that have been confused with UPS inlclude: Pleomorphic leimyosarcoma: Desmin and h-caldesmon ... i.e. high molecular form of caldesmon.) proteins Pleomorphic rhabdomyosarcoma: Desmin and myogenin proteins. Defifferentiated ...
Negative: Epithelial membrane antigen, desmin, p63 and calponin. Alcian blue will give a blue staining to the stromal matrix ...
Spindle-shaped tumor cells that are desmin positive.[citation needed] The disease used to be uniformly fatal, with a 5-year ...
Desmin IFs are structural components of the sarcomeres in muscle cells and connect different cell organells like the desmosomes ... April 2018). "Novel Desmin Mutation p.Glu401Asp Impairs Filament Formation, Disrupts Cell Membrane Integrity, and Causes Severe ... November 2019). "Restrictive Cardiomyopathy is Caused by a Novel Homozygous Desmin (DES) Mutation p.Y122H Leading to a Severe ... June 2019). "Noncompaction cardiomyopathy is caused by a novel in-frame desmin (DES) deletion mutation within the 1A coiled- ...
Variable levels of desmin are also reported among rhabdomyosarcomas. It has previously been suggested that there are four ... The detection of benign nerve sheath tumors, a dense Schwannian cell background, negative test results for desmin, myogenin and ... These neoplastic cells yield positive results for vimentin, smooth muscle actin, and desmin stains; however, myoglobin, myoD1 ... Immunohistochemistry techniques allow for the sensitive detection of desmin, vimentin, muscle specific actin, and MyoD1. ...
Sold in 1965 to Bulet, Bulgaria and renamed Desmin. Sold in 1968 to Navigation Maritime Bulgare, Bulgaria and renamed Stefan ...
Russ DW, Grandy JS (September 2011). "Increased desmin expression in hindlimb muscles of aging rats". Journal of Cachexia, ...
... ': Desmin Borges To Recur In Fox Comedy Series". Deadline Hollywood. 4 December 2020. "'This Country': Jason ... On 4 December 2020, Desmin Borges joined the cast in recurring role. On 30 December 2020, Jason MacDonald joined the cast in a ...
Desmin is a protein that in humans is encoded by the DES gene. Desmin is a muscle-specific, type III intermediate filament that ... In cardiac muscle, desmin is present in Z-discs and intercalated discs. Desmin has been shown to interact with desmoplakin and ... The function of desmin has been deduced through studies in knockout mice. Desmin is one of the earliest protein markers for ... However desmin knockout mice develop normally and only experience defects later in life. Since desmin is expressed at a low ...
Latest comments by Desmin. The Delacy Hotel, Bradford. Used to go with my uncle here in the early 70s...a pint & a fight, a ... Contact Desmin. You need to be logged in to send a message to this user. ...
View mouse Des Chr1:75336973-75345223 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Numbers of nuclei: mCherry, n=352; Desmin-mCherry, n=360; mCherry-Desmin, n=406. *P,0.0001. (C) Desmin-mCherry and desmin ... Numbers of nuclei: mCherry, n=352; Desmin-mCherry, n=360; mCherry-Desmin, n=406. *P,0.0001. (C) Desmin-mCherry and desmin ... 4C). In desmin over-expressing EBs with one additional RSV-driven desmin allele (des+/+desect), association of desmin with the ... desmin-ect.), containing the desmin cDNA under the control of the RSV promoter (Hofner et al., 2007); pshRNA desmin knock-down ...
The desmin mutation R349P increases contractility and fragility of stem cell-generated muscle micro-tissues. Category: Research ... The desmin mutation R349P increases contractility and fragility of stem cell-generated muscle micro-tissues 10. December 2021 ... comprise hereditary myopathies and cardiomyopathies caused by mutations in the intermediate filament protein desmin that lead ...
Scytek presents Desmin; Clone D33 (Concentrate) - A00007-C.1 ( Antibodies, Monoclonal Concentrates) ... Desmin; Clone D33 (Concentrate). Species: Mouse. Immunogen: Proteins from human Leiomyoma.. Clone: D33. Isotype: IgG1, kappa. ... Specificity: Desmin, Clone D33 detects cells of normal smooth, skeletal, and cardiac muscles. This antibody reacts with ...
Association of syncollin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex. ... Association of syncollin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex. ...
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... desmin-positive malignant melanoma. A not uncommon diagnostic pitfall. ...
Description: A sandwich ELISA kit for detection of Desmin from Mouse in samples from blood, serum, plasma, cell culture fluid ... Description: A sandwich quantitative ELISA assay kit for detection of Mouse Desmin (Des) in samples from tissue homogenates or ... Description: A sandwich quantitative ELISA assay kit for detection of Mouse Desmin (Des) in samples from tissue homogenates or ... Description: A sandwich quantitative ELISA assay kit for detection of Rat Desmin (Des) in samples from serum, plasma, tissue ...
Mouse Desmin Ready-To-Use IHC Kit Cat. No.: IHC0143MSample Type: FFPE tissue Size: 50T (including a control slide) Storage and ... The expression pattern of desmin in smooth muscle is much more heterogenous. Coexpression of vimentin and desmin has been ... Home › IHC Kits › Mouse Desmin Ready-To-Use IHC Kit Mouse Desmin Ready-To-Use IHC Kit. ... Mouse Desmin Ready-To-Use IHC Kit Cat. No.: IHC0143M. Sample Type: FFPE tissue Size: 50T (including a control slide) Storage ...
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... recognizes Desmin, which can be used for IHC-Formalin-fixed paraffin-embedded sections testing with Human s ... anti-Desmin 抗体 [SQab21245] is a 小鼠单克隆抗体 [SQab21245] ... anti-Desmin antibody [SQab21245]. anti-Desmin antibody [SQab21245] for IHC-Formalin-fixed paraffin-embedded sections and Human ... desmin. 背景介绍. This gene encodes a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable ...
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DES: desmin. *DGUOK: deoxyguanosine kinase. *DHCR7: 7-dehydrocholesterol reductase. *DHCR24: 24-dehydrocholesterol reductase ...
Start page /Publications /Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal muscle fibers ... article{RN2548, author = {Balogh, J. and Li, Z. and Paulin, D. and Arner, A.}, title = {Desmin filaments influence myofilament ... Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal muscle fibers. ...
Das Zelt-Heiligtum des Min. Rekonstruktion und Deutung eines fragmentarischen Modells (Kestner-Museum 1935.200.250). (MÄS 41). ... Startseite › Das Zelt-Heiligtum des Min. Rekonstruktion und Deutung eines fragmentarischen Modells (Kestner-Museum 1935.200.250 ...
Retroperitoneal fibrosis (RPF) is characterized by the development of extensive fibrosis throughout the retroperitoneum, typically centered over the anterior surface of the fourth and fifth lumbar vertebrae and resulting in entrapment and obstruction of retroperitoneal structures, notably the ureters. See the image below.
Retroperitoneal fibrosis (RPF) is characterized by the development of extensive fibrosis throughout the retroperitoneum, typically centered over the anterior surface of the fourth and fifth lumbar vertebrae and resulting in entrapment and obstruction of retroperitoneal structures, notably the ureters. See the image below.
Desmin / analysis * Desmin / immunology * Female * Genital Neoplasms, Female / diagnosis * Genital Neoplasms, Female / ...
... and sarcomatous elements immunoreactive with alpha-smooth muscle actin and desmin. Immunohistochemistry revealed positive ...
Desmin and nerve terminal expression during embryonic development of the lateral pterygoid muscle in mice. ...
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Staining for desmin is present as a perinuclear dot configuration. Up to 20% of DSRCTs may express CD99. DSRCT also usually ... Although rhabdomyosarcoma may sometimes stain for CD99, myogenic markers such as desmin, myogenin, or MyoD will be positive. [ ... 71, 72] Rare tumors may coexpress desmin or actin. Mesothelial markers such as calretinin are negative, as are epithelial ... Although usually negative for keratin, PNETs may stain focally for keratin, EMA, and desmin. CD99 is regarded as the most ...
4C). Desmin is the specific marker of skeletal muscle satellite cells. Thus, we examined the expression of this specific marker ... We found that 95% of cells were positive for the expression of desmin, which suggests that more than 95% of the cells were ... The primary antibody, mouse anti-chicken desmin (1:30 dilution, Abcam, USA), was added (diluted in PBS, 0.2%) at 4°C overnight ... a desmin protein that was specific to these cells was identified via the analysis of the immunocytochemistry of satellite cells ...
  • Desmin-related myofibrillar myopathy (DRM or desminopathy) is a subgroup of the myofibrillar myopathy diseases and is the result of a mutation in the gene that codes for desmin which by changing the protein structure prevents it from forming protein filaments, and rather, forms aggregates of desmin and other proteins throughout the cell. (wikipedia.org)
  • Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies. (arigobio.cn)
  • The R120G mutation in alphaB-crystallin causes desmin-related myopathy. (worktribe.com)
  • While desmin and αB-crystallin are not mutated in FA, the accumulation of these proteins in FA hearts allows the conclusion that FA cardiomyopathy is a desminopathy akin to desmin myopathy of skeletal muscle. (uni-muenster.de)
  • In 1980, desmin was noted to accumulate in the inclusions, and the name desmin storage myopathy was coined. (medscape.com)
  • A similar protein, vimentin, is present in higher amounts during embryogenesis while desmin is present in higher amounts after differentiation. (wikipedia.org)
  • Coexpression of vimentin and desmin has been observed in tumors derived from muscle tissue, i.e. rhabdomyosarcomas and leiomyosarcomas. (biossusa.com)
  • The second major area of investigation is to understand the role of cytoskeleton proteins, desmin and vimentin in smooth muscle contraction and mitochondrial respiration. (jefferson.edu)
  • In recent years research has shown that desmin and vimentin are involved in signaling pathways and they are the primary factors in facilitating the mechanotransduction. (jefferson.edu)
  • In addition, desmin and vimentin cytoskeleton interacts with mitochondria and possibly modulates respiration. (jefferson.edu)
  • Mitochondrial desmin and vimentin interacts with the VDAC and this interaction disrupts VDAC/MtCK/ANT complex formation, thereby inhibiting the ATP synthesis and promoting ROS production under pathological conditions in smooth muscle. (jefferson.edu)
  • My long term goal of this project is to elucidate our understanding of the mechanism by which desmin and vimentin induces mitochondrial and muscle dysfunction under pathological conditions in smooth muscle. (jefferson.edu)
  • The tissue section was stained with ARG66873 anti-Desmin antibody [SQab21245] for 30 min at RT. (arigobio.cn)
  • Desmin, as all intermediate filaments, shows no polarity when assembled. (wikipedia.org)
  • Desmin is a subunit of intermediate filaments in cardiac muscle, skeletal muscle and smooth muscle tissue. (wikipedia.org)
  • Here, we show that the mutation alters the in vitro binding characteristics of alphaB-crystallin for desmin filaments. (worktribe.com)
  • The apparent dissociation constant of R120G alphaB-crystallin was decreased while the binding capacity was increased significantly and as a result, desmin filaments aggregated. (worktribe.com)
  • These data suggest that the characteristic desmin aggregates seen as part of the disease histopathology can be caused by a direct, but altered interaction of R120G alphaB-crystallin with desmin filaments. (worktribe.com)
  • A proteomic analysis of heart proteins in FA cardiomyopathy by antibody microarray, Western blots, immunohistochemistry, and double-label laser scanning confocal immunofluorescence microscopy revealed upregulation of desmin and its chaperone protein, αB-crystallin. (uni-muenster.de)
  • Description: A sandwich ELISA kit for detection of Desmin from Mouse in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (elisareagents.com)
  • There is some evidence that desmin may also connect the sarcomere to the extracellular matrix (ECM) through desmosomes which could be important in signalling between the ECM and the sarcomere which could regulate muscle contraction and movement. (wikipedia.org)
  • In cardiac muscle, desmin is present in Z-discs and intercalated discs. (wikipedia.org)
  • In skeletal en cardiac muscle cells desmin is localized in the Z-disk region and at the intercalated disk. (biossusa.com)
  • Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. (wikipedia.org)
  • Association of syncollin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex. (ox.ac.uk)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Desmin (Des) in Tissue homogenates and other biological fluids. (elisareagents.com)
  • Regulation of desmin expression is stage and tissue-specific, since it is induced during terminal development of, for example, skeletal muscle cell differentiation. (biossusa.com)
  • Desmin is a muscle-specific, type III intermediate filament that integrates the sarcolemma, Z disk, and nuclear membrane in sarcomeres and regulates sarcomere architecture. (wikipedia.org)
  • Desminopathies comprise hereditary myopathies and cardiomyopathies caused by mutations in the intermediate filament protein desmin that lead to severe and often lethal degeneration of striated muscle tissue. (fau.de)
  • The typical features of eccentric exercise-induced muscle damage is prolonged loss of muscle strength and the most rapid structural change in the fibers is loss of immunostaining for the intermediate filament protein, desmin. (elsevierpure.com)
  • Some of these DES mutations cause an aggregation of desmin within the cytoplasm. (wikipedia.org)
  • Collectively, our data suggest that R120G alphaB-crystallin directly promotes desmin filament aggregation, although this gain of a function can be repressed by some cell situations. (worktribe.com)
  • Desmin is a protein that in humans is encoded by the DES gene. (wikipedia.org)
  • Desmin is a 53.5 kD protein composed of 470 amino acids, encoded by the human DES gene located on the long arm of chromosome 2. (wikipedia.org)
  • There are three major domains to the desmin protein: a conserved alpha helix rod, a variable non alpha helix head, and a carboxy-terminal tail. (wikipedia.org)
  • Desmin is one of the earliest protein markers for muscle tissue in embryogenesis as it is detected in the somites. (wikipedia.org)
  • Since desmin is expressed at a low level during differentiation another protein may be able to compensate for desmin's function early in development but not later on. (wikipedia.org)
  • No case stained positively for desmin or S100 protein. (lww.com)
  • Mitochondria and smooth muscle contraction: Role of desmin cytoskeleton protein. (jefferson.edu)
  • The N-terminal part of the 1A desmin subdomain is a genetic hot spot region for mutations affecting filament assembly. (wikipedia.org)
  • Description - Desmin is an i ntermediate filament present in smooth and striated muscle which is expressed in reactive mesothelial cells, myoblasts, myofibroblasts (variable), endometrial stroma, and smooth muscle cells. (cncpathlab.com)
  • Our data also clearly demonstrate the beneficial role of wild-type alphaB-crystallin in the formation of desmin filament networks. (worktribe.com)
  • Through its connection to the sarcomere, desmin connects the contractile apparatus to the cell nucleus, mitochondria, and post-synaptic areas of motor endplates. (wikipedia.org)
  • Finally, desmin may be important in mitochondria function. (wikipedia.org)
  • Since desmin links the mitochondria to the sarcomere it may transmit information about contractions and energy need and through this regulate the aerobic respiration rate of the muscle cell. (wikipedia.org)
  • In FA, desmin and αB-crystallin aggregate, causing chaotic modification of intercalated discs, clustering of mitochondria, and destruction of the contractile apparatus of cardiomyocytes. (uni-muenster.de)
  • Desmin was first described in 1976, first purified in 1977, the gene was cloned in 1989, and the first knockout mouse was created in 1996. (wikipedia.org)
  • The function of desmin has been deduced through studies in knockout mice. (wikipedia.org)
  • However desmin knockout mice develop normally and only experience defects later in life. (wikipedia.org)
  • A separate study examined this in more detail in cardiac tissue and found that murine hearts lacking desmin developed hypertrophic cardiomyopathy and chamber dilation combined with systolic dysfunction. (wikipedia.org)
  • Furthermore, during myocard dysfunction dramatic changes in the distribution of desmin have been observed. (biossusa.com)
  • Our results suggest that cooling during eccentric contractions may decrease desmin loss but temperature changes after eccentric contractions have no effect on desmin loss. (elsevierpure.com)
  • Immunohistochemical analysis of paraffin embedded mouse heart tissue slide using IHC0143M (Mouse Desmin IHC Kit). (biossusa.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Desmin (Des) in samples from tissue homogenates or other biological fluids. (elisareagents.com)
  • Desmin (approximately 53 kDa) exhibits a high degree of tissue specificity, its expression being predominantly confined to all types of muscle cells (cardiac, skeletal and smooth muscle). (biossusa.com)
  • Western blots of tissue lysates in FA cardiomyopathy reveal a truncated desmin isoprotein that migrates at a lower molecular weight range than wild type desmin. (uni-muenster.de)
  • In human heart failure, desmin expression is upregulated, which has been hypothesized to be a defense mechanism in an attempt to maintain normal sarcomere alignment amidst disease pathogenesis. (wikipedia.org)
  • The expression pattern of desmin in smooth muscle is much more heterogenous. (biossusa.com)
  • Description: A competitive ELISA for quantitative measurement of Mouse Desmin(DES) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (elisareagents.com)
  • Autopsy revealed a liver carcinosarcoma composed both of hepatocellular carcinoma (HCC) and sarcomatous elements immunoreactive with alpha-smooth muscle actin and desmin. (nih.gov)
  • Quinacrine reduced the number of desmin-negative and albumin-positive cells by 88% (P (cdc.gov)
  • Desmin has been shown to interact with desmoplakin and αB-crystallin. (wikipedia.org)
  • Transfection studies show that desmin networks in different cell backgrounds are not equally affected. (worktribe.com)
  • When desmin is not functioning properly there is improper mitochondrial distribution, number, morphology and function. (wikipedia.org)