Desmin
Intermediate Filaments
Vimentin
Intermediate Filament Proteins
Muscle Proteins
alpha-Crystallin B Chain
Myofibrils
Leiomyosarcoma
Actins
Cytoskeleton
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.
Desmin
Desmin Borges
Desmin-related myofibrillar myopathy
Hereditary inclusion body myopathy
Superior vena cava
MYH13
TPM2
List of OMIM disorder codes
Myosin-11
MYH9
MYH10
MYH14
MYH6
Angiofibroma of soft tissue
Plexiform angiomyxoid myofibroblastic tumor
SPTAN1
Widows (2018 film)
Widows (TV series)
Calponin 2
Private Life (2018 film)
Syncoilin
Intraglomerular mesangial cell
Undifferentiated pleomorphic sarcoma
Ectomesenchymal chondromyxoid tumor
Sarcoma botryoides
Intermediate filament
Rhabdomyoblast
List of Empire ships (U-Z)
Dynapenia
This Country
Desmin - Wikipedia
BITE profile - Desmin # beerintheevening.com
Des MGI Mouse Gene Detail - MGI:94885 - desmin
Desmin enters the nucleus of cardiac stem cells and modulates Nkx2.5 expression by participating in transcription factor...
Supplementation of a mutant keratin by stable expression of desmin in cultured human EBS keratinocytes
Desmin - Biophysics Group
Desmin; Clone D33 (Concentrate)
Association of syncollin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex. -...
Desmin 16' Skort - Diamond Geo
Desmin-positive malignant melanoma | Dermpedia
Mouse Des(Desmin) ELISA Kit - ELISA Reagent
Mouse Desmin Ready-To-Use IHC Kit - Bioss
Desmin Test | Desmin Test in Delhi, India | CNC Pathlab
ARG66873 anti-Desmin antibody [SQab21245] IHC-P image
Desmin Borges- Wiki, age, height, net worth, girlfriend, ethnicity - Australiabusinessblog.com
Book Immunohistochemistry Desmin Test Online, Home Collection, Price, Normal Range Max Lab
Lana Condor, Desmin Borges & more join Chase Stokes In 'Valiant One' - My Blog
MedlinePlus: Genes: D
Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal muscle fibers - Biophysics Group
Das Zelt-Heiligtum des Min. Rekonstruktion und Deutung eines fragmenta - Ugarit-Verlag - Buch- und Medienhandel GmbH
Retroperitoneal Fibrosis: Practice Essentials, Background, Pathophysiology
Retroperitoneal Fibrosis Clinical Presentation: History and Physical Examination
Cervical and peritoneal fluid cytology of uterine sarcomas
Carcinosarcoma of the liver producing granulocyte-colony stimulating factor
IRUCAA@TDC : Desmin and nerve terminal expression during embryonic development of the lateral pterygoid muscle in mice
Thomas Hartnett (OL) Stats, News, Rumors, Bio, Video - Dartmouth Big Green - Yahoo Sports
Compare antibodies lab reagents for research - National Centers for Biomedical Computing
Pathology of Nonmesothelial Cancers of the Pleura: Definition, Etiology, Epidemiology
SciELO - Brazil - Expression Pattern of Sulf1 and Sulf2 in Chicken Tissues and Characterization of Their Expression During...
Myopathy5
- 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)
Vimentin7
- 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)
Borges8
- Desmin Borges is a Mexican-American actor. (australiabusinessblog.com)
- Desmin Borges is known for his roles in You're the Worst (2014), Utopia (2020), Private Life (2018) and other films. (australiabusinessblog.com)
- Desmin Carl Borges was born on April 21, 1984 in Chicago, Illinois, in the United States. (australiabusinessblog.com)
- How much is Desmin Borges' net worth? (australiabusinessblog.com)
- Desmin Borges appeared in a number of movies and television series. (australiabusinessblog.com)
- Preacher played by Carlos Desmin Borges has not provided any information about his personal life. (australiabusinessblog.com)
- Who is Desmin Borges dating? (australiabusinessblog.com)
- Desmin Borges has not provided any information about his personal life. (australiabusinessblog.com)
Anti-Desmin1
- The tissue section was stained with ARG66873 anti-Desmin antibody [SQab21245] for 30 min at RT. (arigobio.cn)
Filaments5
- 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)
Immunohistochemistry1
- 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)
ELISA Kit1
- 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)
Extracellular matrix1
- 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)
Cardiac muscle2
- 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)
Proteins2
- 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)
Antibody1
- 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)
Skeletal muscle1
- 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)
Intermediate3
- 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)
Aggregation2
- 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)
Protein7
- 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)
Filament3
- 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)
Mitochondria4
- 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)
Knockout3
- 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)
Dysfunction2
- 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)
Decrease1
- 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)
Paraffin embedded1
- Immunohistochemical analysis of paraffin embedded mouse heart tissue slide using IHC0143M (Mouse Desmin IHC Kit). (biossusa.com)
Tissue3
- 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)
Expression2
- 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)
Mouse1
- 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)
Alpha1
- Autopsy revealed a liver carcinosarcoma composed both of hepatocellular carcinoma (HCC) and sarcomatous elements immunoreactive with alpha-smooth muscle actin and desmin. (nih.gov)
Cells1
- Quinacrine reduced the number of desmin-negative and albumin-positive cells by 88% (P (cdc.gov)
Shown1
- Desmin has been shown to interact with desmoplakin and αB-crystallin. (wikipedia.org)
Studies1
- Transfection studies show that desmin networks in different cell backgrounds are not equally affected. (worktribe.com)
Function1
- When desmin is not functioning properly there is improper mitochondrial distribution, number, morphology and function. (wikipedia.org)