Desmin Antibody Review

 

 

 

Introduction

  • a typical muscle cell marker. PMID: 16382987, PMID: 11738361

  • a muscle-specific structural protein, a key subunit of the intermediate filament in cardiac myocytes, skeletal muscle fibers and certain smooth muscle cells, and one of the earliest known muscle-specific genes to be expressed during cardiac and skeletal muscle development. PMID: 16160856, PMID: 15501438, PMID: 7565929

  • the main intermediate filament (IF) protein of muscle cells. In skeletal muscle, desmin IFs form a scaffold that interconnects the entire contractile apparatus with the subsarcolemmal cytoskeleton and cytoplasmic organelles. PMID: 16007273

  • the major muscle-specific intermediate filament (IF) protein, is essential for mitochondrial behavior, positioning and respiratory function and maintenance of healthy muscle. PMID: 15733906, PMID: 12536120, PMID: 10995435

  • play important role in the mechanical integrity and elasticity of muscle cells. PMID: 16714122

  • Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. PMID: 15558188

  • the muscle-specific member of the intermediate filament (IF) family, is one of the earliest known myogenic markers in both skeletal muscle and heart. PMID: 9113396

  • an early marker for chick somitic myogenesis. PMID: 8075431

  • normally located at Z-bands, beneath the sarcolemma, and prominently at neuromuscular junctions. It is abundant during myogenesis and in regenerating fibers, but decreases in amount with maturation. PMID: 8242173, PMID: 1285499, PMID: 1683724

Normal Expression

  • muscle-specific intermediate filament protein desmin is expressed in mononucleated myoblasts and in differentiated myotubes, associate with the sarcolemma in specific structures, such as neuromuscular junctions and the dystrophin-associated protein complex. PMID: 17036228

  • desmin is a structural protein that is expressed in smooth muscle cells of both airways and alveolar ducts. PMID: 16387753

  • the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. Desmin IFs are present throughout smooth, cardiac and skeletal muscle cells, but can be more concentrated in some particular structures, such as dense bodies, around the nuclei, around the Z-line or in costameres. PMID: 15558188

  • Desmin filaments are mainly located at the periphery of Z-disk of striated muscles and at the dense bodies of smooth muscle cells. PMID: 15501438

  • in normal condition, the desmin-positive pericytes are located around the endothelial cells of the capillary plexus and of larger vessels in the intermediate mesenchyme. PMID: 15219416

  • Desmin is not expressed in early stages of kidney growth, infant and adult kidneys, and proliferative and nonproliferative glomerulonephritis. PMID: 12092643

  • Coexpression of SM alpha-actin and desmin was observed in the pericytes of entire capillary segments, and SM alpha-actin was characterized by prominent filament bundles directed mainly at right angles to the capillary long axis. PMID: 11066040

  • during the initial stages of decidual transformation the desmin intermediate filaments accumulate around the nuclei, often forming caps around the nuclear envelope. As the decidual cells grow, the filaments form bundles and nets that radiate from the nuclei toward the cell surface. During the final stages of differentiation, on day 8 of pregnancy, staining of differentiated decidual cells decreases and most filaments accumulate under the cell surface. PMID: 10857484

  • Compared with vimentin, desmin discriminated mesothelial cells from other tissues except muscle cells. We conclude that desmin may be used in addition to cytokeratins and vimentin as a marker of peritoneal mesothelium. PMID: 9553808

  • expression of desmin was apparently more pronounced in process-lacking astrocytes and was considerably lower in process-bearing ones. In process-lacking astrocytes, in contrast to filamentous cytoplasmic staining for GFAP, the immunoreactivity for desmin was non-filamentous and was irregularly spread in the perinuclear cytoplasm of the cells, while in process-bearing astrocytes the pattern of staining for desmin was similar to that of GFAP. PMID: 9429301

  • A number of desmin filaments were closely associated with the nascent nonstriated myofibrils. Nascent myofibrils were distributed in the subsarcolemmal space at all three developmental stages. Desmin, accompanying the nascent myofibrils, was most abundant after 12 weeks of gestation. An irregular network of desmin filaments was conspicuous in the subsarcolemmal space after 20 weeks of gestation. Desmin filaments penetrated the myofibrils and the Z-discs after 29 weeks of gestation. PMID: 9041701

  • there is a fetal age (or gestation)-dependent expression of IFs in human fetal heart: desmin increases with increasing fetal age, whereas vimentin decreases. there is a fetal age (or gestation)-dependent expression of IFs in human fetal heart: desmin increases with increasing fetal age, whereas vimentin decreases. PMID: 8888968, PMID: 8876824

  • Interestingly, we also found desmin in immature intratubular Sertoli cells between weeks 11 and 14. In adult cryptorchid testes and in peritumour tubules, desmin was also prominently present in Sertoli cells in the vast majority of the cases investigated. PMID: 8624579

  • mesenchymal reticular cell, the basic supporting cell of the germinal center, was stained prominently by anti-vimentin and anti-desmin. Both antibodies stained the bursal cortex but only anti-vimentin bound the bursal secretory dendritic cell of the medulla. PMID: 8579258

  • Desmin-expressing cells were numerous in the liver from the embryonic period to the neonatal age. However, their absolute number per unit area, as well as their number relative to hepatocytes, decreased with age. We suggest that desmin-positive cells in embryonic liver may act as stromal cells in the hepatic hematopoietic microenvironment and support hepatocyte development. PMID: 8575647

  • highly expressed in immature muscle fibers, both during fetal life and regeneration as well as in certain congenital myopathies, together with vimentin. PMID: 7565929

  • In all ovaries, desmin immunoreactivity was restricted to smooth muscle cells in blood vessel walls. PMID: 7576613

  • major site of desmin localization was the bundle of filaments connecting Z-discs of adjacent myofibrils. These desmin filaments were localized not only between but also within myofibrils. PMID: 7548400

  • Both desmin and vimentin expression were observed during the early weeks of pregnancy (3-6 weeks). These two types of IFs were also detected in short-term cultures in a filamentous fashion either within the cell body or at cellular attachment plaques. When decidual cells were cultured for longer periods (40-60 days), the expression of desmin dramatically declined while vimentin expression was maintained in a rather diffuse and more abundant fashion. The in situ expression of desmin and vimentin in later weeks of gestation (7-10 weeks) correlated with immunofluorescence staining of long-term cultured cells in that desmin staining was very weak and mostly undetectable where vimentin expression persisted and was evenly distributed throughout the entire stroma. PMID: 7638108

  • Desmin and vimentin are two intermediate filaments, abundant in fetal skeletal muscle, almost undetectable in mature skeletal muscle which increase in regenerating and partially damaged skeletal muscle fibers. PMID: 7749334

  • An unusual type of stromal cells has been found to be abundantly present in chorionic villi of human placenta of gestational weeks 6, 17, 35-42 and in tissues of early stages of fetal development (gestational weeks 16-21). These mesenchymal cells are loosely arranged throughout the villous interior and contain the intermediate filament (IF) proteins vimentin and desmin. PMID: 8034134

  • Early somite desmin expression was detected by whole-mount in situ confocal microscopy. No detectable somite desmin was observed in embryos of 15 somites (Stage 12) or younger. In embryos having between 16 and 26 somites (Stages 12-15), desmin could be detected in somites positioned increasingly more caudal in the embryo. Finally, in embryos of 27 somites (Stage 16) and older, somite desmin expression was consistently present in all but the caudal-most six somites. Although the rate of somite formation is fairly constant, the rate of observed somite desmin expression progressing caudally in the embryo is greater initially than the rate of segmentation. After an embryo has formed about 27 somites, the rate of desmin appearance parallels the rate of segmentation at a distance of about six somites. PMID: 8288867

  • Immunolocalization of desmin in fetal rat livers shows that on day 12 of gestation a high number of liver cells express desmin. This number decreases from day 14 onward. On day 20 about the same density of desmin-containing cells is found in fetal rat livers as is found in adult rat livers. PMID: 7679087

  • Desmin is present in proliferating rat muscle satellite cells but not in bovine muscle satellite cells. PMID: 1744177

  • During the development of the embryo, desmin was first detected at 8.25 d.p.c. in the ectoderm, where it was transiently coexpressed with keratin and vimentin. At later stages, the ectoderm contained only keratin and to a certain extent also vimentin IF. PMID: 2693040

  • immunohistochemistry of intermediate filaments allows for the differentiation between fat-storing cells, which are desmin- and vimentin-positive, and myofibroblasts or fibroblasts, which are desmin-negative but vimentin-positive. Smooth muscle cells are also vimentin-positive and become desmin-negative after the first passage. PMID: 3292636

  • Desmin-containing IFs were located in an axial bundle that partially surrounds the nucleus and were associated with numerous mitochondria near the poles of the nucleus. The bundle probably extends the length of the cell. Antibody labeling also showed concentrations of IF around and between cytoplasmic dense bodies (CDB) and also between CDB and membrane-associated dense bodies (MADB). PMID: 3191532

  • Pericytes in capillaries of cardiac muscle, exocrine pancreas, and kidney (peritubular capillary) were found to contain both desmin and vimentin. In some capillaries where pericytes do not exist, cells apposed to endothelial cells--the Ito cell in the hepatic sinusoid and the reticular cell in the splenic sinusoid--were shown to contain both of the intermediate filament proteins. PMID: 3305702

  • Endothelial cells of the peritubular capillary in the renal cortex, the hepatic sinusoid, and the splenic sinusoid were found to contain only desmin; those of the exocrine pancreas capillary contained both desmin and vimentin; and the endothelial cells of the macrovasculatures and of all the other microvasculatures examined, including the vasa recta of the renal medulla, contained only vimentin. PMID: 3539944

  • In adult human and rat testis, the peritubular myoid cell layer was brightly positive for desmin, the muscle type of intermediate filament protein. The desmin-positive myoid cell layer could already be identified in newborn rat testis but was more compact in appearance 23 days after birth. Both squash preparations and cultured cells from adult rat seminiferous tubules revealed distinct cell populations positive for desmin. PMID: 3518542

  • In rat brain and spinal cord, GFA protein and desmin were selectively localized in astrocytes. Neurons and axons were not stained. PMID: 7037941

  • desmin antigen is located almost entirely between Z-lines of adjacent parallel myofibrils and that there is no obvious correlation between locations of T-tubules and desmin structures. The electron-dense reaction product often followed an approximately linear course between Z-lines of adjacent myofibrils and indicated the desmin antibodies had decorated a small number of filaments spanning this region. PMID: 7035176

Abnormal Expression

  • in one case, we observed typical desmin-positive chondrocytes in the layer of cartilage filling the defect of the articular cartilage surface. PMID: 16382987

  • Desmin and EMA appear to be the most useful markers in distinguishing benign from malignant mesothelial proliferations. Desmin appears to be preferentially expressed in reactive mesothelium and EMA appears to be preferentially expressed in neoplastic mesothelium. PMID: 12940775

  • Desmin appears at 6-12 h post-injury and becomes the predominant IF in myofibers simultaneously with the appearance of cross-striations. PMID: 11398835

  • Ductular epithelial cells in cholangiocarcinoma were positive for keratin, with desmin and actin positive ductular walls. Presumptive perisinusoidal cells in primarily trabecular and schirrous hepatocellular carcinoma were also actin positive. Only one spindle cell proliferative lesion was positive for any of the antibodies (desmin). PMID: 7767965

  • muscle immunocytochemical studies in sporadic, adult onset myotubular myopathy (SAOMM), which show intramyofibrillar central, perinuclear desmin and vimentin. PMID: 1283202

  • Vimentin and desmin are both strongly expressed in fetal myotubes and their immunohistochemical demonstration persists until 36 weeks' gestation. These cytoskeletal proteins are uniformly expressed in myofibers of neonates with X-linked recessive myotubular myopathy. Desmin but not vimentin is diffusely increased in infantile cases of myotonic dystrophy, in some cases of congenital muscle fiber-type disproportion, and in cerebrohepatorenal disease. In nemaline rod myopathy, desmin is focally increased in perinuclear zones and in regions of aggregated rods. The small myofibers in infantile spinal muscular atrophy show increased vimentin and desmin in the subsarcolemmal region. PMID: 1641160

  • desmin is located in the filamentous core of cellular processes at myotendinous junctions at sites 30 nm or more from the membrane. This core lies deep to subsarcolemmal material previously shown to contain talin, vinculin, and dystrophin. The distance from desmin to the membrane suggests desmin does not interact directly with membrane proteins at the junction. PMID: 1544366

  • Muscle biopsy showed sarcoplasmic accumulation of desmin filaments leading to diagnosis of desmin storage myopathy. PMID: 1483042

  • In fibres which had undergone neurogenic atrophy, cytoplasmic lectin binding was seen only with Griffonia simplicifolia 1 lectin, and desmin was expressed more strongly than in normal fibres. PMID: 2809885

Expression Alteration

  • cytoskeletal protein desmin increases in response to a high-tension, concentric-only load consequent to sprint training. Desmin appears to increase as the force generating capacity of the muscle increases. PMID: 15468102

  • myocardial tissue of patients with end-stage heart failure of ischaemic origin, shows a decreased number in desmin-positive myocytes at immunochemistry evaluation compared to normal individuals. PMID: 15182762

  • expression of desmin is very often upregulated rather than downregulated in many cardiac diseases. Altered distribution of desmin protein has been observed in dilated cardiomyopathy, as well as desminopathies to which a number of mutations of desmin and a missense mutation of alphaB-crystallin (CryAB) have been linked. PMID: 12555134

  • first desmin-, MyoD1- and myogenin-positive myoblasts were seen after 12 hours, but satellite cell proliferation was not seen until 24 hours after the injury. PMID: 7898053

  • Disarrayed myofibers from all specimens of HCM showed the following abnormalities in the pattern of desmin intermediate filament distribution: (1) decrease or loss of labeling of intercalated discs and Z bands, (2) longitudinal arrangement of desmin intermediate filaments, and (3) intense, granular staining of several myocytes. This spectrum of desmin alterations was never observed in disarrayed myofibers in specimens of toF or acquired myocardial hypertrophy or in EMBs. Altered distribution of desmin intermediate filaments seems to be specific to myofiber disarray in HCM and it may play a role in the altered myocyte arrangement in HCM. PMID: 7890275

  • altered arrangement of desmin filaments in the disarrayed cardiac muscle fibers may play a role in the altered contractility that occurs in patients with HCM. PMID: 1374188

  • Desmin staining is lost at an early stage of necrosis and is present at an early stage of regeneration. Desmin staining in combination with morphometrical assessment of the rate of fusion and growth of regenerating fibres provides a powerful method for evaluating the processes of muscle regeneration in experimental situations. PMID: 3171773

  • Using immunohistochemical methods, we have confirmed that the perisinusoidal cells in rat liver express the intermediate filament protein, desmin. A significant increase in desmin-positive cells was observed in areas of necrosis as early as 48 h following the administration of a single bolus of carbon tetrachloride. This reached a peak at 72 h, with a five-fold increase in desmin-positive cells in areas of necrosis. PMID: 3783322

Function

  • desmin is a load-bearing protein that stiffens the airways and consequently the lung and modulates airway contractile response. PMID: 16387753

  • functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. PMID: 15558188

  • lack of the intermediate filament system decreases isometric stress production and that the desmin knockout muscle is less vulnerable to mechanical injury. PMID: 11003592

  • desmin immunoreactivity, in the absence of other muscle-associated protein expression, might be considered a clue to the diagnosis of the blastemal WT. PMID: 9310952

  • combined results strengthen the view that desmin (within a strictly defined context of round cell tumours in young people) is a reliable marker for rhabdomyoblastic differentiation. PMID: 2558065, PMID: 2798221

  • desmin intermediate filaments may have an important role in organization of the postsynaptic cytoplasm in rat muscle. PMID: 2740991

  • desmin is a useful marker for immunohistochemical identification of canine leiomyomas and leiomyosarcomas. PMID: 3300003

  • Desmin is a specific marker for rhabdomyosarcomas of human and rat origin. PMID: 3881039, PMID: 6177091

Applications

 

Electron Microscopy (EM)

  • Desmin accumulation was diagnosed by means of ultrastructural and immunocytochemical studies of EMB in four unrelated probands with RCM and AVB. PMID: 16376610

  • Using postembedding immunogold labeling of Lowicryl sections and immunogold labeling of ultrathin cryosections, we show that plectin is associated with desmin IFs linking myofibrils to mitochondria at the level of the Z-disc and along the entire length of the sarcomere. PMID: 10527638

  • light and electron microscopy and immunohistochemistry were used to establish the presence of desmin cardiomyopathy. PMID: 9502648

  • A quantitative immunohistochemical study using light and electron microscopy was carried out to evaluate the morphological and quantitative distribution of the peritubular cells that immunoreact with actin, vimentin and desmin, alone or in combinations, in normal adult testes and the changes in these cells in elderly men. PMID: 9227372

  • Using 10nm gold-particle-labeling immunoelectron microscopy, desmin intermediate filaments were localized in skeletal muscles of 12, 20 and 29-week-old human fetuses. PMID: 9041701

  • By double-labeling immunoelectron microscopy, desmin and vimentin intermediate filaments were localized in developing skeletal muscles of 20-29-week-old human fetuses. PMID: 8876824

  • we reevaluate the light microscopic and ultrastructural features of the myopathy with abnormal foci of desmin positivity. PMID: 8627346

  • A porcine antibody was used to clarify the localization of desmin filaments in the swine longissimus muscle by post-embedding immuno-electron microscopy. PMID: 7548400

  • Immunoelectron microscopy using colloidal gold showed that the dense amorphous material reacted strongly with desmin antisera and could, therefore, represent a defective or phosphorylated form of the protein. PMID: 7676812

  • Cytoplasmic body myopathy: familial cases with accumulation of desmin and dystrophin. An immunohistochemical, immunoelectron microscopic and biochemical study. PMID: 7484090

  • Immunohistologic and electron microscopic abnormalities of desmin and dystrophin in familial cardiomyopathy and myopathy. PMID: 7747013

  • We have used monoclonal antibodies to desmin and titin, and a combination of immunofluorescence and immunogold labelling to study the disposition of these two proteins in normal human muscle fibres and in fibres at various stages of degeneration in dystrophic muscle. PMID: 1557948

  • Myopathy associated with desmin type intermediate filaments. An immunoelectron microscopic study. PMID: 2926442

  • Microtubules and desmin filaments during onset of heart hypertrophy in rat: a double immunoelectron microscope study. PMID: 2953507

  • Distributions of vimentin and desmin in developing chick myotubes in vivo. II. Immunoelectron microscopic study. PMID: 3884634

  • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken cardiac muscle. PMID: 6406518

  • Immunoelectron microscopic studies of desmin (skeletin) localization and intermediate filament organization in chicken skeletal muscle. PMID: 6343403

  • Detection of desmin-containing intermediate filaments in cultured muscle and nonmuscle cells by immunoelectron microscopy. PMID: 6339515

  • Immunoelectron and immunofluorescence localization of desmin in mature avian muscles. PMID: 7035176

ELISA

  • Desmin was selectively expressed in decidualized stroma, as demonstrated by SDS-PAGE analysis and positive response with a monoclonal antibody specific for desmin in ELISA and in western blot analysis. PMID: 2056017

Immunocytochemistry (ICC)

  • a high resolution immunocytochemical method was used to investigate the changes of desmin and actin in human muscles following a bout of eccentric exercise that lead to DOMS 2-3 days post-exercise. PMID: 12189520

  • immunocytochemical (ICC) staining for desmin on 65 fine needle aspiration biopsies from 45 patients with rhabdomyosarcoma, using the avidin-biotin-peroxidase complex method (ABC), and two types of antibodies, D33 and DE-R-11. PMID: 10877277

  • Our studies show a heterogeneity of staining within the cultured heart cells when various anti-desmin and anti-vimentin antibodies are used. PMID: 8056617

  • The expression patterns of low and high molecular weight cytokeratins (LCK and HCK) vimentin and desmin were investigated by immunocytochemistry in the rete testis and epididymis in the dog. PMID: 7512542

  • To investigate the in vitro development of myofibrils in skeletal muscle cells derived from adult human muscle biopsies, immunohistochemical analysis was performed using monoclonal antibodies against desmin, titin, and nebulin. PMID: 8186663

  • Using antibodies to desmin and vimentin, we studied by immunoperoxidase technique the distribution of these proteins in subcultured SMCs derived from porcine aorta and coronary artery. PMID: 2261944

  • Immunocytochemistry of eye lens cells from transgenic mice coexpressing desmin and vimentin reveals that the transgenic desmin expression is not uniform. PMID: 2076709

Immunofluorescence (IF)

  • we have analyzed the association between desmin filaments and the outer nuclear surface in nuclei isolated from pectoral skeletal muscle of chick embryos and in primary chick myogenic cell cultures by using immunofluorescence microscopy, negative staining, immunogold, and transmission electron microscopy. PMID: 16160856

  • We used indirect immunofluorescence microscopy and reverse transcription polymerase chain reaction (RT-PCR) to analyze desmin distribution and expression in C2C12 cells grown in the presence or absence of EGTA. PMID: 16007273

  • expression of actin, myosin, desmin, alpha-actinin, titin, and troponin using immunofluorescence microscopy of zebrafish (Danio rerio) embryos. PMID: 12128209

  • Colocalization of nestin and vimentin/desmin in skeletal muscle cells demonstrated by three-dimensional fluorescence digital imaging microscopy. PMID: 7925640

  • architecture of desmin intermediate filament arrangements in cultured cardiomyocytes from heart of normal and cardiomyopathic hamsters was studied by immunofluorescent light microscopy and immunogold replica electron microscopy. PMID: 1796736

  • Desmin expression by myoblasts cultured from embryonic and adult chicken breast muscle was examined employing indirect immunofluorescence. PMID: 2292359

  • presence of desmin, regarded as a marker of myogenic cells, in glomerular epithelial cells (GECs) of the kidney was studied in four strains of rat (SHR, Lewis, Fischer 344, WKA) by immunofluorescence microscopy and immunoelectron microscopy. PMID: 2183627

  • Immunofluorescent, immunogold, and electrophoretic studies for desmin in embryonic hearts of normal and cardiac mutant Mexican axolotls, Ambystoma mexicanum. PMID: 2681791

  • Immunofluorescent localization of desmin and vimentin in developing cardiac muscle of Syrian hamster. PMID: 2653108

  • Immunofluorescence and immunogold electron microscopy of desmin in isolated adult heart myocytes of the rat. PMID: 2681089

  • expression of desmin and vimentin in 35 "smooth muscle tumors" of the digestive tract was investigated using formalin-fixed and paraffin-embedded materials and the indirect immunoperoxidase method. PMID: 3400467

  • Immunofluorescence studies on the distributions of vimentin and desmin in embryonic rat cardiac muscle cells in culture were carried out, using antibodies against vimentin and desmin. PMID: 3525015

  • distribution of desmin, and alpha-actinin was studied in vivo growing rat heart myocytes and in vitro cultured heart myocytes using double indirect immunofluorescence labelling. PMID: 3904718

  • Distributions of vimentin and desmin in developing chick myotubes in vivo. I. Immunofluorescence study. PMID: 6373787

Immunohistochemistry (IHC)

  • To evaluate the immunoexpression of desmin and actins in spindle cell lipomas of different histological subtypes a retrospective immunohistochemical study of 25 spindle cell lipomas using archival formalin-fixed, paraffin-embedded tissue was performed. PMID: 15322874

  • We studied 100 consecutive cases of dermatofibroma using hematoxylin-eosin-stained sections and immunoperoxidase staining with antibodies against desmin, SM-MHC, and smooth muscle actin. PMID: 12296754

  • Immunohistochemical analysis of development of desmin-positive hepatic stellate cells in mouse liver. PMID: 11197537

  • evaluate the utility of immunohistochemical stains for desmin in discriminating mesothelial cells from adenocarcinoma in serous fluid cell block preparations. PMID: 11127755

  • distribution of vimentin- and desmin-positive cells in the budgerigar (Melopsittacus undulatus) dermis was investigated by means of immunohistochemical reactivity with the commercially available (Euro-Diagnostics) polyclonal antibodies. PMID: 9334495

  • distribution of desmin and fibronectin in the chick embryo gonad in and after sexual differentiation was investigated immunohistochemically. PMID: 9271454

  • Biopsies were sectioned and successive sections stained immunohistochemically with antibodies for actin or desmin. Image analysis was used to quantify the proportion of smooth muscle fibres in the cavernous tissue. PMID: 8800897

  • distribution of the intermediate filament (IF) proteins desmin, keratin, and vimentin was studied immunohistochemically in bovine ovaries. PMID: 7576613

  • D33 desmin clone used with the EPOS method is more reliable for identifying desmin filaments in tumours than other desmin antibodies tested. Different desmin clones using a routine technique label different rhabdomyosarcoma cells and therefore it is justifiable to use more than one clone. PMID: 7665696

  • Expression of these markers might vary considerably and immunoperoxidase stainings need to be carefully evaluated. Utilization of several antibodies directed against different desmin epitopes might be advantageous. PMID: 7520048

  • distribution of keratin, vimentin, desmin, muscular actin, S100, specific neuron enolase, and chromogranin was studied by immunoperoxidase staining in mesothelium, malignant mesotheliomas, and pulmonary carcinomas. PMID: 7520015

  • Immunohistochemical distribution of vimentin, desmin, glial fibrillary acidic protein and neurofilament proteins in feline tissues. PMID: 8085393

  • Immunohistochemical techniques determined the chronology and positions of desmin expression during early craniofacial development. PMID: 1525013

  • Comparative immunohistochemical staining for desmin and muscle-specific actin. A study of 576 cases. PMID: 1712542

  • Expression of vimentin, desmin, alpha-sarcomeric and alpha-smooth muscle actins in embryonic tissues of rat and mice was examined using an immunohistochemical approach. PMID: 2283002

  • We localized desmin at human neuromuscular junctions (NMJs) using specific anti-desmin monoclonal and polyclonal antibodies. PMID: 2189082

  • purpose of this study was to analyze normal ovaries, ovarian stromal tumors (fibroma/thecomata and granulosa cell tumors), and ovarian leiomyomata for desmin reactivity. PMID: 2159271

  • Immunohistochemical localization of desmin in the quail ovary. Demonstration of a suspensory apparatus. PMID: 2715048

  • Coexpression of vimentin and desmin in gastric leiomyomas. An immunohistochemical study in paraffin sections. PMID: 2670616

  • Alveolar soft part sarcoma. Assessment of immunohistochemical demonstration of desmin using paraffin sections and frozen sections. PMID: 2499107

Western Blot (WB)

  • measurement of vimentin and desmin were done by Western blotting and densitometry. PMID: 16940012

  • A Western blot analysis for nestin, vimentin, and desmin demonstrated their exclusive expression in glomeruli and showed their increase in expression in nephrotic glomeruli. PMID: 16418842

  • By Western blot analyses, 53-kDa desmin and 54-kDa vimentin were present in all fetal heart tissues examined. PMID: 8888968

  • occurrence of the intermediate filament desmin in ovary and corpus luteum of pseudopregnant rats was studied using Western blot analysis and immunohistochemistry. PMID: 8452038

  • two rosette-forming primitive neuroectodermal tumors that were found to contain desmin by both immunohistochemistry and Western blotting. PMID: 1599027

  • Alpha-smooth-muscle actin and desmin were demonstrated in the S-type cloned cells by indirect immunofluorescence, as well as by 2-dimensional Western blot analysis. PMID: 2019470