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