Disease relevance of Des

• Mutations in desmin have been associated with a subset of human myopathies [1].
• When expressed in cultured rat neonatal cardiac myocytes via adenovirus infection, these mutant proteins disrupted the endogenous desmin filament to an extent that correlated with their defects in in vitro assembly properties [1].
• Microtubules and desmin filaments during onset of heart hypertrophy in rat: a double immunoelectron microscope study [2].
• Immunohistochemical analysis revealed that desmin-positive cells and alpha-sm-actin-positive cells were increased in the hepatic fibrosis, whereas neither cells were seen in livers of DMN-treated rats given dHGF [3].
• At the age of 11-21 weeks, all male mice carrying both genetic lesions developed embryonal rhabdomyosarcomas expressing desmin, myosin, and insulin-like growth factor-II, in the genitourinary tract [4].

High impact information on Des

• An increase in desmin and vimentin in mesangial regions was also noted [5].
• HSCs were characterized by expression of glial fibrillary acidic protein, desmin, and vascular cell adhesion molecule 1, which were almost completely absent in rat liver myofibroblasts [6].
• The electrocyte is filled up with a transversal network of intermediate filaments (IF) of desmin which contact in an end-on fashion both sides of the cell [7].
• Specific attachment of desmin filaments to desmosomal plaques in cardiac myocytes [8].
• Like cytokeratin filaments in epithelial cells, desmin filaments attach laterally to the desmosomal plaque [8].

Chemical compound and disease context of Des

• In CCl(4)-induced fibrosis, factor VIII-related antigen-positive blood vessels, desmin-, or alpha-smooth muscle actin (alphaSMA)-positive mesenchymal cells, bromodeoxyuridine (BrdU)-positive mesenchymal cells also decreased in number by treatment with TNP-470 [9].
• During induction of fibrosis by carbon tetrachloride, nestin-positive stellate cells appeared at 6 weeks, which was late in comparison with the induction of desmin and smooth muscle alpha-actin [10].
• The relationship of fibrosis to stellate cell activation was studied by staining of serial sections for alphaSMA, desmin, PDGFRbeta, and collagen, and by dual-staining for alphaSMA plus either Sirius Red or in situ hybridization for procollagen alpha(1) (I) mRNA [11].
• In aminonucleoside nephrosis, GECs showed extremely enhanced desmin staining in parallel with urinary protein excretion [12].
• METHODS: Immortalized rat proximal tubular cells (IRPTC) were cultured in normobaric hypoxia (1% O2) for 3, 6, or 15 days, with match control in normoxic conditions. alpha-SMA, vimentin, and desmin chosen as markers of EMT were measured by immunocytochemistry and immunoblots collagen I production and cell motility were chosen as functional assays [13].

Biological context of Des

• Serum hormone levels, histomorphometrical changes and immunoexpression of intermediate filaments (vimentin, cytokeratins and desmin), cadherins and proliferation cellular nuclear antigen were examined [14].
• S1 mapping reveals that the same transcription initiation site is used in all desmin mRNA containing tissues [15].
• Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis [16].
• Amino acid sequence predicted from 199E indicates that the 57 kd protein is a type III IF protein like vimentin and desmin [17].
• The cell phenotype was characterized by immunostaining and Western blot for alpha-actin and desmin [18].

Anatomical context of Des

• Immunohistochemical localization of desmin was restricted to the theca externa [14].
• Acute effects of desmin mutations on cytoskeletal and cellular integrity in cardiac myocytes [1].
• Northern analysis of RNA from different organs reveals that, as expected, desmin is expressed in striated, heart and smooth muscle cells containing tissues; among other tissues, lung displays relatively high expression levels, while desmin mRNA is barely detectable in spleen, kidney and liver [15].
• Desmin is a differentiation marker for all types of muscle cells [15].
• Both squash preparations and cultured cells from adult rat seminiferous tubules revealed distinct cell populations positive for desmin [19].

Associations of Des with chemical compounds

• Streptomycin and EDTA decrease the number of desmin-negative fibers following stretch injury [20].
• In passaged cultures we ascertained vascular smooth muscle purity of > 98% by morphology; contraction to norepinephrine and angiotensin; positive immunofluorescence staining through the sixth passage with monoclonal antibodies to smooth muscle-specific alpha- and gamma-isoactins, myosin, and desmin; and the absence of von Willebrand factor [21].
• Less than 10% of the desmin-positive cells were positive for vitamin A auto-fluorescence [22].
• Immunohistochemistry was used to identify proliferating (desmin-positive/bromodeoxyuridine (BrdU)-positive cells) and activated (alpha-smooth-muscle actin [alpha-SMA]-positive cells) HSCs [23].
• Chronic carbon tetrachloride exposure induced a spatial change in the expression of GFAP and desmin [24].

Enzymatic interactions of Des

• p21-activated kinase PAK phosphorylates desmin at sites different from those for Rho-associated kinase [25].

Co-localisations of Des

• Immunofluorescence analysis revealed that plectin was colocalized with desmin at the periphery of Z-discs [26].

Regulatory relationships of Des

• In all cases, when terminal myogenic differentiation is inhibited the basal levels of desmin and alpha 7 expression are not altered [27].
• Sequential changes of extracellular matrix and proliferation of Ito cells with enhanced expression of desmin and actin in focal hepatic injury [28].

Other interactions of Des

• The present study demonstrated that heparin recovered Ang receptors and differentiation markers, such as desmin, SM-22 and smooth muscle alpha-actin in VSMCs at the ninth passage [29].
• The analysis of neural agrin expression and myogenic desmin, myogenin, MyoD, Trisk 51, and nicotinic-acetycholine receptor (nACh-receptor) epsilon-subunit expression revealed the differentiation of the myoblasts to myofibers [30].
• We applied monoclonal antibodies recognizing desmin, sm-alpha-actin and smoothelin, a novel marker specific for the differentiated phenotype of SMC [31].
• Northern blot analysis showed that dHGF suppressed the increase of messenger RNA (mRNA) levels of procollagen alpha 2(I), alpha l(III), alpha 1(IV), transforming growth factor beta 1 (TGF-beta1), desmin (a marker of hepatic lipocytes), and alpha-smooth muscle (sm)-actin (a marker of activated hepatic lipocytes) [3].
• At 48 hours, we observed a collapse of PCs in the centrilobular zone, coinciding with strongly positive staining for IGF-II/M6P receptor in fat-storing cells (FSCs), identified by dual IGF-II/M6P receptor and desmin immunostaining [32].

Analytical, diagnostic and therapeutic context of Des

• The expression patterns of alpha-smooth muscle actin, myosin, desmin, vimentin, and collagen III and I were analyzed by immunohistochemistry and Western blotting [33].
• These collagen-positive cells were confirmed to be Ito cells by immunohistochemistry for desmin [34].
• The distribution of tubulin and desmin, the constituent proteins of microtubules and intermediate filaments, respectively, were studied in normal and hypertrophied rat myocardium by high-resolution immunofluorescence and immunoelectron microscopy [2].
• In the normal heart, double immunolabelling of ultrathin frozen sections of papillary muscle using gold-labelled probes for tubulin and desmin showed that microtubules ran primarily in a longitudinal direction through the intermyofibrillar spaces, perpendicularly to the desmin filaments [2].
• Immunocytochemistry with desmin antibodies combined with in situ hybridization on the same tissue sections identified the cells expressing high level of collagen type I transcripts as fat-storing cells [35].

References