Disease relevance of DES

• We have investigated the expression, using immunohistochemical and Western blot methods, of some cytoskeletal proteins including desmin, vimentin, actin, alpha-actinin, and ubiquitin in hereditary myopathy of the diaphragmatic muscles in Holstein-Friesian cattle (the histochemical and electron microscopical aspects have been previously reported) [1].
• We assayed antibodies against desmin, a cytoskeletal muscle protein, in 18 patients with acute infectious myopericarditis (AIM), in 24 patients with acute uncomplicated infections, in ten patients with acute myocardial infarction, and in 68 blood donors by an immunoenzymatic assay using purified desmin from Purkinje fibers of cow heart [2].
• Neoplastic cells showing intense staining for desmin, vimentin and proliferating cell nuclear antigen irrespective of their size differed from those in an embryonal rhabdomyosarcoma that exhibited a wide spectrum of differentiation, reminiscent of normal skeletal myogenesis [3].

High impact information on DES

• Smooth muscle cells of the digestive, respiratory, and urogenital tracts contain desmin as their major, if not exclusive, intermediate-size filament constituent and also show a predominance of gamma-type smooth muscle actin [4].
• Immunocytochemical studies with antibodies to smooth muscle specific actin, desmin, and vimentin demonstrated that cells within these foci, as well as tropoelastin mRNA-positive cells, were SMC [5].
• In contrast, both variants of desmin, synemin, caldesmon, and 5 cytosolic proteins are phosphorylated at varying rates and remain phosphorylated for the duration of carbachol action [6].
• The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin [7].
• We conclude that GFA protein and desmin are distinct with respect to primary structure, but probably represent two of the more closely related classes of intermediate filament proteins [8].

Biological context of DES

• This difference was not present if the time from first ovulation to conception was compared (50.5+/-5.3 versus 43.5+/-9.3 days, CON versus DES; P>0.05) [9].
• Using specific antibodies, we analyzed the expression of smooth muscle (SM) contractile and cytoskeletal proteins (alpha-SM-actin, SM myosin, calponin, desmin, and meta-vinculin) in the main pulmonary artery of fetal (60 to 270 days of gestation), neonatal, and adult animals [10].
• In contrast, forskolin, an adenylate cyclase activator and a potent smooth muscle relaxant, induces the phosphorylation protein 3 and one variant of desmin [6].
• In order to further examine the relationship between satellite cell differentiation and desmin expression, 5-bromo-2'-deoxyuridine (BrdU) was added to culture medium at the time of plating to inhibit differentiation [11].
• Application of desmin staining to rat satellite cell growth assays indicated that rat satellite cells cultured in serum-containing medium were contaminated with fibroblasts at levels that ranged from approximately 5% in 24 hr cultures to 15% in mature cultures [11].

Anatomical context of DES

• Purified glial fibrillary acidic protein and desmin are distinct intermediate filament proteins exhibiting similar properties [8].
• Glial fibrillary acidic (GFA) protein and desmin were purified from bovine brain and large intestine, respectively, and used in a comparison of the major protein components of two classes of intermediate filaments, the glial and smooth muscle filaments [8].
• In regenerating areas of the muscle many desmin-positive cells were present, and only a few cells stained positive for skeletal muscle myosin [11].
• Fibroblast colonies from both species were desmin-negative [11].
• In primary cultures, positive immunohistochemical staining for desmin and skeletal muscle myosin was observed in rat and bovine myotubes [11].

Associations of DES with chemical compounds

• Comparison of four levels of protein supplementation with and without oral DES on reproductive traits and testosterone of bulls [12].
• A number of DES cows showed a low and transient rise in plasma progesterone around 21 days after implant removal [9].
• It was insensitive to DES and ICI 182780, dependent on PKC and PLC, blocked by tamoxifen and it did not require gene transcription or translation [13].
• By sodium dodecyl sulfate-gel electrophoresis, GFA protein is about 5,000 daltons smaller than desmin [8].
• Bovine epidermal keratin IF, which are obligate heteropolymers, were thus characterized and compared with facultative heteropolymers of vimentin and desmin and with earlier observations of homopolymer vimentin IF [7].

Other interactions of DES

• Some cows displayed oestrus but did not appear to form a fully functional corpus luteum with this phenomenon being more prevalent among DES cows (7 of 37 versus 1 of 21; P<0.05) [9].
• Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle [14].
• The differentiation was studied by immunocytochemistry with specific antibodies for foetal, I, II (IIa and IIb), I and IIb, I and IIa myosin heavy chains (MHCs) and connectin respectively, and by immunoblotting with desmin antibody [15].
• Within 24 h of culture, vimentin rather than desmin was the predominant intermediate filament protein, with little change in alpha-actin content [16].

Analytical, diagnostic and therapeutic context of DES

• The excretion of DES in the urine and faeces was monitored using radioimmunoassay following chromatographic purification of the urine and faeces extracts [17].
• In bovine satellite cell cultures 13% of the mononucleated cells were desmin-positive, while 84% of the mononucleated cells in rat satellite cell cultures were desmin-positive [11].
• One of the Mabs, 39AB6, revealed desmin only in cow Purkinje fibers and did not react with desmins from other muscle cells, including ventricular cardiac muscle, striated muscle and smooth muscle, as revealed by both immunoblotting and immunocytochemistry [18].
• Affinity chromatography data indicate that desmin-binding sites are located in the N-terminal 22 kDa fragment of calponin [19].
• Western blot analysis of the diseased muscles revealed a significant increase in the amount of desmin and vimentin immunoreactivities and similar amounts of actin and alpha-actinin compared with the control muscles [1].

References