Desmin (DES) ELISA Kits

Zebrafish Desmin (DES) Interaktionspartner

1. Desmin intermediate filaments are required for normal active force generation.

2. Desmin distribution during muscle maturation changes from dispersed aggregates to a perinuclear concentration to striated afterwards.

Human Desmin (DES) Interaktionspartner

1. The coexpression of ACTA2 and DES was related to the expression of MMP2, and positively correlated with lymph node metastasis. Activation of pancreatic stellate cells may promote the expression of MMP2 and enhance the invasion and metastasis of pancreatic carcinoma.

2. In cardiac extracts from human ischemic and nonischemic heart failure, desmin preamyloid oligomers (PAOs) accumulate in myocardial cells. A 2-fold increase of both desmin PAOs and desmin cleavage was also observed in dilated (nonischemic) cardiomyopathy compared with nonfailing human hearts. Ser31 phosphorylated desmin is a likely candidate seed for the nucleation process leading to cardiac PAOs deposition.

3. The DES-p.Glu401Asp mutation causes predominant inherited left ventricular arrhythmogenic cardiomyopathy/dysplasia with a high incidence of adverse clinical events in the absence of skeletal myopathy or conduction system disorders.

4. There was no association of any of the rs1058261 genotypes with hypertension at the age of 50. At age of 60, after adjustment for gender and body mass index, subjects with the genotype CC had higher incidence of cerebrovascular events compared with the T allele (1.6%) (p = 0.046). In addition, those with CC genotype had a higher incidence of all combined cardiovascular events compared with subjects with the T allele.

5. A novel mutation (c.679 C>T /p.R227C) in exon 3 of DES was identified and cosegregated with the affected members of a Chinese family with isolated Dilated cardiomyopathy (DCM) phenotypes (left ventricle and left atrial diameters).

6. Desmin, Glial Fibrillary Acidic Protein, Vimentin, and Peripherin are type III intermediate filaments that have roles in health and disease [review]

7. Phenotypic expression of a novel desmin gene mutation: hypertrophic cardiomyopathy followed by systemic myopathy.

8. Using a combination of co-sedimentation centrifugation, viscometric assays and electron microscopy of negatively stained filaments to analyse the in vitro assembly of desmin filaments, this study shows that the binding of CRYAB to desmin is subject to its assembly status, to the subunit organization within filaments formed and to the integrity of the C-terminal tail domain of desmin.

9. Targeted sequencing revealed trigenic mutations: c.700G>A/p.E234K in DES, c.2966G>A/p.R989H in MYPN, and c.5918G>C/p.R1973P in CACNA1C in a family of hypertrophic cardiomyopathy with early repolarization and short QT syndrome.

10. demonstrate that the expression of mutant desmin causes disruption of the extrasarcomeric desmin cytoskeleton and extensive mitochondrial abnormalities regarding subcellular distribution, number and shape

11. Mutation in the Core Structure of Desmin Intermediate Filaments Affects Myoblast Elasticity

12. Data show that the filament elongation of both desmin and keratin K8/K18 proceeds very similar to that of vimentin.

13. Cdk1-induced desmin phosphorylation is required for efficient separation of desmin-IFs and generally detected in muscular mitotic cells in vivo.

14. Desmin, Lamin A/C, MMP9, and histone H4 were upregulated in the placental villi of women experiencing early pregnancy loss.

15. Ile367Phe, Pro419Ser, and Arg415Glu mutations were associated with desminopathy causing cardiomyopathy in 4 families studied.

16. Increasing desmin abnormalities were correlated with diastolic dysfunction progression.

17. expression level of mutant versus wild-type desmin in mouse model as well as in skeletal muscle specimens derived from human R350P desminopathies; findings demonstrate missense-mutant desmin inflicts changes of the subcellular localization and turnover of desmin itself and of direct desmin-binding partners

18. Results propose that the mutations affect desmin structure and cause its aberrant folding and subsequent aggregation, triggering disruption of myofibrils organization.

19. identified disruption of the desmin system in gastrocnemius myofibers as an index of the myopathy and limitation of muscle function in patients with peripheral artery disease.

20. The desmin intermediate filament network plays a major role in striated muscle development and maintenance by integrating and coordinating most cellular components necessary for proper mechanochemical signaling, organelle cross-talk, energy production and trafficking processes required for proper tissue homeostasis. [Review]

Mouse (Murine) Desmin (DES) Interaktionspartner

1. phosphorylation of desmin filaments by GSK3-beta is a key molecular event required for calpain-1-mediated depolymerization, and the subsequent myofibril destruction.

2. In experimental pressure-overload-induced heart failure, toxic cardiac preamyloid oligomers (PAOs) in the myocardium of mice subjected to transverse aortic constriction comigrate with the cytoskeletal protein desmin. There was a 5-fold increase in desmin. Wild-type desmin generates PAOs in cryAB (alpha-B-crystallin) mice.

3. Data suggest that mutated desmin markedly impedes myocyte structure and function at pre-symptomatic stages of myofibrillar myopathies.

4. Moderate MnSOD and/or catalase overexpression in desmin-null hearts leads to a marked decrease in intracellular reactive oxygen species, ameliorates mitochondrial and other ultrastructural defects, minimizes myocardial degeneration and leads to a significant improvement of cardiac function.

5. R349P mutant desmin-related remodeling of the 3D myofibrillar architecture during aging, which provides a structural basis for the progressive muscle weakness.

6. demonstrate that the expression of mutant desmin causes disruption of the extrasarcomeric desmin cytoskeleton and extensive mitochondrial abnormalities regarding subcellular distribution, number and shape

7. The disease-mutant desmin variants E245D and T453I exhibited increased binding affinity for nebulette, delayed filament assembly kinetics, and caused significant weakening of networks.

8. desmin and alphaBeta-crystallin are localized at sarcoplasmic reticulum (SR)-mitochondria-associated membranes (MAMs), where they interact with VDAC, Mic60 - the core component of mitochondrial contact site and cristae organizing system (MICOS) complex - and ATP synthase, suggesting that these associations could be crucial in mitoprotection at different levels.

9. Complete lack or markedly decreased expression of mutant R349P desmin impairs the structural and functional integrity of neuromuscular endplates.

10. Cdk1-induced desmin phosphorylation is required for efficient separation of desmin-IFs and generally detected in muscular mitotic cells in vivo.

11. the coordinated up-regulations of desmin and alpha- actinin specifically in the early stage of diastolic heart failure mouse models indicate a novel myocardial response.

12. E413K mutation induces desmin network disorganization, desmin aggregate formation and alters the traction forces generation of single myoblasts.

13. This study identifies desmin as a new Asb2b target for proteasomal degradation in cardiomyocytes and suggests that accumulation of desmin could contribute to UPS impairment in Hypertrophic cardiomyopathy mice and patients

14. found that inhibition of the Rac1 pathway (a G protein signaling pathway involved in diverse cellular processes), antioxidant treatment, and stimulation of macroautophagy reduced desmin aggregation by up to 75% in this model

15. This demonstration of biomechanical integration by the desmin intermediate filament system suggests that it plays an active biological role in muscle in addition to its accepted structural role

16. expression level of mutant versus wild-type desmin in mouse model as well as in skeletal muscle specimens derived from human R350P desminopathies; findings demonstrate missense-mutant desmin inflicts changes of the subcellular localization and turnover of desmin itself and of direct desmin-binding partners

17. Disruption of both nesprin 1 and desmin results in decreased lifespan, body weight and muscle strength.

18. The desmin intermediate filament network plays a major role in striated muscle development and maintenance by integrating and coordinating most cellular components necessary for proper mechanochemical signaling, organelle cross-talk, energy production and trafficking processes required for proper tissue homeostasis. [Review]

19. Desmin content and transversal stiffness of the left ventricle mouse cardiomyocytes and skeletal muscle fibers after a 30-day space flight on board "BION-M1" biosatellite

20. the observed decline in [Ca(2+)]mit was due to desmin aggregate accumulation resulting in the loss of desmin mitochondria interactions

Cow (Bovine) Desmin (DES) Interaktionspartner

1. Results show that expression of desmin increased during the late fattening stage of of hanwoo steers and it contributes to the muscle contractile apparatus.