▪ Abstract Striated muscle is an intricate, efficient, and precise machine that contains complex interconnected cytoskeletal networks critical for its contractile activity. The individual units of the sarcomere, the basic contractile unit of myofibrils, include the thin, thick, titin, and nebulin filaments. These filament systems have been investigated intensely for some time, but the details of their functions, as well as how they are connected to other cytoskeletal elements, are just beginning to be elucidated. These investigations have advanced significantly in recent years through the identification of novel sarcomeric and sarcomeric-associated proteins and their subsequent functional analyses in model systems. Mutations in these cytoskeletal components account for a large percentage of human myopathies, and thus insight into the normal functions of these proteins has provided a much needed mechanistic understanding of these disorders. In this review, we highlight the components of striated muscle cyt...

Striated muscle cytoarchitecture: an intricate web of form and function.

Intermediate filaments (IFs) are cytoskeletal polymers whose protein constituents are encoded by a large family of differentially expressed genes. Owing in part to their properties and intracellular organization, IFs provide crucial structural support in the cytoplasm and nucleus, the perturbation of which causes cell and tissue fragility and accounts for a large number of genetic diseases in humans. A number of additional roles, nonmechanical in nature, have been recently uncovered for IF proteins. These include the regulation of key signaling pathways that control cell survival, cell growth, and vectorial processes including protein targeting in polarized cellular settings. As this discovery process continues to unfold, a rationale for the large size of this family and the context-dependent regulation of its members is finally emerging.

/pdf/intermediate-filament-scaffolds-fulfill-mechanical-4gjg8dxgu8.pdf

Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm

The corneal fibrosis response to epithelial–stromal injury

Patients with peripheral artery disease (PAD) develop a myopathy in their ischemic lower extremities, which is characterized by myofiber degeneration, mitochondrial dysfunction and impaired limb function. Desmin, a protein of the cytoskeleton, is central to maintenance of the structure, shape and function of the myofiber and its organelles, especially the mitochondria, and to translation of sarcomere contraction into muscle contraction. In this study, we investigated the hypothesis that disruption of the desmin network occurs in gastrocnemius myofibers of PAD patients and correlates with altered myofiber morphology, mitochondrial dysfunction, and impaired limb function. Using fluorescence microscopy, we evaluated desmin organization and quantified myofiber content in the gastrocnemius of PAD and control patients. Desmin was highly disorganized in PAD but not control muscles and myofiber content was increased significantly in PAD compared to control muscles. By qPCR, we found that desmin gene transcripts were increased in the gastrocnemius of PAD patients as compared with control patients. Increased desmin and desmin gene transcripts in PAD muscles correlated with altered myofiber morphology, decreased mitochondrial respiration, reduced calf muscle strength and decreased walking performance. In conclusion, our studies identified disruption of the desmin system in gastrocnemius myofibers as an index of the myopathy and limitation of muscle function in patients with PAD.

https://journals.sagepub.com/doi/pdf/10.1369/0022155415569348

Abnormal accumulation of desmin in gastrocnemius myofibers of patients with peripheral artery disease: associations with altered myofiber morphology and density, mitochondrial dysfunction and impaired limb function.

Immunohistochemistry of soft tissue tumors: progress and prospects.

With electron microscopy, a morphological class of filaments with an average diameter of 100 A has been identified in many vertebrate cells These filaments were initially referred to as intermediate filaments since their diameter is intermediate to those of the 60 A actin filaments and the 250 A microtubules in nonmuscle cells and intermediate to those of the 60 A actin filaments and the 150 A myosin filaments in muscle cells Presently, intermediate filaments are commonly referred to as neurofilaments in neurons, glial filaments in glial cells, 10 nm filaments in fibroblastic cells, tonofilaments or keratin filaments in epiderimal and epithelial cells, and intermediate filaments in skeletal, cardiac, and smooth muscle cells Due to their wide distribution and morphological similarity, it was originally believed that the major subunit of the intermediate filaments from these various sources would be highly conserved in its amino acid sequence as is the case with actin and tubulin The recent isolation of intermediate filaments from a variety of avian or mammalian cell types has enabled investigators to characterize the subunit proteins of these different filament preparations and to determine the extent of their homology By a number of criteria including peptide mapping, antibody cross-reactivity, isoelectric point and molecular weight, it was shown that the major protein subunit of the intermediate filaments from muscle cells (desmin), fibroblasts, glial cells, neurons, and epidermal and epithelial cells (keratins) was distinct (Benitz et al 1976; Dahl and Bignami 1976; Davison et al 1977; Schachner et al 1977; Schlaepfer 1977; Franke et al 1978; Lazarides 1978; Lazarides and Balzer 1978; Milstone and McGuire 1978; Schlaepfer and Freeman 1978; Starger et al 1978; Sun and Green 1978)

Desmin and intermediate filaments in muscle cells.

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Desmin and intermediate filaments in muscle cells.