Desmin heterogeneity in the main electric organ of Electrophorus electricus

Costa, Márcio Henrique Sá Netto; Moura‐Neto, Vivaldo; Chagas, Carlos

doi:10.1016/0300-9084(88)90108-3

Cited by 13 publications

(13 citation statements)

References 23 publications

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“…All peptides migrated at the same positions. Desmin produced a typical digestion pattern under this condition, as we have previously demonstrated (COSTA et al, 1988).…”

Section: Resultssupporting

confidence: 78%

“…The protein band that migrates near the region of egg albumin (42 KDa) could be actin, a prominent protein in this tissue (AYRES SA et al, 1991). A second protein migrating near 55 KDa could correspond to desmin, a major protein present in the electric tissue (COSTA et al, 1986(COSTA et al, , 1988CORDEIRO et al, 1995). SDS-PAGE revealed another protein (100 KDa), alpha-actinin, that has been previously described by us in these membrane fractions (MERMELSTEIN et al, 1988).…”

Section: Resultsmentioning

confidence: 96%

“…Since desmin is an abundant protein in the intermediate filaments of the electric organ of E. electricus, L (COSTA et al, 1986(COSTA et al, , 1988CORDEIRO et al, 1995), we postulated that it might be the main protein in the cytoplasmic filaments of the electrocytes in this eel. Our ultrastructural analysis revealed that intermediate filaments form a transcellular meshwork in the electrocyte, suggesting that this cytoskeletal component could be responsible for the maintenance of the polarity of the cell.…”

Section: Electrophorusmentioning

confidence: 82%

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Desmin and Actin Filaments in Membrane-Cytoskeletal Preparations of the Electric Tissue of Electrophorus electricus, L.

Mermelstein

Benchimol

Taffarel

et al. 1997

Archives of Histology and Cytology

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“…All peptides migrated at the same positions. Desmin produced a typical digestion pattern under this condition, as we have previously demonstrated (COSTA et al, 1988).…”

Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 96%

Section: Electrophorusmentioning

confidence: 82%

See 1 more Smart Citation

Desmin and Actin Filaments in Membrane-Cytoskeletal Preparations of the Electric Tissue of Electrophorus electricus, L.

Mermelstein

Benchimol

Taffarel

et al. 1997

Archives of Histology and Cytology

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“…In people with familial congenital heart disease, there are also 5-6 isoforms (16). We could show that there are five desmin isoforms in the electric organs of the electric eel Electrophorus electricus L. (17). Furthermore, our group showed that each of the three different electric organs of the electric eel has a distinct desmin isoform pattern (18).…”

Section: Biochemical Aspectsmentioning

confidence: 70%

“…Since the IF proteins are cell type specific, they have been used to type the origin of undifferentiated cells in tumors or other cells of unknown origin, like electrocytes (17).…”

Section: Desminopathiesmentioning

confidence: 99%

Desmin: molecular interactions and putative functions of the muscle intermediate filament protein

Costa

Escaleira

Cataldo

et al. 2004

Braz J Med Biol Res

115

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Desmin is the intermediate filament (IF) protein occurring exclusively in muscle and endothelial cells. There are other IF proteins in muscle such as nestin, peripherin, and vimentin, besides the ubiquitous lamins, but they are not unique to muscle. Desmin was purified in 1977, the desmin gene was characterized in 1989, and knock-out animals were generated in 1996. Several isoforms have been described. 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. Desmin is up-regulated in muscle-derived cellular adaptations, including conductive fibers in the heart, electric organs, some myopathies, and experimental treatments with drugs that induce muscle degeneration, like phorbol esters. Many molecules have been reported to associate with desmin, such as other IF proteins (including members of the membrane dystroglycan complex), nebulin, the actin and tubulin binding protein plectin, the molecular motor dynein, the gene regulatory protein MyoD, DNA, the chaperone αB-crystallin, and proteases such as calpain and caspase. Desmin has an important medical role, since it is used as a marker of tumors' origin. More recently, several myopathies have been described, with accumulation of desmin deposits. Yet, after almost 30 years since its identification, the function of desmin is still unclear. Suggested functions include myofibrillogenesis, mechanical support for the muscle, mitochondrial localization, gene expression regulation, and intracellular signaling. This review focuses on the biochemical interactions of desmin, with a discussion of its putative functions.

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Differential expression of proteins in muscle and electric organ, a muscle derivative

Patterson

Zakon²

1996

J. Comp. Neurol.

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The electric organ of electric fish develops from a myogenic lineage. We have used immunohistochemistry and immunoblotting to determine which features of the muscle phenotype are retained and whether any new ones are expressed in mature electrocytes of the electric fish Sternopygus. The muscle-specific intermediate filament desmin was found throughout the electrocytes, and different desmin antibodies detected molecules with different subcellular distributions. Western blots confirm that these antibodies recognize a protein of MW = 53 kD, the molecular weight of desmin. Other muscle proteins were also present within electrocytes: Actin and sarcomeric alpha-actinin were found within the subsynaptic membrane beneath the plasmalemma of the electrocytes, and talin and acetylcholine receptors were detected both at the innervated posterior face and at the non-innervated anterior face. This was confirmed using rhodamine-conjugated alpha-bungarotoxin. Neither myosin heavy chain nor tropomyosin was present in electrocytes. Finally, we detected within electrocytes a type I acidic keratin that forms a filamentous meshwork within each cell. Immunoblots corroborate this result: A keratin-positive doublet of MW = 50 kD and 57 kD was found in both electrocytes and skin. Myosin, actin, talin, tropomyosin, desmin, alpha-actinin, and acetylcholine receptor, but not keratin, were all expressed in fish skeletal muscle fibers. Thus, electrocytes retain some muscle-specific proteins, do not express others, and in addition, express a non-muscle protein.

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Desmin heterogeneity in the main electric organ of Electrophorus electricus

Cited by 13 publications

References 23 publications

Desmin and Actin Filaments in Membrane-Cytoskeletal Preparations of the Electric Tissue of Electrophorus electricus, L.

Desmin and Actin Filaments in Membrane-Cytoskeletal Preparations of the Electric Tissue of Electrophorus electricus, L.

Desmin: molecular interactions and putative functions of the muscle intermediate filament protein

Differential expression of proteins in muscle and electric organ, a muscle derivative

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