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Costa,M.L.; Escaleira,R.; Cataldo,A.; Oliveira,F.; Mermelstein,C.S.. |
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... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Desmin; Intermediate filaments; Muscle; Myogenesis; Myopathy. |
Ano: 2004 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004001200007 |
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Garbuglia,M.; Verzini,M.; Sorci,G.; Bianchi,R.; Giambanco,I.; Agneletti,A.L.; Donato,R.. |
The Ca2+-modulated, dimeric proteins of the EF-hand (helix-loop-helix) type, S100A1 and S100B, that have been shown to inhibit microtubule (MT) protein assembly and to promote MT disassembly, interact with the type III intermediate filament (IF) subunits, desmin and glial fibrillary acidic protein (GFAP), with a stoichiometry of 2 mol of IF subunit/mol of S100A1 or S100B dimer and an affinity of 0.5-1.0 µM in the presence of a few micromolar concentrations of Ca2+. Binding of S100A1 and S100B results in inhibition of desmin and GFAP assemblies into IFs and stimulation of the disassembly of preformed desmin and GFAP IFs. S100A1 and S100B interact with a stretch of residues in the N-terminal (head) domain of desmin and GFAP, thereby blocking the head-to-tail... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: S100A1; S100B; Intermediate filaments; Calcium; Regulatory effects; Assembly-disassembly. |
Ano: 1999 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1999001000001 |
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