Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains

1996 ◽  
Vol 264 (5) ◽  
pp. 933-953 ◽  
Author(s):  
Harald Herrmann ◽  
Markus Häner ◽  
Monika Brettel ◽  
Shirley A. Müller ◽  
Kenneth N. Goldie ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein

scholarly journals Role of synemin, an intermediate filament protein, in adult skeletal muscle (1102.25)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Karla Garcia‐Pelagio ◽  
Joaquin Muriel ◽  
Linda Lund ◽  
Meredith Bond ◽  
Robert Bloch
Keyword(s):  
Skeletal Muscle ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Adult Skeletal Muscle ◽  
Filament Protein

scholarly journals Sarcolemmal Organization in Skeletal Muscle Lacking Desmin: Evidence for Cytokeratins Associated with the Membrane Skeleton at Costameres

2002 ◽  
Vol 13 (7) ◽  
pp. 2347-2359 ◽  
Author(s):  
Andrea O'Neill ◽  
McRae W. Williams ◽  
Wendy G. Resneck ◽  
Derek J. Milner ◽  
Yassemi Capetanaki ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Tibialis Anterior Muscle ◽  
Membrane Skeleton ◽  
Intermediate Filament Protein ◽  
Mouse Muscle ◽  
Intermediate Filament Proteins ◽  
Fast Twitch Muscle ◽  
Filament Protein ◽  
Fast Twitch

The sarcolemma of fast-twitch muscle is organized into “costameres,” structures that are oriented transversely, over the Z and M lines of nearby myofibrils, and longitudinally, to form a rectilinear lattice. Here we examine the role of desmin, the major intermediate filament protein of muscle in organizing costameres. In control mouse muscle, desmin is enriched at the sarcolemmal domains that lie over nearby Z lines and that also contain β-spectrin. In tibialis anterior muscle from mice lacking desmin due to homologous recombination, most costameres are lost. In myofibers from desmin −/− quadriceps, by contrast, most costameric structures are stable. Alternatively, Z line domains may be lost, whereas domains oriented longitudinally or lying over M lines are retained. Experiments with pan-specific antibodies to intermediate filament proteins and to cytokeratins suggest that control and desmin −/− muscles express similar levels of cytokeratins. Cytokeratins concentrate at the sarcolemma at all three domains of costameres when the latter are retained in desmin −/− muscle and redistribute with β-spectrin at the sarcolemma when costameres are lost. Our results suggest that desmin associates with and selectively stabilizes the Z line domains of costameres, but that cytokeratins associate with all three domains of costameres, even in the absence of desmin.

An immunoelectron microscopic examination of the intermediate filament protein, desmin, in exercise-damaged skeletal muscle

1991 ◽  
Vol 49 ◽  
pp. 14-15
Author(s):  
C.M. Waterman-Storer
Keyword(s):  
Skeletal Muscle ◽  
Eccentric Exercise ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Tension Development ◽  
Filament System ◽  
Exercise Muscle ◽  
Exercise Induced ◽  
Filament Protein

Intense exercise has been shown to produce pathological changes in normal skeletal muscle ultrastructure. Eccentric exercise (muscle lengthening during active tension development) in particular has been shown to cause the most severe muscle damage, and studies of both human and animal tissue following eccentric exercise have documented disruption to the contractile apparatus. The disruption originates at the Z-disc, which appears broadened, smeared, or totally disrupted, with Z-discs of adjacent myofibrils out of register and running a “zig-zag” course transversely across the fiber. This condition is known as Z-line streaming. Several researchers have implicated the disruption of the intermediate filament system in the etiology of exercise-induced Z-line streaming, as these filaments are believed to link adjacent myofibrils at the level of the Z-disc. The intermediate filaments are composed predominantly of the proteins desmin and vimentin. This study utilized immunoelectron microscopic localization of desmin in order to elucidate the role of the intermediate filament system in Zline streaming of eccentrically-exercised skeletal muscle.

scholarly journals The role of gigaxonin in the degradation of the glial-specific intermediate filament protein GFAP

2016 ◽  
Vol 27 (25) ◽  
pp. 3980-3990 ◽  
Author(s):  
Ni-Hsuan Lin ◽  
Yu-Shan Huang ◽  
Puneet Opal ◽  
Robert D. Goldman ◽  
Albee Messing ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Genetic Disorder ◽  
Giant Axon ◽  
Alexander Disease ◽  
Intermediate Filament Protein ◽  
Gene Encoding ◽  
Recessive Mutations ◽  
Proteasome Pathway ◽  
Filament Protein

Alexander disease (AxD) is a primary genetic disorder of astrocytes caused by dominant mutations in the gene encoding the intermediate filament (IF) protein GFAP. This disease is characterized by excessive accumulation of GFAP, known as Rosenthal fibers, within astrocytes. Abnormal GFAP aggregation also occurs in giant axon neuropathy (GAN), which is caused by recessive mutations in the gene encoding gigaxonin. Given that one of the functions of gigaxonin is to facilitate proteasomal degradation of several IF proteins, we sought to determine whether gigaxonin is involved in the degradation of GFAP. Using a lentiviral transduction system, we demonstrated that gigaxonin levels influence the degradation of GFAP in primary astrocytes and in cell lines that express this IF protein. Gigaxonin was similarly involved in the degradation of some but not all AxD-associated GFAP mutants. In addition, gigaxonin directly bound to GFAP, and inhibition of proteasome reversed the clearance of GFAP in cells achieved by overexpressing gigaxonin. These studies identify gigaxonin as an important factor that targets GFAP for degradation through the proteasome pathway. Our findings provide a critical foundation for future studies aimed at reducing or reversing pathological accumulation of GFAP as a potential therapeutic strategy for AxD and related diseases.

Maintenance of the intestinal tube in Caenorhabditis elegans: the role of the intermediate filament protein IFC-2

2008 ◽  
Vol 76 (8) ◽  
pp. 881-s3 ◽  
Author(s):  
Katrin Hüsken ◽  
Tobias Wiesenfahrt ◽  
Christian Abraham ◽  
Reinhard Windoffer ◽  
Olaf Bossinger ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Intestinal Tube ◽  
Filament Protein
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