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 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

The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells

1994 ◽  
Vol 107 (6) ◽  
pp. 1593-1607 ◽  
Author(s):  
A.J. Sarria ◽  
J.G. Lieber ◽  
S.K. Nordeen ◽  
R.M. Evans
Keyword(s):  
Electron Microscopy ◽  
Intermediate Filament ◽  
Nuclear Morphology ◽  
Intermediate Filament Protein ◽  
Mosaic Pattern ◽  
Expression Plasmid ◽  
Vimentin Expression ◽  
Filament System ◽  
Filament Protein ◽  
Filament Network

Human SW-13 cells express the intermediate filament protein vimentin in a mosaic pattern (Hedberg, K. K. and Chen, L. B. (1986). Exp. Cell Res. 163, 509–517). We have isolated SW-13 clones that do (vim+) or do not (vim-) synthesize vimentin as analyzed using anti-intermediate filament immunofluorescence, electron microscopy and two-dimensional gel analysis of detergent-extracted preparations. Vimentin is the only cytoplasmic intermediate filament protein present in the vim+ cells, and the vim- cells do not contain any detectable cytoplasmic intermediate filament system. The presence or absence of intermediate filaments did not observably affect the distribution of mitochondria, endoplasmic reticulum, microtubules or actin stress fibers when these structures were visualized by fluorescence microscopy. However, electron microscopy and anti-lamin A/C immunofluorescence studies showed that nuclear morphology in vim- cells was frequently characterized by large folds or invaginations, while vim+ cells had a more regular or smooth nuclear shape. When vim- cells were transfected with a mouse vimentin expression plasmid, the synthesis of a mouse vimentin filament network restored the smooth nuclear morphology characteristic of vim+ cells. Conversely, when vim+ cells were transfected with a carboxy-terminally truncated mutant vimentin, expression of the mutant protein disrupted the organization of the endogenous vimentin filaments and resulted in nuclei with a prominently invaginated morphology. These results indicated that in SW-13 cells the vimentin filament system affects the shape of the nucleus.

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 The Expression of Intermediate Filament protein Nestin as Related to Vimentin and Desmin in Regenerating Skeletal Muscle

2001 ◽  
Vol 60 (6) ◽  
pp. 588-597 ◽  
Author(s):  
Samuli Vaittinen ◽  
Riitta Lukka ◽  
Cecilia Sahlgren ◽  
Timo Hurme ◽  
Jussi Rantanen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Intermediate Filament ◽  
Intermediate Filament Protein ◽  
Filament Protein

The distribution of intermediate filament protein (skeletin) in normal and diseased human skeletal muscle

1980 ◽  
Vol 47 (2) ◽  
pp. 153-170 ◽  
Author(s):  
Lars-Eric Thornell ◽  
Lars Edström ◽  
Anders Eriksson ◽  
Karl-Gösta Henriksson ◽  
Karl-Axel Ängqvist
Keyword(s):  
Skeletal Muscle ◽  
Intermediate Filament ◽  
Human Skeletal Muscle ◽  
Intermediate Filament Protein ◽  
Filament Protein

The intermediate filament protein desmin in cardiac and skeletal muscle from normal and dystrophic (BIO 14.6) hamsters

1985 ◽  
Vol 63 (6) ◽  
pp. 430-438 ◽  
Author(s):  
Michael Pollock ◽  
Burr G. Atkinson
Keyword(s):  
Skeletal Muscle ◽  
Cardiac Muscle ◽  
Electrophoretic Mobility ◽  
Isoelectric Point ◽  
Intermediate Filament ◽  
Relative Mass ◽  
Intermediate Filament Protein ◽  
Electrophoretic Separation ◽  
Immunofluorescence Analysis ◽  
Filament Protein

Electrophoretic separation on polyacrylamide gels of polypeptides extracted from skeletal and cardiac muscle of BIO 14.6 dystrophic, carrier, and random-bred normal hamsters demonstrates similar quantities and electrophoretic mobility of a protein having a relative mass of 52 000 daltons (apparent isoelectric point 6.2) from all sources examined; we have tentatively identified this protein as the intermediate filament protein desmin. Reaction of such separated polypeptides transferred to nitrocellulose blots with antibodies raised against this protein fails to show immunological differences in this 52 000 dalton protein in cardiac and skeletal muscle from normal and dystrophic animals. Indirect immunofluorescence analysis of skeletal myofibrils from 30- to 60-day normal and dystrophic animals shows no differences in Z-line staining when immunoglobulins from anti-α-actinin serum are used as primary antibodies. Immunoglobulins from the putative anti-desmin serum also produce Z-line staining of skeletal myofibrils from normal animals, but fail to bind to the Z-lines of some skeletal myofibrils from dystrophic hamsters.

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.

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