Merosin (laminin-2) localization in basal lamina of normal skeletal muscle fibers and changes in plasma membrane of merosin-deficient skeletal muscle fibers

2003 ◽  
Vol 36 (4) ◽  
pp. 213-220 ◽  
Author(s):  
Seiji Shibuya ◽  
Yoshihiro Wakayama ◽  
Masahiko Inoue ◽  
Hiroko Kojima ◽  
Hiroaki Oniki
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Basal Lamina ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers

scholarly journals Immunohistochemical localization in normal tissues of different epitopes in the multidrug transport protein P170: evidence for localization in brain capillaries and crossreactivity of one antibody with a muscle protein.

1989 ◽  
Vol 37 (2) ◽  
pp. 159-164 ◽  
Author(s):  
F Thiebaut ◽  
T Tsuruo ◽  
H Hamada ◽  
M M Gottesman ◽  
I Pastan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Cardiac Muscle ◽  
Muscle Fibers ◽  
Transport Protein ◽  
Rat Tissues ◽  
Human Tissues ◽  
Normal Tissues ◽  
Skeletal Muscle Fibers ◽  
Muscle Myosin

Using peroxidase immunohistochemistry, we examined the distribution of P170, a multidrug transport protein, in normal tissues by use of two different monoclonal antibodies (MAb). MAb MRK16 is a MAb that has been shown to react with an epitope in P170 located on the external face of the plasma membrane of multidrug-resistant human cells. MAb C219 has been shown to react with P170 in many mammalian species, and detects an epitope located on the cytoplasmic face of the plasma membrane. Using MRK16, we have previously described the localization of P170 on the bile canalicular face of hepatocytes, the apical surface of proximal tubular cells in kidney, and the surface epithelium in the lower GI tract in normal human tissues. In this work, we report that MRK16 also detects P170 in the capillaries of some human brain samples. A similar pattern was found using MAb C219 in rat tissues. in addition, MAb C219 showed intense localization in selected skeletal muscle fibers and all cardiac muscle fibers in rat and human tissues. ATPase cytochemistry showed that these reactive skeletal muscle fibers were of the type I (slow-twitch) class. Other additional sites of C219 reactivity in rat tissues were found in pancreatic acini, seminal vesicle, and testis. Electrophoretic gel immunoblotting showed two protein bands reactive with MAb C219. In liver, MAb C219 reacted with a approximately 170 KD band. In skeletal and cardiac muscle, MAb C219 reacted with a approximately 200 KD band which migrated in the same position as myosin. This band also reacted with an antibody to skeletal muscle myosin. This result suggests that C219 may crossreact with the heavy chain of muscle myosin in cardiac and skeletal muscle. Because MAb C219 reacts with proteins other than P170, it should be used with caution in studies of multidrug resistance.

Immunogold and freeze etch electron microscopic studies of merosin localization in basal lamina of human skeletal muscle fibers

1997 ◽  
Vol 93 (1) ◽  
pp. 34-42 ◽  
Author(s):  
Y. Wakayama ◽  
Makoto Murahashi ◽  
Takahiro Jimi ◽  
Hiroko Kojima ◽  
Seiji Shibuya ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Basal Lamina ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Electron Microscopic ◽  
Skeletal Muscle Fibers ◽  
Microscopic Studies

Dystrophin is localized to the plasma membrane of human skeletal muscle fibers by electron-microscopic cytochemical study

1990 ◽  
Vol 13 (5) ◽  
pp. 376-380 ◽  
Author(s):  
Stirling Carpenter ◽  
George Karpati ◽  
Elizabeth Zubrzycka-Gaarn ◽  
Dennis E. Bulman ◽  
Peter N. Ray ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Human Skeletal Muscle ◽  
Muscle Fibers ◽  
Electron Microscopic ◽  
Cytochemical Study ◽  
Skeletal Muscle Fibers

scholarly journals Aggregates of acetylcholine receptors are associated with plaques of a basal lamina heparan sulfate proteoglycan on the surface of skeletal muscle fibers.

1983 ◽  
Vol 97 (5) ◽  
pp. 1396-1411 ◽  
Author(s):  
M J Anderson ◽  
D M Fambrough
Keyword(s):  
Skeletal Muscle ◽  
Neuromuscular Junction ◽  
Heparan Sulfate ◽  
Basal Lamina ◽  
Acetylcholine Receptors ◽  
Muscle Fibers ◽  
Muscle Cells ◽  
Heparan Sulfate Proteoglycan ◽  
Sulfate Proteoglycan ◽  
Skeletal Muscle Fibers

Hybridoma techniques have been used to generate monoclonal antibodies to an antigen concentrated in the basal lamina at the Xenopus laevis neuromuscular junction. The antibodies selectively precipitate a high molecular weight heparan sulfate proteoglycan from conditioned medium of muscle cultures grown in the presence of [35S]methionine or [35S]sulfate. Electron microscope autoradiography of adult X. laevis muscle fibers exposed to 125I-labeled antibody confirms that the antigen is localized within the basal lamina of skeletal muscle fibers and is concentrated at least fivefold within the specialized basal lamina at the neuromuscular junction. Fluorescence immunocytochemical experiments suggest that a similar proteoglycan is also present in other basement membranes, including those associated with blood vessels, myelinated axons, nerve sheath, and notochord. During development in culture, the surface of embryonic muscle cells displays a conspicuously non-uniform distribution of this basal lamina proteoglycan, consisting of large areas with a low antigen site-density and a variety of discrete plaques and fibrils. Clusters of acetylcholine receptors that form on muscle cells cultured without nerve are invariably associated with adjacent, congruent plaques containing basal lamina proteoglycan. This is also true for clusters of junctional receptors formed during synaptogenesis in vitro. This correlation indicates that the spatial organization of receptor and proteoglycan is coordinately regulated, and suggests that interactions between these two species may contribute to the localization of acetylcholine receptors at the neuromuscular junction.

Carbonic anhydrases IV and IX: subcellular localization and functional role in mouse skeletal muscle

2008 ◽  
Vol 294 (2) ◽  
pp. C402-C412 ◽  
Author(s):  
Renate J. Scheibe ◽  
Karsten Mundhenk ◽  
Tilman Becker ◽  
Janine Hallerdei ◽  
Abdul Waheed ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Subcellular Localization ◽  
Laser Scanning ◽  
Muscle Fibers ◽  
Laser Scanning Microscopy ◽  
Confocal Laser ◽  
Mouse Skeletal Muscle ◽  
Ca Ix ◽  
Skeletal Muscle Fibers

The subcellular localization of carbonic anhydrase (CA) IV and CA IX in mouse skeletal muscle fibers has been studied immunohistochemically by confocal laser scanning microscopy. CA IV has been found to be located on the plasma membrane as well as on the sarcoplasmic reticulum (SR) membrane. CA IX is not localized in the plasma membrane but in the region of the t-tubular (TT)/terminal SR membrane. CA IV contributes 20% and CA IX 60% to the total CA activity of SR membrane vesicles isolated from mouse skeletal muscles. Our aim was to examine whether SR CA IV and TT/SR CA IX affect muscle contraction. Isolated fiber bundles of fast-twitch extensor digitorum longus and slow-twitch soleus muscle from mouse were investigated for isometric twitch and tetanic contractions and by a fatigue test. The muscle functions of CA IV knockout (KO) fibers and of CA IX KO fibers do not differ from the function of wild-type (WT) fibers. Muscle function of CA IV/XIV double KO mice unexpectedly shows a decrease in rise and relaxation time and in force of single twitches. In contrast, the CA inhibitor dorzolamide, whether applied to WT or to double KO muscle fibers, leads to a significant increase in rise time and force of twitches. It is concluded that the function of mouse skeletal muscle fibers expressing three membrane-associated CAs, IV, IX, and XIV, is not affected by the lack of one isoform but is possibly affected by the lack of all three CAs, as indicated by the inhibition studies.

scholarly journals BASAL LAMINA: THE SCAFFOLD FOR ORDERLY CELL REPLACEMENT

1972 ◽  
Vol 55 (2) ◽  
pp. 406-419 ◽  
Author(s):  
Rudolf Vracko ◽  
Earl P. Benditt
Keyword(s):  
Skeletal Muscle ◽  
Basal Lamina ◽  
Plasma Membranes ◽  
Muscle Fibers ◽  
Spatial Relationship ◽  
Supporting Surface ◽  
Skeletal Muscle Fibers ◽  
Type Of Injury ◽  
Rabbit Skeletal Muscles

To explore in detail the relationships between basal lamina (BL) and regenerating cells, we have studied the reconstruction of skeletal muscle fibers and their associated capillaries in portions of rat and rabbit skeletal muscles after injury with either freezing, ischemia, or in situ autografting. Each type of injury produces complete necrosis of cells. The BL, however, remains intact in the area of injury and maintains a "map" of the outline of the spatial relationships between muscle fibers and capillaries. Repopulation of the defect with new cells occurs primarily along the old BL. The spatial relationship between cells, as it existed before injury, is thus reestablished. This process appears to be aided by the ability of each category of regenerating cells to grow along the cell-supporting surface of its own BL. The regenerating cells of muscle fibers and capillaries frequently form a new layer of BL. It is of the usual thickness and is deposited primarily along the outer surfaces of plasma membranes in locations in which the new cells are separated from the old BL. Where an old layer of BL is present overlying a newly formed layer, the old layer may be retained or it may be removed. Removal of redundant BL is probably mediated by interstitial cells which embrace the outside surfaces of BL of regenerated skeletal muscle fibers and capillaries.

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