Small size of orthogonal array in muscle plasma membrane of Fukuyama type congenital muscular dystrophy

1986 ◽  
Vol 72 (2) ◽  
pp. 130-133 ◽  
Author(s):  
Y. Wakayama ◽  
T. Kumagai ◽  
T. Jimi
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Orthogonal Array ◽  
Congenital Muscular Dystrophy ◽  
Muscle Plasma Membrane

Freeze–fracture analysis of muscle plasma membrane in Becker's muscular dystrophy

1994 ◽  
Vol 20 (5) ◽  
pp. 487-494 ◽  
Author(s):  
S. Shibuya ◽  
Y. Wakayama ◽  
T. Jimi ◽  
H. Oniki ◽  
T. Kobayashi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Freeze Fracture ◽  
Fracture Analysis ◽  
Muscle Plasma Membrane

Freeze fracture studies of muscle plasma membrane in human muscular dystrophy

1981 ◽  
Vol 54 (3) ◽  
pp. 189-197 ◽  
Author(s):  
D. L. Schotland ◽  
E. Bonilla ◽  
Y. Wakayama
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Freeze Fracture ◽  
Muscle Plasma Membrane

Freeze-fracture study of muscle plasma membrane in obligate carriers of Duchenne muscular dystrophy

Neurology ◽  
1983 ◽  
Vol 33 (10) ◽  
pp. 1346-1346 ◽  
Author(s):  
E. Bonilla ◽  
K. H. Fischbeck ◽  
D. L. Schotland
Keyword(s):  
Plasma Membrane ◽  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Freeze Fracture ◽  
Muscle Plasma Membrane ◽  
Fracture Study

scholarly journals Immunohistochemical alterations of dystrophin in congenital muscular dystrophy

1995 ◽  
Vol 53 (3a) ◽  
pp. 416-423 ◽  
Author(s):  
Lineu Cesar Werneck ◽  
Eduardo Bonilla
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Muscle Biopsy ◽  
Polyclonal Antibody ◽  
Autosomal Recessive ◽  
Congenital Muscular Dystrophy ◽  
Becker Muscular Dystrophy ◽  
Muscle Membrane ◽  
Total Absence ◽  
Dystrophin Expression

The dystrophin distribution in the plasma muscle membrane using immunohystochemistry was studied in 22 children with congenital muscular dystrophy. The dystrophin was detected by immunofluorescence in muscle biopsy through a polyclonal antibody. All the cases had patchy interruptions of the fluorescence in the plasma membrane. A large patchy interruption of the sarcolemma was found in 17 cases, small interruption in 12, and a combination of large and small patchy discontinuity in 7. Small gaps around the fiber like a rosary were found in 15 cases. The frequency of these abnormalities ranged cases from: all fibers in 5 cases, frequent in 8, occasional in 5, and rare in 4. Five cases had total absence of immunofluorescence. These results suggest that the dystrophin expression is abnormal in this group of children and that this type of abnormalities can not be differentiated from early Becker muscular dystrophy nor childhood autosomal recessive muscular dystrophy through immunohystochemistry alone.

The erythrocyte plasma membrane in murine muscular dystrophy: a scanning electron microscopic and freeze fracture study

1979 ◽  
Vol 57 (5) ◽  
pp. 983-986 ◽  
Author(s):  
Burr G. Atkinson ◽  
Richard R. Shivers ◽  
Bruce Nixon ◽  
Kristine H. Atkinson
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Plasma Membranes ◽  
Genetic Disorder ◽  
Freeze Fracture ◽  
Congenital Muscular Dystrophy ◽  
Molecular Architecture ◽  
Intramembrane Particles

The plasma membrane of red blood cells from mice afflicated with congenital muscular dystrophy exhibits a dramatic depletion of intramembrane particles. Examination of protein particles on fracture faces of erythrocyte plasma membranes from dystrophic mice revealed a 33% decrease in the number of intramembrane particles when compared with similarly prepared erythrocytes from nondystrophic animals. This alteration in the internal molecular architecture of these plasma membranes is correlated with the morphological distortion manifested by most red blood cells from mice inflicted with this genetic disorder.

scholarly journals Reduced Aquaporin 4 Expression in the Muscle Plasma Membrane of Patients With Duchenne Muscular Dystrophy

2002 ◽  
Vol 59 (3) ◽  
pp. 431 ◽  
Author(s):  
Yoshihiro Wakayama ◽  
Takahiro Jimi ◽  
Masahiko Inoue ◽  
Hiroko Kojima ◽  
Makoto Murahashi ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Aquaporin 4 ◽  
Muscle Plasma Membrane

scholarly journals Membrane Targeting and Stabilization of Sarcospan Is Mediated by the Sarcoglycan Subcomplex

1999 ◽  
Vol 145 (1) ◽  
pp. 153-165 ◽  
Author(s):  
Rachelle H. Crosbie ◽  
Connie S. Lebakken ◽  
Kathleen H. Holt ◽  
David P. Venzke ◽  
Volker Straub ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Genetic Mutations ◽  
Myotendinous Junction ◽  
Normal Muscle ◽  
Glycoprotein Complex ◽  
Muscle Plasma Membrane ◽  
Dystrophin Glycoprotein Complex ◽  
And Function ◽  
Dystrophin Glycoprotein

The dystrophin–glycoprotein complex (DGC) is a multisubunit complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. The proteins of the DGC are structurally organized into distinct subcomplexes, and genetic mutations in many individual components are manifested as muscular dystrophy. We recently identified a unique tetraspan-like dystrophin-associated protein, which we have named sarcospan (SPN) for its multiple sarcolemma spanning domains (Crosbie, R.H., J. Heighway, D.P. Venzke, J.C. Lee, and K.P. Campbell. 1997. J. Biol. Chem. 272:31221–31224). To probe molecular associations of SPN within the DGC, we investigated SPN expression in normal muscle as a baseline for comparison to SPN's expression in animal models of muscular dystrophy. We show that, in addition to its sarcolemma localization, SPN is enriched at the myotendinous junction (MTJ) and neuromuscular junction (NMJ), where it is a component of both the dystrophin– and utrophin–glycoprotein complexes. We demonstrate that SPN is preferentially associated with the sarcoglycan (SG) subcomplex, and this interaction is critical for stable localization of SPN to the sarcolemma, NMJ, and MTJ. Our experiments indicate that assembly of the SG subcomplex is a prerequisite for targeting SPN to the sarcolemma. In addition, the SG– SPN subcomplex functions to stabilize α-dystroglycan to the muscle plasma membrane. Taken together, our data provide important information about assembly and function of the SG–SPN subcomplex.

Muscle plasma membrane abnormalities in infants with Duchenne muscular dystrophy

Neurology ◽  
1983 ◽  
Vol 33 (10) ◽  
pp. 1368-1368 ◽  
Author(s):  
Y. Wakayama ◽  
E. Bonilla ◽  
D. L. Schotland
Keyword(s):  
Plasma Membrane ◽  
Duchenne Muscular Dystrophy ◽  
Muscular Dystrophy ◽  
Muscle Plasma Membrane
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