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Science 3 November 1995:
Vol. 270. no. 5237, p. 755
DOI: 10.1126/science.270.5237.755
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Perspectives

Ronald Worton

Defects in the gene for the muscle protein dystrophin cause many cases of muscular dystrophy. Worton discusses three new papers, one in this issue of Science (Noguchi et al., p. 819) and two in the November issue of Nature Genetics, which report that defects in the sarcoglycans, transmembrane glycoproteins that associate with dystrophin, underlie certain other types of muscular dystrophy.

The author is in the Department of Genetics, Research Institute, The Hospital for Sick Children, 555 University Avenue, Toronto M5G 1X8 and the Department of Molecular and Medical Genetics, University of Toronto, Toronto M5S 1A8, Canada. E-mail: rworton@sickkids.on.ca

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Simultaneous Dystrophin and Dysferlin Deficiencies Associated with High-Level Expression of the Coxsackie and Adenovirus Receptor in Transgenic Mice.
C. A. Shaw, N. Larochelle, R. W.R. Dudley, H. Lochmuller, G. Danialou, B. J. Petrof, G. Karpati, P. C. Holland, and J. Nalbantoglu (2006)
Am. J. Pathol. 169, 2148-2160
   Abstract »    Full Text »    PDF »
Regenerative capacity of the dystrophic (mdx) diaphragm after induced injury.
S. Matecki, G. H. Guibinga, and B. J. Petrof (2004)
Am J Physiol Regulatory Integrative Comp Physiol 287, R961-R968
   Abstract »    Full Text »    PDF »
Novel sarcoglycan gene mutations in a large cohort of Italian patients.
C Boito, M Fanin, G Siciliano, C Angelini, and E Pegoraro (2003)
J. Med. Genet. 40, e67-67
   Full Text »    PDF »
Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein.
J. D. Neely, M. Amiry-Moghaddam, O. P. Ottersen, S. C. Froehner, P. Agre, and M. E. Adams (2001)
PNAS 98, 14108-14113
   Abstract »    Full Text »    PDF »
Increased expression of utrophin in a slow vs. a fast muscle involves posttranscriptional events.
A. O. Gramolini, G. Belanger, J. M. Thompson, J. V. Chakkalakal, and B. J. Jasmin (2001)
Am J Physiol Cell Physiol 281, C1300-C1309
   Abstract »    Full Text »    PDF »
Dystrophin-deficient myocardium is vulnerable to pressure overload in vivo.
Y. Kamogawa, S. Biro, M. Maeda, M. Setoguchi, T. Hirakawa, H. Yoshida, and C. Tei (2001)
Cardiovasc Res 50, 509-515
   Abstract »    Full Text »    PDF »
Polycystin: New Aspects of Structure, Function, and Regulation.
P. D. WILSON (2001)
J. Am. Soc. Nephrol. 12, 834-845
   Abstract »    Full Text »    PDF »
Application of Passive Stretch and Its Implications for Muscle Fibers.
P. G De Deyne (2001)
Physical Therapy 81, 819-827
   Abstract »    Full Text »    PDF »
Differential effects of dystrophin and utrophin gene transfer in immunocompetent muscular dystrophy (mdx) mice.
S. EBIHARA, G.-H. GUIBINGA, R. GILBERT, J. NALBANTOGLU, B. MASSIE, G. KARPATI, and B. J. PETROF (2000)
Physiol Genomics 3, 133-144
   Abstract »    Full Text »    PDF »
A cross section of autosomal recessive limb-girdle muscular dystrophies in 38 families.
P. Dinçer, Z. Akçören, E. Demir, I. Richard, O. Sancak, G. Kale, E. Tan, J A. Urtizberea, and J. S Beckmann (2000)
J. Med. Genet. 37, 361-367
   Abstract »    Full Text »
Expression of Agrin, Dystroglycan, and Utrophin in Normal Renal Tissue and in Experimental Glomerulopathies.
C. J. I. Raats, J. van den Born, M. A. H. Bakker, B. Oppers-Walgreen, B. J. M. Pisa, H. B. P. M. Dijkman, K. J. M. Assmann, and J. H. M. Berden (2000)
Am. J. Pathol. 156, 1749-1765
   Abstract »    Full Text »    PDF »
Making sense of the limb-girdle muscular dystrophies.
K. M. D. Bushby (1999)
Brain 122, 1403-1420
   Abstract »    Full Text »    PDF »
alpha -Dystroglycan Is a Laminin Receptor Involved in Extracellular Matrix Assembly on Myotubes and Muscle Cell Viability.
F. Montanaro, M. Lindenbaum, and S. Carbonetto (1999)
J. Cell Biol. 145, 1325-1340
   Abstract »    Full Text »    PDF »
Induction of utrophin gene expression by heregulin in skeletal muscle cells: Role of the N-box motif and GA binding protein.
A. O. Gramolini, L. M. Angus, L. Schaeffer, E. A. Burton, J. M. Tinsley, K. E. Davies, J.-P. Changeux, and B. J. Jasmin (1999)
PNAS 96, 3223-3227
   Abstract »    Full Text »    PDF »
A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-actin through an Electrostatic Interaction.
K. J. Amann, B. A. Renley, and J. M. Ervasti (1998)
J. Biol. Chem. 273, 28419-28423
   Abstract »    Full Text »    PDF »
Molecular Basis of Genetic Heterogeneity: Role of the Clinical Neurologist.
L. P. Rowland (1998)
J Child Neurol 13, 122-132
   Abstract »    PDF »
Agrin Is a High-affinity Binding Protein of Dystroglycan in Non-muscle Tissue.
M. Gesemann, A. Brancaccio, B. Schumacher, and M. A. Ruegg (1998)
J. Biol. Chem. 273, 600-605
   Abstract »    Full Text »    PDF »
Presence of Laminin alpha 5 Chain and Lack of Laminin alpha 1 Chain during Human Muscle Development and in Muscular Dystrophies.
C.-F. Tiger, M.-F. Champliaud, F. Pedrosa-Domellof, L.-E. Thornell, P. Ekblom, and D. Gullberg (1997)
J. Biol. Chem. 272, 28590-28595
   Abstract »    Full Text »    PDF »
Dystrophin-Glycoprotein Complex Is Monomeric and Stabilizes Actin Filaments in Vitro through a Lateral Association.
I. N. Rybakova and J. M. Ervasti (1997)
J. Biol. Chem. 272, 28771-28778
   Abstract »    Full Text »    PDF »
Tissue-specific Heterogeneity in alpha -Dystroglycan Sialoglycosylation. SKELETAL MUSCLE alpha -DYSTROGLYCAN IS A LATENT RECEPTOR FOR VICIA VILLOSA AGGLUTININ B4 MASKED BY SIALIC ACID MODIFICATION.
J. M. Ervasti, A. L. Burwell, and A. L. Geissler (1997)
J. Biol. Chem. 272, 22315-22321
   Abstract »    Full Text »    PDF »
In situ molecular association of dystrophin with actin revealed by sensitized emission immuno-resonance energy transfer.
D. D. Root (1997)
PNAS 94, 5685-5690
   Abstract »    Full Text »    PDF »
Agrin Binds to the Nerve-Muscle Basal Lamina via Laminin.
A. J. Denzer, R. Brandenberger, M. Gesemann, M. Chiquet, and M. A. Ruegg (1997)
J. Cell Biol. 137, 671-683
   Abstract »    Full Text »    PDF »
Laminin-induced Clustering of Dystroglycan on Embryonic Muscle Cells: Comparison with Agrin-induced Clustering.
M. W. Cohen, C. Jacobson, P. D. Yurchenco, G. E. Morris, and S. Carbonetto (1997)
J. Cell Biol. 136, 1047-1058
   Abstract »    Full Text »    PDF »
Mutations in the Sarcoglycan Genes in Patients with Myopathy.
D. J. Duggan, J. R. Gorospe, M. Fanin, E. P. Hoffman, C. Angelini, E. Pegoraro, S. Noguchi, E. Ozawa, W. Pendlebury, A.J. Waclawik, et al. (1997)
N. Engl. J. Med. 336, 618-625
   Abstract »    Full Text »    PDF »
Structure of the Human Laminin alpha 2-Chain Gene (LAMA2), Which Is Affected in Congenital Muscular Dystrophy.
X. Zhang, R. Vuolteenaho, and K. Tryggvason (1996)
J. Biol. Chem. 271, 27664-27669
   Abstract »    Full Text »    PDF »
Expression of Caveolin-3 in Skeletal, Cardiac, and Smooth Muscle Cells. CAVEOLIN-3 IS A COMPONENT OF THE SARCOLEMMA AND CO-FRACTIONATES WITH DYSTROPHIN AND DYSTROPHIN-ASSOCIATED GLYCOPROTEINS.
K. S. Song, P. E. Scherer, Z. Tang, T. Okamoto, S. Li, M. Chafel, C. Chu, D. S. Kohtz, and M. P. Lisanti (1996)
J. Biol. Chem. 271, 15160-15165
   Abstract »    Full Text »    PDF »
Distinct regions in the 3' untranslated region are responsible for targeting and stabilizing utrophin transcripts in skeletal muscle cells.
A. O. Gramolini, G. Belanger, and B. J. Jasmin (2001)
J. Cell Biol. 154, 1173-1184
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)