Treatment of congenital muscular dystrophies

Details Treatment of congenital muscular dystrophies Treatment of congenital muscular dystrophies

2006-07-18

2006-07-18

Landsman, Robert S. (Department: 1647)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C514S04400A

Reexamination Certificate

active

07078379

ABSTRACT:
The invention provides a method of treating congenital muscular dystrophy due to a mutation in the LAMA2 gene in a mammal. The method comprises administering to the mammal a therapeutically effective amount of a protein comprising at least one binding domain for a laminin, at least one binding domain for α-dystroglycan, and at least one follastatin-like domain.

REFERENCES:
Burgess et al,; “Alternatively Spliced Isoforms of Nerve- and Muscle-derived Agrin: Their Roles at the Neuromuscular Junction,”Neuron, vol. 23, 33-44 (1999).
Campbell; “Three Muscular Dystrophies: Loss of Cytoskeleton-Extracellular Matrix Linkage,”Cell, vol. 80, 675-679 (1995).
Denzer et al.; “Agrin Binds to the Nerve-Muscle Basal Lamina via Laminin,”The Journal of Cell Biology, vol. 137, No. 3, 671-683 (1997).
Denzer et al.; “An Amino-terminal Extension Is Required for the Secretion of Chick Agrin and its Binding to Extracellular Matrix,”The Journal of Cell Biology, vol. 131, No. 6, 1547-1560 (1995).
Denzer et al.; “Electron microscopic structure of agrin and mapping of its binding site in laminin-1,”The EMBO Journal, vol. 17 No. 2, 335-343 (1998).
Fox et al.; “Recombinant Nidogen Consists of Three Globular Domains and Mediates Binding of Laminin to Collagen Type IV,”The EMBO Journal, vol. 10, No. 11, 3137-3146 (1991).
Gesemann et al.; “Agrin Is a High-affinity Binding Protein of Dystroglycan in Non-muscle Tissue,”The Journal of Biological Chemistry, vol. 273, No. 1, 600-605 (1998).
Hohenester et al.; “The Crystal Structure of Laminin G-like Module Reveals the Molecular Basis of α-Dystroglycan Binding to Laminins, Perlecan, and Agrin,”Molecular Cell, vol. 4, 783-792 (1999).
Kohfeldt et al.; “Properties of the Extracellular Calcium Binding Module of the Proteoglycan Testican,”Federation of European Biological Societies, vol. 414, 557-561 (1997).
Mann et al.; “Amino Acid Sequence of Mouse Nidogen, a Multidomain Basement Membrane Protein with Binding Activity for Laminin, Collagen IV and Cells,”the EMBO Journal, vol. 8, No. 1, 65-72 (1989).
Mayer et al,; “Absence of Integrin α7 Causes a Novel Form of Muscular Dystrophy,”Nature Genetics, vol. 17, 318-323 (1997).
Meier et al.; “A Minigene of Neural Agrin Encoding the Laminin-binding and Acetylcholine Receptor-aggregating Domains is Sufficient to induce Postsynaptic Differentation in Muscle Fibres,”European Journal of Neuroscience, vol. 10, 3141-3152 (1998).
Moll et al.; “An Agrin Minigene Rescues Dystrophic Symptoms in a Mouse Model for Congenital Muscular Dystrophy, ”Nature, vol. 413, 302-307 (2001).
Noonan et al.; “Identification of cDNA Clones Encoding Different Domains of the Basement Membrane Heparan Sulfate Proteoglycan,”The Journal of Biological Chemistry, vol. 263, No. 31, 16379-16387 (1988).
Ruegg et al.; “The Agrin Gene Codes for a Family of Basal Lamina Proteins That Differ in Function and Distribution,”Neuron, vol. 8, 691-699, (1992).
Ruegg et al.; “Agrin orchestrates synaptic differentiation at the vertebrate neuromuscular junction,”TINS, vol. 21, No. 1, 22-27 (1998).
Sugita et al,; “A Stoichiometric Complex of Neurexins and Dystroglycan in Brain,”The Journal of Cell Biology, vol. 154, No. 2, 435-445 (2001).
Talks et al,; “Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins,”The EMBO Journal, vol. 18, No. 4, 863-870 (1999).
Talts et al,; “Structual Analysis and Proteolytic Processing of Recombinant G Domain of Mouse Laminin α2 Chain,”Federation of European Biochemical Societies, vol. 426, 71-76 (1998).

Affiliated with

Also associated with

Rating

Treatment of congenital muscular dystrophies does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Treatment of congenital muscular dystrophies, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Treatment of congenital muscular dystrophies will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3525144