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Antibodies to myostatin

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Title: Antibodies to myostatin.
Abstract: The present invention relates to antibodies including human antibodies and antigen-binding portions thereof that bind to myostatin, and that function to inhibit myostatin. The invention also relates to human anti-myostatin antibodies and antigen-binding portions thereof. The invention also relates to antibodies that are chimeric, bispecific, derivatized, single chain antibodies or portions of fusion proteins. The invention also relates to isolated heavy and light chain immunoglobulins derived from human anti-myostatin antibodies and nucleic acid molecules encoding such immunoglobulins. The present invention also relates to methods of making human anti-myostatin antibodies, compositions comprising these antibodies and methods of using the antibodies and compositions for diagnosis and treatment. The invention also provides gene therapy methods using nucleic acid molecules encoding the heavy and/or light immunoglobulin molecules that comprise the human anti-myostatin antibodies. The invention also relates to transgenic animals or plants comprising nucleic acid molecules of the present invention. ...


USPTO Applicaton #: #20110091455 - Class: 4241331 (USPTO) - 04/21/11 - Class 424 
Drug, Bio-affecting And Body Treating Compositions > Immunoglobulin, Antiserum, Antibody, Or Antibody Fragment, Except Conjugate Or Complex Of The Same With Nonimmunoglobulin Material >Structurally-modified Antibody, Immunoglobulin, Or Fragment Thereof (e.g., Chimeric, Humanized, Cdr-grafted, Mutated, Etc.)

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The Patent Description & Claims data below is from USPTO Patent Application 20110091455, Antibodies to myostatin.

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REFERENCE TO RELATED APPLICATIONS

This application is a divisional of U.S. application Ser. No. 11/410,886 filed Apr. 24, 2006, which claims the benefit of the filing date of U.S. Provisional application No. 60/674,933, filed Apr. 25, 2005. The above-referenced applications are herein incorporated by reference in their entirety.

BACKGROUND OF THE INVENTION

A growing body of evidence indicates that myostatin (mstn, Growth and Differentiation Factor-8, or GDF-8) negatively regulates skeletal muscle growth. For example, a myostatin null mutation in a child has been associated with dramatic muscle hypertrophy without any obvious abnormalities (Schuelke et al. (2004) Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child. New Engl. J. Med. 350:2682-8). A negative correlation between muscle myostatin protein levels and skeletal muscle mass has also been demonstrated (Schulte, J. N. and Yarasheski, K. E. (2001). Effects of resistance training on the rate of muscle protein synthesis in frail elderly people. Int. J. Sport Nutr. Exerc. Metab. 11 Suppl:S111-820; Walker K S et al. (2004) Resistance training alters plasma myostatin but not IGF-1 in healthy men. Med Sci Sports Exerc. 36(5):787-93.). For example, there is an increased expression of muscle myostatin levels with age and increased myostatin expression has also been shown to contribute to muscle wasting in HIV-infected patients (Gonzalez-cadavid et al. (1998) Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. PNAS 95:14938-4321). In addition, elevated myostatin levels are found in elderly populations. (Yarasheski K E et al., (2002) Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting. J. Nutr. Health Aging. 6(5):343-8). Myostatin also influences bone mass as myostatin-deficient mice have increased bone mineral density (Hamrick et al., (2003) Bone Architecture and Disc Degeneration in the Lumbar Spine of Mice Lacking GDF-8 (Myostatin). J. Orthopaedic Res. 21: 1025-1032 (and references therein).

Antibodies to circulating myostatin have been shown to cause increased muscle mass and improved glucose homeostasis in murine models of type 2 diabetes mellitus. Inhibition of myostatin by ip injection of a neutralizing antibody increases skeletal muscle mass, lowers fasting blood glucose and improves glucose sensitivity in obese diabetic mice (Li X. et al. (2002) Inhibition of myostatin increases muscle mass and improves glucose sensitivity in obese, diabetic mice. Poster #224, in Keystone Symposia: Diabetes Mellitus: Molecular Mechanisms, Genetics and New Therapies). In addition, Ay/a mice are known to develop insulin resistance and are used as a model for type 2 diabetes. When Ay/a mice are made devoid of myostatin by deletion of the myostatin locus, they have normal fed glucose and insulin levels, and dramatically lower glucose levels following an exogenous glucose load relative to normal Ay/amice (McPherron et al. (2002) J. Clin. Invest. 109:595-601).

Considering the detrimental muscle, bone and metabolic defects associated with myostatin, there is an urgent need for antibodies as therapeutics that are specific for myostatin and which prevent or treat conditions by reducing myostatin activity, as well as antibodies as diagnostics to identify individuals that are in need of treatment to reduce myostatin activity.

SUMMARY

OF THE INVENTION

The invention provides anti-myostatin antibodies, nucleic acids encoding them, vectors and host cells for producing the antibodies, compositions and kits comprising the antibodies and methods of making and using the antibodies. Various embodiments of the invention described in the following numbered paragraphs include, but are not limited to those. 1. A human, chimeric or humanized monoclonal antibody or an antigen-binding portion thereof that specifically binds to myostatin. 2. The monoclonal antibody or antigen-binding portion according to paragraph 1 wherein the myostatin is human myostatin. 3. A monoclonal antibody or antigen-binding portion according to paragraph 1, wherein said antibody or portion selectively binds myostatin over GDF11 by at least 50-fold. 4. A monoclonal antibody or antigen-binding portion according to paragraph 3, wherein said antibody or portion inhibits myostatin binding to an activin type I or type II receptor. 5. A monoclonal antibody or antigen-binding portion according to paragraph 1, wherein the antibody or portion thereof has at least one property selected from the group consisting of: (a) competes for binding to myostatin with an antibody selected from the group consisting of 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V; (b) binds to the same epitope of myostatin as an antibody selected from the group consisting of 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V; (c) binds to myostatin with substantially the same KD as an antibody selected from the group consisting of 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—1; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V; and (d) binds to myostatin with substantially the same off rate as an antibody selected from the group consisting of 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—1; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V. 6. A monoclonal antibody or antigen-binding portion thereof comprising: (a) a CDR set, CDR1, CDR2, and CDR3, that sequentially together are at least 90% identical in amino acid sequence to heavy chain CDRs, CDR1, CDR2, and CDR3, sequentially together, that are included in the amino acid sequence set forth in any one of SEQ ID NOs: 45, 49, 53, 57, 61, 65, 69, 73, 77, 81, 85 and 118; (b) a CDR set, CDR1, CDR2, and CDR3, that sequentially together are at least 90% identical in amino acid sequence to light chain CDRs, CDR1, CDR2, and CDR3, sequentially together, that are included in the amino acid sequence set forth in any one of SEQ ID NOs: 47, 51, 55, 59, 63, 67, 71, 75, 83, 87 and 120; or (c) a first CDR set of (a) and a second CDR set of (b). 7. A monoclonal antibody or antigen-binding portion thereof according to paragraph 1, wherein said antibody comprises heavy chain CDRs CDR1, CDR2, and CDR3, that sequentially together are at least 90% identical in amino acid sequence to heavy chain CDRs, CDR1, CDR2, and CDR3, sequentially together, that are included in the amino acid sequence set forth in any one of SEQ ID NOs: 45, 49, 53, 57, 61, 65, 69, 73, 77, 81, 85 and 118. 8. A monoclonal antibody or antigen-binding portion thereof according to paragraph 1, wherein said antibody comprises light chain CDRs CDR1, CDR2, and CDR3, that sequentially together are at least 90% identical in amino acid sequence to light chain CDRs, CDR1, CDR2, and CDR3, sequentially together, that are included in the amino acid sequence set forth in any one of SEQ ID NOs: 47, 51, 55, 59, 63, 67, 71, 75, 83, 87 and 120. 9. A monoclonal antibody or antigen-binding portion according to paragraph 1, wherein said antibody or antigen-binding portion comprises the heavy chain CDR1, CDR2 and CDR3 sequences found in any one of SEQ ID NOs: 45, 49, 53, 57, 61, 65, 69, 73, 77, 81, 85 or 118. 10. A monoclonal antibody or antigen-binding portion according to paragraph 1, wherein said antibody or antigen-binding portion comprises the light chain CDR1, CDR2 and CDR3 sequences found in any one of SEQ ID NOs: 47, 51, 55, 59, 63, 67, 71, 75, 79, 83, 87 or 120. 11. A monoclonal antibody or antigen-binding portion according to paragraph 1, wherein said antibody or portion comprises a heavy chain that utilizes a human VH 1-02 gene, a human VH 3-21 gene or a human VH 3-23 gene. 12. A monoclonal antibody or an antigen-binding portion according to paragraph 1, wherein said antibody or portion comprises a light chain that utilizes a human VK L2 gene, a human VK A3 gene or a human VK A30 gene. 13. A monoclonal antibody according to paragraph 1 comprising a VH domain at least 90% identical in amino acid sequence to the VH domain in any one of SEQ ID NOs: 2, 6, 10, 14, 18, 22, 26, 30, 34, 38, 42 or 115. 14. A monoclonal antibody according to paragraph 1 comprising a VL domain at least 90% identical in amino acid sequence to the VL domain in any one of SEQ ID NOs:4, 8, 12, 16, 20, 24, 28, 32, 36, 40, 44 or 117. 15. A monoclonal antibody or an antigen-binding portion according to paragraph 1 that specifically binds myostatin, wherein: (a) the heavy chain comprises the heavy chain CDR1, CDR2 and CDR3 amino acid sequences of an antibody selected from the group consisting of: 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V; (b) the light chain comprises the light chain CDR1, CDR2 and CDR3 amino acid sequences of an antibody selected from the group consisting of 1—116—1; 1—136—3; 1—257—1; 1—46—1; 2—112—; 1—314—1; 1—66—1; 2—43—1; 2—177—1; 1—132—1; 1—268—1; 2—112_K; 1—116—1L-Q45K; 1—257—1L-L21I; 1—314—1H-T92A; 1—46—1H-L81M; 2—112—1H-I12V; 2—112—1L-F58I; 2—112—1L-I85V; 2—112—1H-L81M, L-F58I; 2—112—1H-L81M, L-I85V; and 2—112—1H-L81M, L-F58I, I85V; or (c) the antibody comprises a heavy chain of (a) and a light chain of (b). 16. A monoclonal antibody according to paragraph 12 further comprising a VL domain at least 90% identical in amino acid sequence to the variable domain in any one of SEQ ID NOs: 4, 8, 12, 16, 20, 24, 28, 32, 36, 40, 44 or 117. 17. A monoclonal antibody selected from the group consisting of: (a) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 2 and SEQ ID NO: 4. (b) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 6 and SEQ ID NO: 8; (c) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 10 and SEQ ID NO: 12; (d) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 14 and SEQ ID NO: 16; (e) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 18 and SEQ ID NO: 20; (f) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 22 and SEQ ID NO: 24; (g) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 26 and SEQ ID NO: 28; (h) an antibody comprising the amino acid sequences set forth in SEQ ID NO: 30 and SEQ ID NO: 32;

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stats Patent Info
Application #
US 20110091455 A1
Publish Date
04/21/2011
Document #
File Date
10/22/2014
USPTO Class
Other USPTO Classes
International Class
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Gene Therapy
Immunoglobulin
Immunoglobulin M
Immunoglobulins


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