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Pegylated factor vii glycoformsRelated Patent Categories: Drug, Bio-affecting And Body Treating Compositions, Designated Organic Active Ingredient Containing (doai), Peptide Containing (e.g., Protein, Peptones, Fibrinogen, Etc.) Doai, Glycoprotein (carbohydrate Containing)Pegylated factor vii glycoforms description/claimsThe Patent Description & Claims data below is from USPTO Patent Application 20080039373, Pegylated factor vii glycoforms. Brief Patent Description - Full Patent Description - Patent Application Claims
CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application is a continuation of U.S. patent application Ser. No. 10/609,701, filed Jun. 30, 2003, which was a continuation of International Application no. PCT/DK03/00420, filed Jun. 20, 2003, and claims priority under 35 U.S.C. 119 of Danish application no. PA 2002 00964, filed Jun. 21, 2002, and U.S. application No. 60/394,778, filed Jul. 1, 2002, the contents of which are fully incorporated herein by reference. FIELD OF THE INVENTION [0002] The present invention relates to compositions comprising Factor VII conjugates having predetermined patterns of glycosylation. BACKGROUND OF THE INVENTION [0003] Factor VII is a vitamin K-dependent plasma protein synthesized in the liver and secreted into the blood as a single chain glycoprotein with a molecular weight of approximately 50 kDa. The FVII zymogen is converted into an activated form (FVIIa) by proteolytic cleavage. FVIIa in complex with tissue factor (TF) is able to convert both Factor IX and Factor X into their activated forms, followed by reactions leading to rapid thrombin generation and fibrin formation. [0004] The proteins involved in the clotting cascade, including, e.g., Factor VII, Factor VIII, Factor IX, Factor X, and Protein C, are proving to be useful therapeutic agents to treat a variety of pathological conditions. Accordingly, there is an increasing need for formulations comprising these proteins that are pharmaceutically acceptable and exhibit a uniform and predetermined clinical efficacy. [0005] Because of the many disadvantages of using human plasma as a source of pharmaceutical products, it is preferred to produce these proteins in recombinant systems. The clotting proteins, however, are subject to a variety of co- and post-translational modifications, including, e.g., asparagine-linked (N-linked) glycosylation; O-linked glycosylation; and .gamma.-carboxylation of glu residues. These modifications may be qualitatively or quantitatively different when heterologous cells are used as hosts for large-scale production of the proteins. In particular, production in heterologous cells often results in a different array of glycoforms, which are identical polypeptides having different covalently linked oligosaccharide structures. [0006] In different systems, variations in the oligosaccharide structure of therapeutic proteins have been linked to, inter alia, changes in immunogenicity and in vivo clearance. [0007] Besides in vivo clearance also functional in vivo half-life is of importance to the period of time during which the compound is "therapeutically available" in the body. [0008] The circulating half-life of rFVIIa is about 2.3 hours ("Summary Basis for Approval for NovoSeven.COPYRGT.", FDA reference number 96-0597). [0009] Commercial preparations of human recombinant FVIIa are sold as NovoSeven.RTM.. NovoSeven.RTM. is the only rFVIIa for effective and reliable treatment of bleeding episodes available on the market. Relatively high doses and frequent administration are necessary to reach and sustain the desired therapeutic or prophylactic effect. As a consequence adequate dose regulation is difficult to obtain and the need of frequent intravenous administrations imposes restrictions on the patient's way of living. [0010] A molecule with a longer circulation half-life would decrease the number of necessary administrations. Given the association of current FVIIa product with frequent injections, there is a clear need for improved FVII molecules. [0011] One way of improving the circulation is to ensure that the rate of clearance from the body is reduced. As said, variations in the oligosaccharide structure of therapeutic proteins have been linked to, inter alia, in vivo clearance. Furthermore, attachment of a chemical moiety to the polypeptide may confer reduced renal clearance to the polypeptide. [0012] Inactive forms of FVII have been reported. The inactivated form is capable of competing with wild type FVII or FVIIa for binding to tissue factor and inhibiting clotting activity. The inactivated form of FVIIa is suggested to be used for treatment of patients being in hypercoagulable states, such as patients with sepsis, in risk of myocardial infarction or of thrombotic stroke. [0013] WO 98/32466 suggests that FVII, among many other proteins, may be PEGylated but does not contain any further information in this respect. [0014] WO 01/58935 claims conjugates of non-polypeptide moieties (e.g., PEG) with a polypeptide wherein the amino acid sequence differs from that of wild-type FVII in that at least one amino acid residue comprising an attachment group for a non-peptidic moiety has been introduced or removed. [0015] U.S. Pat. No. 4,847,325 suggests that colony stimulating factor-1 (CSF-1) could be attached to PEG by reacting PEG derivatives with oxidized CSF-1. [0016] Thus, there is a need in the art for compositions and methods that provide clotting protein preparations, particularly preparations comprising improved recombinant human Factor VII, modified Factor VII, or Factor VII-related polypeptide. SUMMARY OF THE INVENTION [0017] It has been found by the present investigators that preparations of Factor VII polypeptides having glycoform patterns which contain at least one oligosaccharide group covalently linked to at least one polymeric group exhibit improved functional properties. Accordingly, the present invention relates to methods and compositions that provide these conjugate protein preparations. [0018] Accordingly, the present invention relates in a first aspect to a preparation comprising a plurality of Factor VII polypeptides or Factor VII-related polypeptides, wherein the polypeptides comprise asparagine-linked and/or serine-linked oligosaccharide chains, and wherein at least one oligosaccharide group is covalently attached to at least one polymeric group. [0019] In one embodiment thereof, the polymeric group is covalently attached to a sialic acid moiety. In another embodiment thereof, the polymeric group is covalently attached to a galactose moiety. [0020] In one embodiment thereof, between about 94-100% of the oligosaccharide chains comprise at least one sialic acid moiety. Continue reading about Pegylated factor vii glycoforms... 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