Appeal No. 2004-1259
Application No. 09/832,355
Claims 1, 9, 12 and 17 are illustrative of the claims on appeal and read as
follows:
1. A fusion protein comprising a first non-heparin-binding VEGF-A peptide
portion, or a peptide portion that exhibits at least about 80% homology to a VEGF-A
peptide portion, and a second non-VEGF peptide portion covalently associated with the
first peptide portion, which first and second peptide portions separately promote
angiogenesis or bone growth, and wherein the second peptide portion lacks a collagen
binding domain.
9. The fusion protein of claim 1, wherein the fusion protein is more angiogenic
than a protein consisting essentially of the first peptide portion and/or is more
angiogenic than a protein consisting essentially of the second peptide portion.
12. The fusion protein of claim 9, wherein blood vessels resulting from
administration of the fusion protein to a mammalian host are associated with more
smooth muscle cells, a greater concentration of smooth muscle cells, more endothelial
cells, a greater concentration of endothelial cells, or any combination thereof, than
blood vessels resulting from administration of a protein consisting essentially of the first
peptide portion.
17. The fusion protein of claim 1, wherein the second peptide portion comprises
a peptide which promotes blood vessel wall maturation, blood vessel wall dilatation,
blood vessel remodeling, extracellular matrix degradation, decreases blood vessel
permeability, or any combination thereof.
The references cited by the examiner are:
Gill et al. (Gill) 6,291,667 Sept. 18, 2001
Rockwell et al. (Rockwell) 5,874,542 Feb. 23, 1999
Davis et al. (Davis) WO 00/37642 Jun. 29, 2000
Yoon et al. (Yoon), “Cloning and Cytotoxicity of Fusion Proteins of EGF and
Angiogenin,” Life Sciences, Vol. 64, No.16, pp. 1435-1445 (1999)
References cited by Appellants are:
N. Ferrara, “VEGF: an update on biological and therapeutic aspects,” Curr. Opinion
Biotech., Vol. 11, pp. 617-624 (2000)
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