Appeal No. 2004-1259
Application No. 09/832,355
Appellants argue in response, that the Ang-1 peptide portion of the VEGF-Ang-1
fusion protein disclosed in the Davis '642 PCT application does not separately promote
angiogenesis or bone growth, as required by ....the claims.” Brief, page 9. Appellants
argue that, “[t]he Davis '642 PCT application indicates that Ang-1 'clustering' induces or
enhances its biological activity.” Davis also (Brief, page 10):
discloses that monomeric Ang-1 has low affinity for the Tie-2 receptor as
compared to highly clustered (e.g., tetrameric) VEGF-Ang-1 fusion
proteins.
Therefore, the non-VEGF peptide portion of the fusion protein
disclosed in the '642 PCT application does not separately promote
angiogenesis, bone growth, and/or wound healing, as required by claims 1
and 43, but rather requires multimerization to exert its biological activity.
We do not agree with appellants' characterization of Davis. Davis discloses at
page 9, lines 9-14, that the fusion protein may comprise, as a first subunit, the receptor
binding domain of VEGF and the second subunit may comprise the receptor binding
domain of angiopoietin. “Still further, the first and second subunits may each have one
or more than one copy of the receptor binding domain of their respective ligand.” Id.
Thus Davis appears to describe not only fusion proteins comprising highly clustered
proteins but also single subunits having one copy of the receptor binding domain of
their respective ligand.
Moreover, the examiner indicates (Answer, pages 24-25) that “VEGF and
angiopoietin-1 function together during vascular development, with VEGF acting during
early vessel formation, and angiopoietin-1 acting later during vessel remodeling,
maturation and stabilization.” “Thus, separate from VEGF-1, in the sense that they do
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