Appeal No. 2004-0005 Page 6
Application No. 07/644,361
references are silent as to the increase phosphorylation of the c-erbB-2, this property is
an expected property that follows in ligand-receptor internalization/down modulation
systems.”
Appellants do not argue that the examiner’s references fail to suggest a drug
combination that comprises an anti-neoplastic agent and a molecule that binds to c-
erbB-2 cell protein on tumor cells. Rather, appellants “argue the single point of whether
it would have been expected that such c-erbB-2 antibodies, in the context of the claimed
invention, would induce an increase in c-erbB-2 phosphorylation.” Appeal Brief, page 4.
Appellants explain:
To support this position, [Hudziak ‘692] was cited. This application
disclosed a method for treating a tumor with antibodies to the HER2
receptor (also known as c-erb-B2 or p185) and a therapeutically effective
amount of a ‘cytotoxic factor.’ See, e.g., [Hudziak] ‘692 application, Page
6, lines 24-27 and Page 7, lines 9-14. The cytotoxic factor described in
the ‘692 application included anti-neoplastic agents, such as those
disclosed for the present application. Compare, e.g., [Hudziak] ‘692
application, Page 12, lines 1-10. Like the drug combination claimed by
Applicant, the combination of Genentech’s antibody and cytotoxic factor
was cytotoxic to breast tumor cells. See, e.g., [Hudziak] ‘692 application,
Page 34, lines 15-35; Figs. 5 and 6; Page 8, lines 5-10. Significantly, the
Genentech antibody inhibited the tyrosine kinase activity of the receptor.
See, e.g., [Hudziak] ‘692 application, Page 9, lines 28-29.
Since tyrosine kinase activity is responsible for receptor phosphorylation,
inhibiting it would also inhibit the appearance of any phosphorylation.
Appeal Brief, page 4. Alberts is relied upon by appellants for the proposition that
“phosphorylation as described in [Hudziak] ‘692 application referred to the receptor
protein itself.” Id., page 5.
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