Appeal No. 2004-0005 Page 10
Application No. 07/644,361
Lippman, col. 9, lines 11-27. Lippman summarizes their work as follows:
In brief, we have identified a novel polypeptide of 75 kDa that binds to
the p185erbB-2 receptor. The effects of p75 on cells with very high levels of
erbB-2 were similar to the reported effects of the other ligand, gp30. In
contrast to gp30, p75 appears to be specific for p185erbB-2 receptor.
Furthermore, we have provided evidence that cells that overexpress the
erbB-2 receptor may also secrete one of its ligands, which is required for
their proliferation, therefore implying an autocrine loop. we believe that
manipulation of this and other erbB-2 ligands may turn out to have an
important biological effect on growth of human neoplasia.
Id., col. 56, lines 26-36.
Apart from whether the disclosure of Lippman is prior art to the claims on appeal,
this disclosure should be taken into account in the event of further prosecution of this
subject matter since it raises questions as to the results reported in appellants’ Example
8D relied upon in support of their assertion that TAb 250 induces phosphorylation of
c-erbB-2 protein. If the autocrine loop described by Lippman exists in the cells used in
appellants’ Example 8D, it does not appear that one can reasonably ascribe the
induction of phosphorylation to TAb 250 as opposed to the ligands described in
Lippman.
Another document that appellants and the examiner should consider in the event
of further prosecution is Erickson. Erickson states that ErbB2, ErbB3 and ErbB4 have
nearly identical molecular sizes and it is not possible to discern which protein is
becoming tyrosine phosphorylated when whole-cell lysates are evaluated by Western
blot analysis. Id., col. 28, lines 55-64. It appears that appellants’ Example 8D used
whole-cell lysates. Thus, if the cells used in Example 8D also express ErbB3 and
ErbB4, it may not be reasonable for appellants to conclude that the work described in
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