Appeal No. 2007-0057
Application No. 10/174,586
We agree with the Examiner that the evidence shows that, despite the
overall similarity of PRO270 and thioredoxin, PRO270 is unlikely to have
the same activity as thioredoxin. Therefore, thioredoxin’s activity cannot be
relied on as a basis for the patentable utility of PRO270.
Appellants argue that “members of the thioredoxin family (1) have a
specific function in mediating the transfer of electrons and (2) that this
mediation has been shown to be applicable to a variety of specific
therapeutic purposes.” (Br. 12.) Appellants argue that Holmgren teaches
that thioredoxin was known to function in electron transfer via reversible
oxidation of two vicinal –SH groups. (Id. at 13.) Appellants also cite Sen,3
as teaching that thioredoxin has “specific effects on gene expression, for
example, by regulating the transcription factor NF-κB.” (Id.) Finally,
Appellants rely on Gallegos4 for its teaching that transfection of human
breast cancer cells with a dominant-negative mutant of thioredoxin reverses
the transformed phenotype. (Id.)
The utilities relied on by Appellants are based on thioredoxin’s
activity in electron transfer and regulation of the oxidation-reduction (redox)
state. Those activities, in turn, rely on the reversible oxidation of the two
cysteine residues in thioredoxin’s active site. Since PRO270 lacks those
cysteine residues, it is unlikely to share thioredoxin’s electron transfer and
3 Sen et al., “Antioxidant and redox regulation of gene transcription,”
FASEB J., Vol. 10, pp. 709-720 (1996).
4 Gallegos et al., “Transfection with human thioredoxin increases cell
proliferation and a dominant-negative mutant thioredoxin reverses the
transformed phenotype of human breast cancer cells,” Cancer Research,
Vol. 56, pp. 5765-5770 (1996).
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