Affiliations: Department of Medicinal Chemistry and Molecular
Pharmacology, HANS Life Sciences Research Building, Purdue University, West
Lafayette, IN, USA | NOX Technologies, Inc., West Lafayette, IN, USA | Department of Foods and Nutrition, Purdue University,
West Lafayette, IN, USA
Note: [] Address for correspondence: D.J. Morré, Department of
Medicinal Chemistry and Molecular Pharmacology, HANS Life Sciences Research
Building, Purdue University, 201 South University Street, West Lafayette, IN
47907-2064, USA. Fax: +1 765 494 4007; E-mail: dj_morre@yahoo.com
Abstract: A proteomics approach with detection on western blots using an
S-peptide tagged pan-tNOX (ENOX2) recombinant (scFv) antibody followed by
alkaline phosphatase-linked anti S has revealed a family of more than 20 ENOX2
isoforms of varying molecular weights (34 to 94 kDa) and mostly of low
isoelectric points (4.6 ± 0.7) based on serum analysis.
Different isoforms characterize cancers of different tissue origins indicative
of both cancer presence and tissue site of origin. ENOX2 proteins are
cancer-associated and differ from constitutive (CNOX or ENOX1) proteins
primarily by the absence of a drug binding site to which the cancer-specific
scFv is directed. All are located on the cell surface where they function both
as terminal oxidases for plasma membrane electron transport and carry out
protein disulfide-thiol interchange. These proteins are shed into the blood and
can also be found in urine. The tNOX isoform technology is under development as
a clinical aid to identify unknown or uncertain primary cancers, evaluation of
metastatic spread in post surgery patients, monitoring remission following
cessation of therapy and for early diagnosis in at-risk populations.
DOI: 10.3233/BIO-2009-1073
Journal: BioFactors, vol. 34, no. 3, pp. 201-207, 2009
