Oncose Technology

TECHNOLOGY DESCRIPTION

Researchers estimate that approximately 70% of all proteins encoded by the human genome are glycosylated; that is, they are modified during synthesis by enzymes that add a specific glycan to the primary protein structure.

There is a wealth of scientific evidence that when cells become cancerous, they produce altered glycoprotein structures, detectable using advanced instrumentation in blood serum or urine. Importantly, these changes in glycostructure are not random, but depend instead on the type of cell, the stage of oncogenesis, the type of cancer and other factors. These changes in glycosylation have the potential to serve as specific molecular fingerprints or markers for cancer cells, providing critical information to clinicians wanting to confirm a suspected diagnosis, assess the patient’s prognosis and optimize selection of therapies. How selected markers fractionate, change over time and/or are expressed in tandem with other glycoproteins is expected to provide far greater clinical insight into cancer detection and treatment than current lab tests in use today.
As “proof of concept”, Pierce and Puett have developed successful prototype tests to detect and evaluate specific glycoproteins for three cancers: human chorionic gonadotropin (hCG) for choriocarcinoma; prostate-specific antigen (PSA) for prostate cancer; and pancreatic RNAse (pRNAse) for pancreatic cancer. In each case, variant glycoforms of these markers were detected and measured in cancerous cells—but not in healthy ones. Findings on hCG and choriocarcinoma were published in the March 2005 edition of Analytical Biochemistry.