Do mad cow disease prions show up in early pancreatic cancer as biomarkers?

A prion protein identified as a novel early pancreatic cancer biomarker has been found by researchers. Do prions from animal-based foods or even glandular and mammalian ingredients put in vegetarian products play any kind of role in the cause of pancreatic cancer? That's what researchers are currently studying.

What the scientists are researching is the prion protein from mad cow disease to see if, how, and why it shows up in early pancreatic cancer as a biomarker. At Case Western Reserve researchers are following mad cow disease's prion's path from mad cow disease to deadly cancer.

The School of Medicine's primary affiliate is University Hospitals Case Medical Center and is additionally affiliated with MetroHealth Medical Center, the Louis Stokes Cleveland Department of Veterans Affairs Medical Center, and the Cleveland Clinic, with which it established the Cleveland Clinic Lerner College of Medicine of Case Western Reserve University in 2002.

The science team followed the path of prions from mad cow disease to cancer. What further research does this prion protein point to for those studying cancer biomarkers related to prions? Who's researching the relationship between prions and novel pancreatic cancer?

Mad cow disease is caused by the accumulation of an abnormal protein, the prion, in the brain of an affected patient. Outside of the brain, very little is known about prions. Case Western Reserve University School of Medicine, researchers have, for the first time, identified the prion as a biomarker for pancreatic cancer. Pancreatic cancer is one of the most deadly cancers in humans; the five year survival rate is less than 10 percent.

Chaoyang Li, Ph.D., Wei Xin, M.D., and professor of pathology, Man-Sun Sy, Ph.D., discovered the mechanism by which prions causes tumors to grow more aggressively. They published these findings in the September issue of the Journal of Clinical Investigation.

Unlike normal cells, in human pancreatic cancer cells the prion is incompletely processed and binds to a molecule inside the cell known as filamin A. Filamin A is an important regulator of the cell's skeleton and its signaling machineries.

The binding of the incompletely processed prion to filamin A disrupts the cell's organization and signaling. As a result, the tumor cells grow more aggressively. On the other hand, when the prion level is reduced, the tumor cell loses its ability to grow in tissue culture and in animals.

Most importantly, Dr. Li, et al. found that a subpopulation of patients had incompletely processed prion protein in their pancreatic cancer. This subgroup of patients had significantly shorter survival compared to patients whose tumors do not have prion.

According to Dr. Sy, "Currently there is no early diagnostic marker for pancreatic cancer. Detection of the incompletely processed prion may provide such a marker. Preventing the binding of prion to filamin A may open new avenues for therapeutic intervention of this deadly disease." Next, Drs. Li and Sy will look to determine if this type of prion protein expression is seen in other types of cancer.

For further information, view the article at the Case Western Reserve University School of Medicine site, "Prion Protein Identified as a Novel Early Pancreatic Cance Biomarker."

The School of Medicine's primary affiliate is University Hospitals Case Medical Center and is additionally affiliated with MetroHealth Medical Center, the Louis Stokes Cleveland Department of Veterans Affairs Medical Center, and the Cleveland Clinic, with which it established the Cleveland Clinic Lerner College of Medicine of Case Western Reserve University in 2002.