St. Louis, MO (Press Release) – A com­pound found in green tea could have lifesaving poten­tial for patients with multiple myeloma and amyloidosis, who face often-fatal medical com­pli­ca­tions asso­ci­ated with bone-marrow disorders, according to a team of engi­neers at Washington University in St. Louis and their German col­lab­o­rators.

Jan Bieschke, assistant professor of biomedical engi­neer­ing at the School of Engineering & Applied Science, studies how proteins fold and shape themselves, and how these processes can con­trib­ute to a variety of diseases. He says the com­pound epigallocatechine-3-gallate (EGCG), a polyphenol found in green tea leaves, may be of particular benefit to patients struggling with multiple myeloma and amyloidosis. These patients are sus­cep­tible to a frequently fatal con­di­tion called light chain amyloidosis, in which parts of the body’s own anti­bodies become misshapen and can accumulate in various organs, in­­clud­ing the heart and kidneys.

“The idea here is twofold: We wanted to better under­stand how light chain amyloidosis works, and how the green tea com­pound affects this specific protein,” Bieschke said.

Bieschke’s team first isolated individual light chains from nine patients with bone marrow disorders that caused multiple myeloma or amyloidosis, then ran lab experiments to determine how the green tea com­pound affected the light chain protein.

Bieschke pre­vi­ously examined EGCG’s effect in both Parkinson’s and Alzheimer’s disease, and found it pre­vented dangerous buildups of protein present in both diseases. His team had a similar conclusion in this study: In the lab using samples from bone marrow patients, the EGCG transformed light chain amyloid, pre­vent­ing the misshapen form from replicating and accumulating dangerously.

“In the presence of green tea, the chains have a dif­fer­en­t internal structure,” Bieschke said. “The ECGC pulled the light chain into a dif­fer­en­t type of aggregate that wasn’t toxic and didn’t form fibril structures,” as happens to organs affected by amyloidosis.

While Bieschke is gaining a greater under­stand­ing at the intracellular processes involved, his partners at the University of Heidelberg are work­ing in tandem with him, running clin­i­cal trials.

“My group is looking at the mech­a­nism of the protein in a test tube; we are studying how it works on a foun­da­tional level. At the same time, clin­i­cal trials at the Amyloidosis Center in Heidelberg, with Alzheimer’s in Berlin and with Parkinson’s in China examine the process in people. We all want this com­pound to work in a patient.”

The research was recently published in the Journal of Biological Chemistry (Andrich, K, et al, "Aggregation of Full Length Immunoglobulin Light Chains from AL Amyloidosis Patients Is Remodeled by Epigallocatechin-3-gallate," Journal of Biological Chemistry, Dec 2016).

Source: Washington University in St. Louis.