Jan Bieschke of Washington University in St. Louis studies how proteins fold and shape themselves, and how these processes can contribute to a variety of diseases.
Patients with these bone marrow disorders 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.
Light Chain Amyloidosis
Bieschke, assistant professor of biomedical engineering at the School of Engineering & Applied Science, explains:
“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.”
His 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.
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 says.
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.
Epigallocatechine-3-gallate is found in high content in the dried leaves of white tea (4245 mg per 100 g), green tea (7380 mg per 100 g) and, in smaller quantities, black tea. Trace amounts are also found in apple skin, plums, onions, hazelnuts, pecans and carob powder.
Kathrin Andrich, et al Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate The Journal of Biological Chemistry 292, 2328-2344