Green Tea Could Help Patients With Bone-Marrow Disorders: Study
- A compound found in green tea may have lifesaving potential for patients
- The patients are susceptible to a fatal condition- light chain amyloidosis
- In presence of green tea, the chains have a different internal structures
Washington: A compound found in green tea may have lifesaving potential for patients with multiple myeloma and amyloidosis, who face often-fatal medical complications associated with bone-marrow disorders, a new study claims. According to researchers at Washington University in the US and colleagues, 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, said Jan Bieschke, assistant professor at Washington University.
The 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.
In the new study the team found that in 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 was not toxic and did not form fibril structures, as happens to organs affected by amyloidosis, he said.
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, said Bieschke.
The research was published in the Journal of Biological Chemistry.