Pathology faculty present amyloidosis research at international meetings

Guillermo Herrera, M.D., gives a talk on renal AL amyloidosis.

Guillermo Herrera, M.D., professor and chair of pathology at the Whiddon College of Medicine, and Luis del Pozo-Yauner, M.D., Ph.D., assistant professor of pathology, recently presented their research on amyloidosis to international experts in the field.  

They shared key findings from their research at the joint XIX International Symposium on Amyloidosis and the International Kidney & Monoclonal Gammopathy Research Group’s annual meeting, both held in Rochester, Minnesota. The events featured oral presentations and poster sessions highlighting scientific advancements in understanding the causes of amyloidosis and the most effective strategies for diagnosis, prognosis and treatment.

Amyloidosis is a condition in which abnormal proteins called amyloids build up in organs and tissues, disrupting their function. This pathogenic phenomenon is shared by a growing list of diseases, such as Alzheimer's and Parkinson's diseases, type II diabetes mellitus, and light chain-derived (AL) amyloidosis.

“The symposium provided an invaluable opportunity to learn from the most reputable experts about advances in translational and clinical research on the molecular basis of amyloid aggregation and its impact on the group of diseases known as amyloidosis,” del Pozo-Yauner said. 

Herrera presented a talk on the SORL1 receptor, which was identified in his lab a few years ago. SORL1 plays a crucial role in the pathogenesis and progression of renal AL amyloidosis, Herrera said. In particular, it affects renal mesangial cells, which are cells in the kidneys that help filter blood and remove waste products. Understanding the role of SORL1 could potentially lead to new treatments or strategies to prevent the buildup of these harmful proteins in the kidneys.

Luis del Pozo-Yauner, M.D., Ph.D., presents his

research at the XIX International Symposium 

on Amyloidosis.

Del Pozo-Yauner presented research on developing conformation-sensitive antibodies for diagnosing and treating AL amyloidosis. Current treatments aim to eliminate the plasma cell clone responsible for producing amyloidogenic light chains, but some patients still suffer organ damage from existing AL deposits. 

“Therefore, there is growing interest in therapies aimed at removing AL deposits by enhancing physiological mechanisms such as enzymatic degradation, cellular uptake, and clearance by specialized macrophage-like cells,” del Pozo-Yauner said. “Antibodies are ideal for this purpose due to their unique recognition properties and biological functions.” 

The research team’s approach involves creating antibodies specific to structurally similar light chains within the same subgroup, rather than broadly targeting all AL types. This method shows potential for developing subgroup-specific antibodies with therapeutic benefits against AL amyloidosis, offering new avenues for improved treatment strategies.

In addition to Herrera and del Pozo-Yauner,  Elba A. Turbat-Herrera, M.D., professor of pathology and interdisciplinary clinical oncology; Jiamin Teng, M.D., Ph.D., associate professor of pathology; Chung Zeng, research associate; and Bing Liu, electron microscopy specialist, contributed to the research.