Biotech Values

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Inhaled Insulin Forms Toxic Pulmonary Amyloid Aggregates

A recent article (August 2010) investigating the effects of inhaled insulin in mice raises concerns for humans. Previous studies investigating the relationship between altered pulmonary function and the use of inhaled insulin have focused on the generation of antibodies toward insulin or with pulmonary inflammation and subsequent airway remodeling. This study demonstrates "that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow." [My guess is denial.]


Lasagna-Reeves CA, Clos AL, Midoro-Hiriuti T, Goldblum RM, Jackson GR, Kayed R. Inhaled Insulin Forms Toxic Pulmonary Amyloid Aggregates. Endocrinology:en.2010-0457. http://endo.endojournals.org/cgi/content/abstract/en.2010-0457v1

It is well known that interfaces, such as polar-nonpolar or liquid-air, play a key role in triggering protein aggregation in vitro, in particular the aggregation of peptides and proteins with the predisposition of misfolding and aggregation. Here we show that the interface present in the lungs predisposes the lungs to form aggregation of inhaled insulin. Insulin inhalers were introduced, and a large number of diabetic patients have used them. Although inhalers were safe and effective, decreases in pulmonary capacity have been reported in response to inhaled insulin.

We hypothesize that the lung air-tissue interface provides a template for the aggregation of inhaled insulin. Our studies were designed to investigate the harmful potential that inhaled insulin has in pulmonary tissue in vivo, through an amyloid formation mechanism.

Our data demonstrate that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow. Our studies exemplify the importance that interfaces play in protein aggregation in vivo, illustrating the potential aggregation of inhaled proteins and the formation of amyloid deposits in the lungs. These insulin deposits resemble the amyloid structures implicated in protein misfolding disorders, such as Alzheimer's and Parkinson's diseases, and could as well be deleterious in nature.