Related Experiment Video
Updated: Jun 10, 2026
15:04
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
Published on: September 28, 2019
Inhaled insulin forms toxic pulmonary amyloid aggregates
Cristian A Lasagna-Reeves1, Audra L Clos, Terumi Midoro-Hiriuti
1George and Cynthia Mitchell Center for Neurodegenerative Diseases, Department of Neurology, University of Texas Medical Branch, 301 University Boulevard, Medical Research Building, Room 10.138C, Galveston, Texas 77555-1045, USA.
Endocrinology
|August 6, 2010
Summary
Inhaled insulin can form amyloid deposits in the lungs, potentially reducing pulmonary capacity. This study highlights how lung interfaces can trigger protein aggregation, similar to mechanisms in neurodegenerative diseases.
Area of Science:
- Biochemistry
- Pulmonology
- Protein Misfolding Disorders
Background:
- Interfaces are known to trigger protein aggregation in vitro.
- Inhaled insulin, used by diabetic patients, has been linked to decreased pulmonary capacity.
Purpose of the Study:
- To investigate the potential harm of inhaled insulin in pulmonary tissue.
- To explore amyloid formation as a mechanism for inhaled insulin aggregation in vivo.
- To understand the role of the lung air-tissue interface in protein aggregation.
Main Methods:
- In vivo studies using animal models to assess inhaled insulin's effects.
- Analysis of amyloid formation in lung tissue.
- Measurement of pulmonary airflow changes.
Main Results:
- Inhaled insulin rapidly forms amyloid deposits in the lungs.
- These amyloid deposits cause a significant reduction in pulmonary airflow.
- The lung air-tissue interface acts as a template for insulin aggregation.
Conclusions:
- Interfaces play a critical role in in vivo protein aggregation.
- Inhaled insulin can aggregate into amyloid structures in the lungs.
- These insulin deposits may pose risks similar to those seen in protein misfolding diseases like Alzheimer's and Parkinson's.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
01:25Insulin: Biosynthesis, Chemistry, and Preparation
The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment primarily uses...
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment primarily uses...
01:27Insulin Formulations: Types and Delivery
Insulin preparations are categorized by their duration of action into short-acting and long-acting types. Two strategies are used to modify insulin's absorption and pharmacokinetic profile: slowing the absorption post-subcutaneous injection, or altering human insulin's amino acid sequence or protein structure. These changes retain the insulin's ability to bind to the insulin receptor, but alter its behavior in solution or after injection.
Short-acting insulins are divided into rapid-acting...
Short-acting insulins are divided into rapid-acting...
01:30Production of Pharmaceuticals
Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
01:25Inhalation Anthrax
Anthrax is a zoonotic disease caused by Bacillus anthracis, a Gram-positive, spore-forming bacterium. It primarily affects herbivorous animals but can be transmitted to humans through skin contact, ingestion, or inhalation of spores.Cutaneous anthrax, the most common form, typically results from direct contact with bacterial spores through skin abrasions and is generally less severe. Gastrointestinal anthrax results from eating undercooked or contaminated meat. It affects the mouth, throat, or...