Why and by How Much is Insulin Absorption Reduced by Insulin-derived Amyloidosis? A Scoping Review.

Yakugaku Zasshi

Department of Clinical Pharmacology, School of Nursing, Faculty of Medicine, University of Miyazaki.

Published: October 2023

AI Article Synopsis

  • * A study reviewed literature on IDLA, revealing insulin absorption at affected sites was 27-94% lower than in normal areas, particularly at palpable IDLA sites.
  • * Four main mechanisms for decreased insulin absorption were identified: reduced blood flow, insulin binding to amyloid fibers, impaired diffusion, and physical handling of insulin. Future research is needed to explore these mechanisms in real-life conditions.

Article Abstract

Insulin therapy is one of the central treatments for diabetes mellitus. Insulin-derived localized amyloidosis (IDLA) is a known skin-related complication of insulin injection. This is one of the causes of poor glycemic control in diabetic patients on insulin therapy. The aim of this study was to review and update the findings on the extent and mechanism of reduced insulin absorption in IDLA. A literature search was conducted on decreased insulin absorption and its mechanisms, and nine references were selected, with seven of these on decreased insulin absorption and four on mechanisms. Insulin absorption at IDLA sites was reported to be 27-94% lower compared with normal sites. In addition, a comparison between nonpalpable and palpable IDLA sites revealed a significant decrease in insulin absorption at the palpable IDLA site. The mechanism of insulin malabsorption was found to be a reduction in insulin absorption at the palpable IDLA sites. Four mechanisms of decreased insulin absorption were identified: decreased subcutaneous blood flow, adsorption of administered insulin onto insulin amyloid fibers, impaired diffusion of insulin subcutaneously, and physical factors such as shaking of the insulin preparation. These mechanisms should be investigated in vivo in the future.

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Source
http://dx.doi.org/10.1248/yakushi.23-00058DOI Listing

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