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Insulin: Biosynthesis, Chemistry, and Preparation01:25

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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.
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The pancreatic islets comprising only 1%-2% of the volume are highly vascularized and innervated mini-organs. They contain five endocrine cell types, including β cells that secrete insulin, which is synthesized as a single polypeptide chain, preproinsulin, processed to proinsulin, and finally to insulin and C-peptide. This process is complex and regulated, involving the Golgi complex, the endoplasmic reticulum, and the secretory granules of the β cell.
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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.
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Insulin amyloid polymorphs: implications for iatrogenic cytotoxicity.

Keisuke Yuzu1, Mikael Lindgren2, Sofie Nyström3

  • 1Department of Chemistry and Biology, Graduate School of Science and Engineering, Ehime University 2-5, Bunkyo-cho Matsuyama Ehime 790-8577 Japan zako.tamotsu.us@ehime-u.ac.jp.

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Summary

New fluorescent probes, pFTAA and BTD21, image structural variations in insulin amyloid aggregates. These probes differentiate toxic and less toxic amyloid structures in diabetes patients and in vitro.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Medical Diagnostics

Background:

  • Protein misfolding and aggregation into amyloids are implicated in diseases like amyloidosis.
  • Amyloid-specific fluorescent probes are crucial for studying disease progression and conformational diversity.
  • Insulin amyloids can form in patients with diabetes and in vitro, impacting treatment and disease understanding.

Purpose of the Study:

  • To image and characterize structural polymorphisms of insulin amyloids using novel fluorescent probes.
  • To assess the ability of pFTAA and BTD21 to differentiate between various insulin amyloid structures.
  • To investigate the cytotoxicity of different insulin amyloid aggregate types.

Main Methods:

  • Utilized amyloid-specific fluorescent probes, pFTAA and benzostyryl capped benzothiadiazole (BTD21).
  • Imaged insulin-derived amyloid aggregates from subcutaneous injection sites in diabetic patients.
  • Formed and analyzed insulin amyloids in vitro, assessing structural polymorphisms and cytotoxicity.

Main Results:

  • pFTAA and BTD21 successfully imaged structural polymorphisms in insulin amyloids both in vivo and in vitro.
  • The probes distinguished between different insulin amyloid structures, including fibrils and filaments.
  • Insulin preparations formed diverse amyloid aggregates with varying cytotoxicities; pFTAA-positive aggregates were more cytotoxic than BTD21-positive ones.

Conclusions:

  • Amyloid-specific fluorescent probes pFTAA and BTD21 are effective tools for characterizing insulin amyloid structural diversity.
  • Distinct amyloid polymorphic structures with differential cytotoxicities are formed by insulin preparations in vivo and in vitro.
  • These findings advance the understanding of insulin amyloid formation and its implications in diabetes management and disease pathology.