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Related Concept Videos

Amyloid Fibrils03:03

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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. 
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Rapid Generation of Amyloid from Native Proteins In vitro
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Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.

Rehana Akter1, Ping Cao1, Harris Noor1

  • 1Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400, USA.

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Islet amyloid polypeptide (IAPP) aggregation contributes to type-2 diabetes complications and islet transplant failure. Further research is needed to understand IAPP amyloid formation and its role in beta-cell death.

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Biophysics

Background:

  • Islet amyloid polypeptide (IAPP, or amylin) is crucial for glucose homeostasis.
  • IAPP aggregation into islet amyloid is implicated in type-2 diabetes, beta-cell dysfunction, and transplant failure.
  • Emerging evidence suggests IAPP aggregation's role in type-2 diabetes cardiovascular complications and potentially type-1 diabetes.

Purpose of the Study:

  • To elucidate the mechanisms underlying IAPP amyloid formation in vitro and in vivo.
  • To define the mechanisms of IAPP-induced beta-cell death.
  • To address open questions regarding IAPP's role in diabetes and develop therapeutic strategies.

Main Methods:

  • Investigating proposed mechanisms of beta-cell death, including inflammasome activation, autophagy defects, ER stress, reactive oxygen species, and membrane disruption.
  • Evaluating the relevance of biophysical studies to in vivo conditions.
  • Exploring factors triggering IAPP amyloid formation and its potential role in type-1 diabetes.

Main Results:

  • The precise mechanisms of IAPP amyloid formation and IAPP-induced beta-cell death remain largely undefined.
  • Multiple pathways, including inflammasome activation and ER stress, are proposed to contribute to beta-cell demise.
  • The in vivo relevance of reductionist biophysical studies requires further investigation.

Conclusions:

  • Understanding IAPP amyloidosis is critical for addressing type-2 diabetes complications and improving islet transplantation outcomes.
  • Further research is needed to clarify the molecular mechanisms of IAPP aggregation and beta-cell toxicity.
  • Developing therapeutic inhibitors and novel IAPP variants holds promise for diabetes management.