Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide.

@article{Kapurniotu1998ContributionOA,
  title={Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide.},
  author={Aphrodite Kapurniotu and J{\"u}rgen Bernhagen and Norma J. Greenfield and Yousef Al-Abed and Saul Teichberg and Ren{\'e} Frank and Wolfgang Voelter and Richard Bucala},
  journal={European journal of biochemistry},
  year={1998},
  volume={251 1-2},
  pages={208-16}
}
The formation of amyloid within the islets of Langerhans is associated with the development of type II diabetes mellitus and occurs by the aggregation and insolubilization of islet amyloid polypeptide (IAPP). Recent in vitro studies suggest that amyloid formation follows a nucleation-dependent polymerization mechanism, i.e. aggregation is initiated by pre-formed aggregates or nucleation seeds. Modification of the Alzheimer's disease amyloid peptide by advanced glycosylation end products (AGEs… CONTINUE READING

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