Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation

@article{Badman1998FibrillarIA,
  title={Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation},
  author={M. K. Badman and Rebecca Pryce and S. B. P. Charg{\'e} and John F. Morris and Anne Clark},
  journal={Cell and Tissue Research},
  year={1998},
  volume={291},
  pages={285-294}
}
Pancreatic islet amyloid, formed from islet amyloid polypeptide, is found in 96% of Type II (non-insulin-dependent) diabetic patients. Islet amyloidosis is progressive and apparently irreversible. Fibrils immunoreactive for islet amyloid polypeptide are found in macrophages associated with amyloid, suggesting that deposits can be phagocytosed. To determine the mechanism for the recognition and internalisation of fibrils, mouse peritoneal macrophages were cultured with fibrillar synthetic human… CONTINUE READING

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