Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules
By S. Maji, M. Perrin, M. Sawaya, Sebastian Jessberger, K. Vadodaria, R. Rissman, P. Singru, K. Nilsson, Rozalyn Simon, D. Schubert and 5 more. Nature Reviews Neuroscience, 2009
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Plethora of Secretory Amyloids Protein aggregation and the formation of amyloids are associated with several dozen pathological conditions in humans, including Alzheimer's disease, Parkinson's disease, and type II diabetes. In addition, a few functional amyloid systems are known: the prions of fungi, the bacterial protein curli, the protein of chorion of the eggshell of silkworm, and the amyloid protein Pmel-17 involved in mammalian skin pigmentation. Now Maji et al. (p. 328, published online 18 June) propose that endocrine hormone peptides and proteins are stored in an amyloid-like state in secretory granules. Thus, the amyloid fold may represent a fundamental, ancient, and evolutionarily conserved protein structural motif that is capable of performing a wide variety of functions contributing to normal cell and tissue physiology. Peptide and protein hormones are stored in secretory granules in a nonpathological amyloid conformation. Amyloids are highly organized cross–β-sheet–rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer’s disease and type II diabetes. However, amyloids may also have a normal biological function, as demonstrated by fungal prions, which are involved in prion replication, and the amyloid protein Pmel17, which is involved in mammalian skin pigmentation. We found that peptide and protein hormones in secretory granules of the endocrine system are stored in an amyloid-like cross–β-sheet–rich conformation. Thus, functional amyloids in the pituitary and other organs can contribute to normal cell and tissue physiology.
Subfields: Cell Biology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/e39600c873920b3e28b868cd51b7f92caa6eec8d
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Citations in the corpus
- Identifying the amylome, proteins capable of forming amyloid-like fibrils (2010, background): “These include the egg stalk of the green lace-wing fly (4), the Pmel17 protein associated with skin pigmentation (5), and a large number of secretory hormones (6).”
- Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “It has recently been proposed that polypeptide hormones are packed in granules with an amyloid-like conformation (“functional amyloid”) (225).”