Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

Samir K. Maji(Board of the Swiss Federal Institutes of Technology), Marilyn H. Perrin(Salk Institute for Biological Studies), M.R. Sawaya(Howard Hughes Medical Institute), Sebastian Jessberger(ETH Zurich), Krishna C. Vadodaria(ETH Zurich), Robert A. Rissman(University of California San Diego), Praful S. Singru(Tufts Medical Center), K. Peter R. Nilsson(Linköping University), Rozalyn Simon(Linköping University), David Schubert(Salk Institute for Biological Studies), David Eisenberg(Howard Hughes Medical Institute), Jean Rivier(Salk Institute for Biological Studies), Paul E. Sawchenko(Salk Institute for Biological Studies), Wylie Vale(Salk Institute for Biological Studies), Roland Riek(Salk Institute for Biological Studies)
Science
June 18, 2009
Cited by 1,054Open Access
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Abstract

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.


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