期刊
BIOPHYSICAL CHEMISTRY
卷 218, 期 -, 页码 58-70出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2016.09.008
关键词
Amylin; Islet amyloid polypeptide; Zinc; Amyloid; Diabetes; Oligomer; Islet
资金
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [403525/2012-8, 472779_2012-5, 309330/2014-9]
- Fundacao de Amparo a Pesquisa do Estado do Rio de Janeiro Carlos Chagas Filho (FAPERJ) [E-26/111.383/2010, E-26/102.823/2011, E-26/111.715/2013, E-26 /201.320/2014-BOLSA, E-26/210.911/2015, E-26/202.080/2015]
The secretory granule of the pancreatic beta-cells is a zinc-rich environment copopulated with the hormones amylin and insulin. The human amylin is shown to interact with zinc ions with major contribution from the single histidine residue, which is absent in amylin from other species such as cat, rhesus and rodents. We report here the interaction of murine amylin with zinc ions in vitro. The self-assembly of murine amylin is tightly regulated by zinc and pH. Ion mobility mass spectrometry revealed zinc interaction with monomers and oligomers. Nuclear magnetic resonance confirms the binding of zinc to murine amylin. The aggregation process of murine amylin into amyloid fibrils is accelerated by zinc. Collectively these data suggest a general role of zinc in the modulation of amylin variants oligomerization and amyloid fibril formation. (C) 2016 Elsevier B.V. All rights reserved.
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