Regulation of the assembly and amyloid aggregation of murine amylin by zinc
| Autor: | Adriana Fonseca Marques, Luiza C. S. Erthal, Gustavo L.M. Melo, Giselle N. Fontes, Katia M. S. Cabral, Luís Maurício T.R. Lima, Fabio C. L. Almeida, Camila M. Carvalho, Leonardo C. Palmieri |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid endocrine system Magnetic Resonance Spectroscopy endocrine system diseases medicine.medical_treatment Biophysics Amylin chemistry.chemical_element macromolecular substances Zinc Biochemistry Oligomer Mass Spectrometry Mice Protein Aggregates 03 medical and health sciences chemistry.chemical_compound medicine Animals geography geography.geographical_feature_category 030102 biochemistry & molecular biology Insulin Organic Chemistry Hydrogen-Ion Concentration Islet In vitro Islet Amyloid Polypeptide 030104 developmental biology Monomer chemistry Hormone |
| Zdroj: | Biophysical Chemistry. 218:58-70 |
| ISSN: | 0301-4622 |
| Popis: | The secretory granule of the pancreatic β-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. |
| Databáze: | OpenAIRE |
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