title: Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide.
abstract: The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. Zinc present in secretory granules has been shown to affect this aggregation. A combination of EXAFS, NMR, and AFM experiments shows that the influence of zinc is most likely due to the stabilization of prefibrillar aggregates of hIAPP.
authors.affiliation: Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
authors.forename: Jeffrey R
authors.initials: JR
authors.lastname: Brender
authors.forename: Janarthanan
authors.initials: J
authors.lastname: Krishnamoorthy
authors.forename: Grazia M L
authors.initials: GM
authors.lastname: Messina
authors.forename: Aniruddha
authors.initials: A
authors.lastname: Deb
authors.forename: Subramanian
authors.initials: S
authors.lastname: Vivekanandan
authors.forename: Carmelo
authors.initials: C
authors.lastname: La Rosa
authors.forename: James E
authors.initials: JE
authors.lastname: Penner-Hahn
authors.forename: Ayyalusamy
authors.initials: A
authors.lastname: Ramamoorthy
mesh_terms: D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D056928:X-Ray Absorption Spectroscopy; D015032:Zinc / Q000737:chemistry*
chemical_list: D058228:Islet Amyloid Polypeptide; D015032:Zinc