Abstract:
:Deposition of beta sheets of islet amyloid polypeptide (IAPP) in pancreatic tissue is implicated in the aetiology of type 2 diabetes mellitus (T2DM). IAPP is cleaved from its precursor protein, pro-islet amyloid polypeptide (ProIAPP) and incomplete cleavage results in ProIAPP(1-48), which is found co-deposited with IAPP. Cu(II) prevents IAPP from forming amyloid and herein we investigated if it would also prevent ProIAPP(1-48) from forming beta sheets. Excess Cu(II) prevented ProIAPP(1-48) from forming amyloid and additionally reversed the formation of beta sheets in pre-formed fibrils of the peptide. The latter was also true for ProIAPP(1-48) fibrils formed in the presence of Al(III). An unexpected finding was the formation of spherulites of ProIAPP(1-48) which were only observed in preparations which included Al(III). The spherulites were 40-100 microm in diameter and stained positively for Al(III) suggesting a role for this metal in their formation. The abolition by Cu(II) of the propensity of ProIAPP(1-48) to form amyloid may have important implications for the treatment of T2DM. The immediate significance for diabetes of the equally novel observation of spherulites of ProIAPP(1-48) is unknown though, as with spherulites of Abeta(42) in Alzheimer's disease, there may be implications for the aetiology of the disease.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Exley C,House E,Patel T,Wu L,Fraser PEdoi
10.1016/j.jinorgbio.2010.05.012subject
Has Abstractpub_date
2010-10-01 00:00:00pages
1125-9issue
10eissn
0162-0134issn
1873-3344pii
S0162-0134(10)00139-Xjournal_volume
104pub_type
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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