RGD Reference Report - Cross-linking and amyloid formation by N- and C-terminal cysteine derivatives of human apolipoprotein C-II. - Rat Genome Database

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Cross-linking and amyloid formation by N- and C-terminal cysteine derivatives of human apolipoprotein C-II.

Authors: Pham, CL  Hatters, DM  Lawrence, LJ  Howlett, GJ 
Citation: Pham CL, etal., Biochemistry 2002 Dec 3;41(48):14313-22.
RGD ID: 1358409
Pubmed: PMID:12450397   (View Abstract at PubMed)

We have investigated the effect of disulfide cross-linking on amyloid formation by human apolipoprotein (apo) C-II. Three derivatives of apoC-II were generated by inserting a cysteine residue on either the N-terminus (C(N)-apoC-II), C-terminus (C(C)-apoC-II), or both termini (C(N)C(C)-apoC-II). Under reducing conditions, all derivatives formed amyloid with a fibrous ribbon morphology similar to that of wild-type apoC-II. Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links. Fibrils formed by C(C)-apoC-II under oxidizing conditions were closely packed but less tangled than fibrils formed by the C(N) and C(N)C(C) derivatives. The frequency of closed ring structures was more than doubled for C(C)-apoC-II compared to wild-type apoC-II. The kinetics of fibril formation by all cysteine derivatives was markedly enhanced under oxidizing conditions, suggesting that disulfide cross-linking promotes amyloid formation. Substoichiometric levels of preformed C(N)- and C(C)-apoC-II dimers accelerate amyloid formation by wild-type apoC-II. These data suggest that the N- and C-termini of apoC-II are close together in the amyloid fibril such that covalent cross-linking of either the N or C end of apoC-II promotes nucleation and the "seeding" of fibril growth.

Objects referenced in this article
Gene APOC2 apolipoprotein C2 Homo sapiens
Gene Apoc2 apolipoprotein C2 Mus musculus
Gene Apoc2 apolipoprotein C2 Rattus norvegicus

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