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Cited by 573

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

Colon, Wilfredo, Kelly, Jeffery W.·1992·Biochemistry
DOI 10.1021/bi00151a036
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Abstract

Amyloid diseases are caused by the self-assembly of a given protein into an insoluble cross-beta-sheet quaternary structural form which is pathogenic. An understanding of the biochemical mechanism of amyloid fibril formation should prove useful in understanding amyloid disease. Toward this end, a procedure for the conversion of the amyloidogenic protein transthyretin into amyloid fibrils under conditions which mimic the acidic environment of a lysosome has been developed. Association of a structured transthyretin denaturation intermediate is sufficient for amyloid fibril formation in vitro. The rate of fibril formation is pH dependent with significant rates being observed at pHs accessible within the lysosome (3.6-4.8). Far-UV CD spectroscopic studies suggest that transthyretin retains its secondary structural features at pHs where fibrils are formed. Near-UV CD studies demonstrate that transthyretin has retained the majority of its tertiary structure during fibril formation as well. Near-UV CD analysis in combination with glutaraldehyde cross-linking studies suggests that a pH-mediated tetramer to monomer transition is operative in the pH range where fibril formation occurs. The rate of fibril formation decreases markedly at pHs below pH 3.6, consistent with denaturation to a monomeric TTR intermediate which has lost its native tertiary structure and capability to form fibrils. It is difficult to specify with certainty which quaternary structural form of transthyretin is the amyloidogenic intermediate at this time. These difficulties arise because the maximal rate of fibril formation occurs at pH 3.6 where tetramer, traces of dimer, and significant amounts of monomer are observed.(ABSTRACT TRUNCATED AT 250 WORDS)

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Metadata

Authors
Colon, W., & Kelly, J. W.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1992-09-15
Volume
31
Issue
36
Pages
8654-8660
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00151a036
OpenAlex
W2011606718
Cited by
573
References
34
FWCI
3.05
Type
journal article
Language
en
Open access
closed

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