Light chain deamidation in ALλ amyloid-associated proteins

C. Murphy, M. Eulitz, D. Weiss, Alan Solomon

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We previously had postulated that light chain deamidation may be a pathogenic factor in AL amyloidosis based on chemical analysis of fibrils and the amyloidogenic precursor Bence Jones protein from a patient with this disorder. We now have extended this study to an additional 17 ALl extracts and confirmed that, in all cases, the asparaginyl residue at Cl position 22 was deamidated, suggesting that this post-translational modification provided a site for proteolysis, thus rendering the cleaved product fibrillogenic.

Original languageEnglish (US)
Pages (from-to)27-28
Number of pages2
JournalAmyloid
Volume18
Issue numberSUPPL. 1
DOIs
StatePublished - Jun 1 2011

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Bence Jones Protein
Amyloidosis
Post Translational Protein Processing
Proteolysis
Light
amyloid protein AL

All Science Journal Classification (ASJC) codes

  • Internal Medicine

Cite this

Light chain deamidation in ALλ amyloid-associated proteins. / Murphy, C.; Eulitz, M.; Weiss, D.; Solomon, Alan.

In: Amyloid, Vol. 18, No. SUPPL. 1, 01.06.2011, p. 27-28.

Research output: Contribution to journalArticle

Murphy, C. ; Eulitz, M. ; Weiss, D. ; Solomon, Alan. / Light chain deamidation in ALλ amyloid-associated proteins. In: Amyloid. 2011 ; Vol. 18, No. SUPPL. 1. pp. 27-28.
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