Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism

Brian R. Anderson, Julius Bogomolovas, Siegfried Labeit, Hendrikus "Henk" Granzier

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Background: A mutation found in titin has been linked to arrhythmogenic cardiomyopathy (AC). Results: The mutation increases Ig10 instability and susceptibility to degradation. Conclusion: The mutation compromises the local structure of Ig10 and has a significant effect on Ig10 unfolding dynamics. Significance: Titin is the first sarcomeric protein to be implicated in AC pathology; a novel titin-based disease mechanism is suggested.

Original languageEnglish (US)
Pages (from-to)5303-5315
Number of pages13
JournalJournal of Biological Chemistry
Volume288
Issue number8
DOIs
StatePublished - Feb 22 2013

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Connectin
Immunoglobulins
Heart Diseases
Spectroscopy
Cardiomyopathies
Mutation
Molecules
Pathology
Degradation
Single Molecule Imaging
Immunoglobulin Domains
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism. / Anderson, Brian R.; Bogomolovas, Julius; Labeit, Siegfried; Granzier, Hendrikus "Henk".

In: Journal of Biological Chemistry, Vol. 288, No. 8, 22.02.2013, p. 5303-5315.

Research output: Contribution to journalArticle

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