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

Brian R. Anderson; Julius Bogomolovas; Siegfried Labeit; Henk Granzier

doi:10.1074/jbc.M112.401372

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

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

Research output: Contribution to journal › Article › peer-review

34 Scopus citations

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 language	English (US)
Pages (from-to)	5303-5315
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	288
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M112.401372
State	Published - Feb 22 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M112.401372

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title = "Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism",

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.",

author = "Anderson, \{Brian R.\} and Julius Bogomolovas and Siegfried Labeit and Henk Granzier",

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doi = "10.1074/jbc.M112.401372",

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T1 - Single molecule force spectroscopy on titin implicates immunoglobulin domain stability as a cardiac disease mechanism

AU - Anderson, Brian R.

AU - Bogomolovas, Julius

AU - Labeit, Siegfried

AU - Granzier, Henk

PY - 2013/2/22

Y1 - 2013/2/22

N2 - 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.

AB - 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.

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DO - 10.1074/jbc.M112.401372

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AN - SCOPUS:84874325300

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JO - Journal of Biological Chemistry

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

Abstract

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