Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy

Chad M. Warren; Grace M. Arteaga; Sudarsan Rajan; Rafeeq P.H. Ahmed; David F. Wieczorek; R. John Solaro

doi:10.1002/pmic.200700772

Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy

Chad M. Warren, Grace M. Arteaga, Sudarsan Rajan, Rafeeq P.H. Ahmed, David F. Wieczorek, R. John Solaro

Pediatric and Adolescent Medicine

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

34 Scopus citations

Abstract

Current electrophoretic methods have not been optimized to fully separate post-translationally modified mutant forms of tropomyosin (Tm) from wild-type cardiac samples. We describe here a method employing a modified 2-D PAGE/2-D DIGE protocol, to fully separate native, mutant (E54K), and phosphorylated forms of Tm. Our data demonstrate the first evidence of a significant (∼40%) decrease in Tm phosphorylation in transgenic compared to non-transgenic mouse hearts, and indicate that altered phosphorylation may be a significant factor in the linkage of the E54K mutation to dilated cardiomyopathy.

Original language	English (US)
Pages (from-to)	100-105
Number of pages	6
Journal	Proteomics
Volume	8
Issue number	1
DOIs	https://doi.org/10.1002/pmic.200700772
State	Published - Jan 2008

Keywords

2-D DIGE
Familial cardiomyopathies
Kinases
Phosphatases
Sarcomere

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1002/pmic.200700772

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abstract = "Current electrophoretic methods have not been optimized to fully separate post-translationally modified mutant forms of tropomyosin (Tm) from wild-type cardiac samples. We describe here a method employing a modified 2-D PAGE/2-D DIGE protocol, to fully separate native, mutant (E54K), and phosphorylated forms of Tm. Our data demonstrate the first evidence of a significant (∼40%) decrease in Tm phosphorylation in transgenic compared to non-transgenic mouse hearts, and indicate that altered phosphorylation may be a significant factor in the linkage of the E54K mutation to dilated cardiomyopathy.",

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AU - Arteaga, Grace M.

AU - Rajan, Sudarsan

AU - Ahmed, Rafeeq P.H.

AU - Wieczorek, David F.

AU - Solaro, R. John

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AB - Current electrophoretic methods have not been optimized to fully separate post-translationally modified mutant forms of tropomyosin (Tm) from wild-type cardiac samples. We describe here a method employing a modified 2-D PAGE/2-D DIGE protocol, to fully separate native, mutant (E54K), and phosphorylated forms of Tm. Our data demonstrate the first evidence of a significant (∼40%) decrease in Tm phosphorylation in transgenic compared to non-transgenic mouse hearts, and indicate that altered phosphorylation may be a significant factor in the linkage of the E54K mutation to dilated cardiomyopathy.

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KW - Phosphatases

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Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy

Abstract

Keywords

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