Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice.

Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Research Abstract Details 

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Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Abstract Text:

Niaz Cohen,Elena Kudryashova,Irina Kramerova,Louise V B Anderson,Jacques S Beckmann,Katherine Bushby,Melissa J Spencer,

Calpain 3 (CAPN3) is a calcium-dependent protease, mutations in which cause limb girdle muscular dystrophy type 2A. To explore the physiological function of CAPN3, we compared the proteomes of transgenic mice that overexpress CAPN3 (CAPN3 Tg) and their nontransgenic (non-Tg) counterparts. We first examined known muscular dystrophy-related proteins to determine if overexpression of CAPN3 results in a change in their distribution or concentration. This analysis did not identify any known muscular dystrophy proteins as substrates of CAPN3. Next, we used a proteomic approach to compare and identify differentially represented proteins in 2-DE of CAPN3 Tg and non-Tg mice. LC-MS/MS analysis led to the identification of ten possible substrates for CAPN3, classified into two major functional categories: metabolic and myofibrillar. Myosin light chain 1 (MLC1) was focused upon because our previous studies suggested a role for CAPN3 in sarcomere remodeling. In this study, CAPN3 was shown to proteolyze MLC1 in vitro. These studies are the first to identify possible substrates for CAPN3 in an in vivo system and support a role for CAPN3 in sarcomere remodeling by cleavage of myofibrillar proteins such as MLC1. In addition, these data also suggest a role for CAPN3 in mitochondrial protein turnover.

Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Publishing Authors By Initials

N Cohen,E Kudryashova,I Kramerova,LV Anderson,JS Beckmann,K Bushby,MJ Spencer,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proteomics

VOLUME: 6

Page Numbers: 6075-84

Journal Abbreviation: Proteomics

ISSN: 1615-9853

DAY: 3

MONTH: Nov

YEAR: 2006

Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101092707

Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: methods

Chemical & Substance for Abstract: Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Information

Substance Name: Capn3 protein, mouse

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice.

AFFILIATION: Department of Neurology, and UCLA Duchenne Muscular Dystrophy Research Center, University of California, Los Angeles, CA 90095-7334, USA.

Country: Germany

AGENCY: United States NIAMS

GRANT: AR48177

ACRONYM: AR

MEDLINETA: Proteomics

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