Comparative Proteomic Profiling of Dystroglycan-Associated Proteins in Wild Type, mdx, and Galgt2 Transgenic Mouse Skeletal Muscle
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- 作者：Jung Hae Yoon ; Eric Johnson ; Rui Xu ; Laura T. Martin ; Paul T. Martin ; Federica Montanaro
- 刊名：Journal of Proteome Research
- 出版年：2012
- 出版时间：September 7, 2012
- 年：2012
- 卷：11
- 期：9
- 页码：4413-4424
- 全文大小：404K
- 年卷期：v.11,no.9(September 7, 2012)
- ISSN：1535-3907
文摘
Dystroglycan is a major cell surface glycoprotein receptor for the extracellular matrix in skeletal muscle. Defects in dystroglycan glycosylation cause muscular dystrophy and alterations in dystroglycan glycosylation can impact extracellular matrix binding. Here we describe an immunoprecipitation technique that allows isolation of beta dystroglycan with members of the dystrophin-associated protein complex (DAPC) from detergent-solubilized skeletal muscle. Immunoprecipitation, coupled with shotgun proteomics, has allowed us to identify new dystroglycan-associated proteins and define changed associations that occur within the DAPC in dystrophic skeletal muscles. In addition, we describe changes that result from overexpression of Galgt2, a normally synaptic muscle glycosyltransferase that can modify alpha dystroglycan and inhibit the development of muscular dystrophy when it is overexpressed. These studies identify new dystroglycan-associated proteins that may participate in dystroglycan鈥檚 roles, both positive and negative, in muscular dystrophy.