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Age-related changes in dystrophin-glycoprotein complex and in utrophin are not correlated with intrinsic laryngeal muscles protection in mdx mice. 2011

Renato Ferretti, and Adriana Pertille, and Humberto Santo Neto, and Maria Julia Marques
Departamento de Anatomia, Biologia Celular, Fisiologia e Biofísica, Instituto de Biologia, Universidade Estadual de Campinas, Campinas, São Paulo 13083-970, Brazil.

In this study we investigate whether dystrophic intrinsic laryngeal muscles (ILM) from aged mdx mice show alterations in dystrophin-glycoprotein complex (DGC) components.Immunofluorescence and immunoblotting analyses of beta-sarcoglycan, beta-dystroglycan, and utrophin showed that aged ILM had a similar pattern of changes in aged affected muscles (diaphragm and limb), suggesting that aging leads to changes in utrophin and DGC proteins in dystrophic ILM that cannot be correlated with their protection from dystrophic change.

UI MeSH Term Description Entries
D007821 Laryngeal Muscles The striated muscle groups which move the LARYNX as a whole or its parts, such as altering tension of the VOCAL CORDS, or size of the slit (RIMA GLOTTIDIS). Cricothyroid Muscles,Aryepiglottic Muscle,Arytenoid Muscle,Cricoarytenoid Muscles,Thyroarytenoid Muscles,Thyroepiglottic Muscle,Vocal Muscle,Vocalis Muscle,Aryepiglottic Muscles,Arytenoid Muscles,Cricoarytenoid Muscle,Cricothyroid Muscle,Laryngeal Muscle,Muscle, Aryepiglottic,Muscle, Arytenoid,Muscle, Cricoarytenoid,Muscle, Cricothyroid,Muscle, Laryngeal,Muscle, Thyroarytenoid,Muscle, Thyroepiglottic,Muscle, Vocal,Muscle, Vocalis,Muscles, Aryepiglottic,Muscles, Arytenoid,Muscles, Cricoarytenoid,Muscles, Cricothyroid,Muscles, Laryngeal,Muscles, Thyroarytenoid,Muscles, Thyroepiglottic,Muscles, Vocal,Muscles, Vocalis,Thyroarytenoid Muscle,Thyroepiglottic Muscles,Vocal Muscles,Vocalis Muscles
D008297 Male Males
D008810 Mice, Inbred C57BL One of the first INBRED MOUSE STRAINS to be sequenced. This strain is commonly used as genetic background for transgenic mouse models. Refractory to many tumors, this strain is also preferred model for studying role of genetic variations in development of diseases. Mice, C57BL,Mouse, C57BL,Mouse, Inbred C57BL,C57BL Mice,C57BL Mice, Inbred,C57BL Mouse,C57BL Mouse, Inbred,Inbred C57BL Mice,Inbred C57BL Mouse
D009137 Muscular Dystrophy, Animal MUSCULAR DYSTROPHY that occurs in VERTEBRATE animals. Animal Muscular Dystrophies,Animal Muscular Dystrophy,Dystrophies, Animal Muscular,Dystrophy, Animal Muscular,Muscular Dystrophies, Animal
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D000375 Aging The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time. Senescence,Aging, Biological,Biological Aging
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D016189 Dystrophin A muscle protein localized in surface membranes which is the product of the Duchenne/Becker muscular dystrophy gene. Individuals with Duchenne muscular dystrophy usually lack dystrophin completely while those with Becker muscular dystrophy have dystrophin of an altered size. It shares features with other cytoskeletal proteins such as SPECTRIN and alpha-actinin but the precise function of dystrophin is not clear. One possible role might be to preserve the integrity and alignment of the plasma membrane to the myofibrils during muscle contraction and relaxation. MW 400 kDa.
D049030 Dystroglycans Dystrophin-associated proteins that play role in the formation of a transmembrane link between laminin-2 and DYSTROPHIN. Both the alpha and the beta subtypes of dystroglycan originate via POST-TRANSLATIONAL PROTEIN PROCESSING of a single precursor protein. Dystroglycan,Cranin,Dystroglycan 1,Dystrophin-Associated Glycoprotein 1,alpha-Dystroglycan,beta-Dystroglycan,Dystrophin Associated Glycoprotein 1,alpha Dystroglycan,beta Dystroglycan
D049031 Sarcoglycans A family of transmembrane dystrophin-associated proteins that play a role in the membrane association of the DYSTROPHIN-ASSOCIATED PROTEIN COMPLEX. Sarcoglycan,beta-Sarcoglycan,43-kDa Dystrophin-Associated Glycoprotein,50-kDa Dystrophin-Associated glycoprotein,Adhalin,Sarcoglycan Complex,Sarcoglycan Complexes,alpha-Sarcoglycan,delta-Sarcoglycan,epsilon-Sarcoglycan,gamma-Sarcoglycan,zeta-Sarcoglycan,43 kDa Dystrophin Associated Glycoprotein,50 kDa Dystrophin Associated glycoprotein,Complex, Sarcoglycan,Complexes, Sarcoglycan,Dystrophin-Associated Glycoprotein, 43-kDa,Dystrophin-Associated glycoprotein, 50-kDa,Glycoprotein, 43-kDa Dystrophin-Associated,alpha Sarcoglycan,beta Sarcoglycan,delta Sarcoglycan,epsilon Sarcoglycan,gamma Sarcoglycan,glycoprotein, 50-kDa Dystrophin-Associated,zeta Sarcoglycan

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