Ultrastructure of diaphragm from dystrophic alpha-sarcoglycan-null mice

• Autorzy: Jakubiec-Puka A. , Biral D. , Krawczyk K. , Betto R.
• Języki publikacji: EN

Abstrakty

EN

α-Sarcoglycan is a 50 kDa single-pass transmembrane glycoprotein exclusively expressed in striated muscle that, together with β-, γ-, and δ-sarcoglycan, forms a sub-complex at the muscle fibre cell membrane. The sarcoglycans are components of the dystrophin-associated glycoprotein (DAG) complex which forms a mechanical link between the intracellular cytoskeleton and extracellular matrix. The DAG complex function is to protect the muscle membrane from the stress of contractile activity and as a structure for the docking of signalling proteins. Genetic defects of DAG components cause muscular dystrophies. A lack or defects of α-sarcoglycan causes the severe type 2D limb girdle muscular dystrophy. α-Sarcoglycan-null (Sgca-null) mice develop progressive muscular dystrophy similar to the human disorder. This animal model was used in the present work for an ultrastructural study of diaphragm muscle. Diaphragm from Sgca-null mouse presents a clear dystrophic phenotype, with necrosis, regeneration, fibre hypertrophy and splitting, excess of collagen and fatty infiltration. Some abnormalities were also observed, such as centrally located nuclei of abnormal shape, fibres containing inclusion bodies within the contractile structure, and fibres with electron-dense material dispersed over almost the entire cell. Additionally, unusual interstitial cells of uncertain identity were detected within muscle fibres. The abnormal ultrastructure of the diaphragm from Sgca-null mice is discussed.

Słowa kluczowe

EN

alpha-sarcoglycan-null mice; mouse; mice; alpha-sarcoglycan; dystrophin; striated muscle; sarcoglycan-deficient mouse; muscle ultrastructure; myopathy; dystrophin-associated glycoprotein

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 2
• Opis fizyczny: p.453-460,fig.,ref.

Twórcy

autor

Jakubiec-Puka A.

• Nencki Institute of Experimental Biology, Warsaw, Poland

autor

Biral D.

autor

Krawczyk K.

autor

Betto R.

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