Rabbit brain and muscle isoforms containing the carboxy-terminal domain of 427 kDa skeletal muscle dystrophin exhibit similar biochemical properties.
The membrane cytoskeletal component dystrophin, which is the protein product of the human Duchenne muscular dystrophy gene, exists in manifold isoforms. Using immunoblot analysis with an antibody to the carboxy-terminal domain of the 427 kDa skeletal muscle dystrophin, we investigated the membrane cytoskeletal properties of dystrophin isoforms from rabbit skeletal muscle, heart and brain. All isoforms identified, including the abundant brain isoforms Dp116 which lacks the amino-terminal actin-binding domain of 427 kDa dystrophin, exhibited similar biochemical properties, i.e. insolubility in non-ionic detergent but extraction from the membrane with alkaline solutions. In muscle, beta-dystroglycan was found to be more tightly associated with dystrophin than alpha-sarcoglycan. These findings agree with the proposed structure of identified muscle and brain dystrophin isoforms and are also consistent with the current model of the dystrophin-glycoprotein complex.
Finn
D M
DM
Department of Pharmacology, University College Dublin, Belfield, Ireland.
Ohlendieck
K
K
D000818:Animals; D001921:Brain / Q000378:metabolism*; D016189:Dystrophin / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D018482:Muscle, Skeletal / Q000378:metabolism*; D011817:Rabbits
D016189:Dystrophin