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Identification and localization of two triad junctional foot protein isoforms in mature avian fast twitch skeletal muscle

Airey, J A ; Beck, C F ; Murakami, K ; Tanksley, S J ; Deerinck, T J ; Ellisman, M H ; Sutko, J L

The Journal of biological chemistry, 1990-08, Vol.265 (24), p.14187-14194 [Revista revisada por pares]

United States: American Society for Biochemistry and Molecular Biology

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Título:
Identification and localization of two triad junctional foot protein isoforms in mature avian fast twitch skeletal muscle
Autor: Airey, J A ; Beck, C F ; Murakami, K ; Tanksley, S J ; Deerinck, T J ; Ellisman, M H ; Sutko, J L
Materias: Alkaloids - metabolism ; Animals ; Binding, Competitive ; Centrifugation, Density Gradient ; Chickens ; foot protein ; Intracellular Membranes - metabolism ; Macromolecular Substances ; Microsomes - metabolism ; Molecular Weight ; Muscle Proteins - isolation & purification ; Muscle Proteins - metabolism ; Muscles - metabolism ; Receptors, Cholinergic - isolation & purification ; Receptors, Cholinergic - metabolism ; Ryanodine - metabolism ; Ryanodine Receptor Calcium Release Channel
Es parte de: The Journal of biological chemistry, 1990-08, Vol.265 (24), p.14187-14194
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descripción: We report evidence for two foot protein isoforms in chicken pectoral muscle. (i) Two polypeptides with molecular masses of approximately 500 kDa copurify with [3H]ryanodine binding. (ii) Both polypeptides are associated with oligomeric proteins similar in size to the mammalian skeletal muscle foot protein. (iii) The polypeptides are shown to be unique by limited proteolysis. (iv) By using isoform-specific antibodies, the polypeptides are shown to be subunits of different [3H]ryanodine-binding proteins. Using immunolabeling techniques, we have localized these proteins in chicken breast muscle by both light and electron microscopy. (v) From immunofluorescent light microscopy of longitudinal sections, it was determined that both ryanodine-binding protein isoforms exhibit identical repetitive punctate distributions near the Z-lines. (vi) In serial cross-sections both proteins have similar distributions in the same fibers. (vii) Both proteins were found to be associated with the terminal cisternae of the sarcoplasmic reticulum by immunoelectron microscopy. Based on their localization to the triadic junction, their large size and their ability to bind [3H]ryanodine, these proteins are identified as foot proteins. In conclusion, two distinct homo-oligomeric foot proteins coexist in avian fast twitch skeletal muscle. We have termed these proteins, alpha and beta foot proteins.
Editor: United States: American Society for Biochemistry and Molecular Biology
Idioma: Inglés

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Identification and localization of two triad junctional foot protein isoforms in mature avian fast twitch skeletal muscle

Airey, J A ; Beck, C F ; Murakami, K ; Tanksley, S J ; Deerinck, T J ; Ellisman, M H ; Sutko, J L

United States: American Society for Biochemistry and Molecular Biology

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