Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line
| Autor: | Andrzej Dzugaj, Dariusz Rakus, Piotr Mamczur, Danuta Dus, Agnieszka Gizak |
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| Rok vydání: | 2003 |
| Předmět: |
Macromolecular Substances
Muscle Fibers Skeletal Coenzymes Biophysics Fructose 1 6-bisphosphatase Fructose-bisphosphate aldolase Plasma protein binding Actinin Biochemistry Fructose-Bisphosphate Aldolase Animals Myocyte Tissue Distribution Molecular Biology Psoas Muscles biology Aldolase A Colocalization Cell Biology Fructose-Bisphosphatase biology.protein Rabbits Metabolon Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 311:294-299 |
| ISSN: | 0006-291X |
| Popis: | Previously we have reported that in vitro muscle aldolase binds to muscle FBPase [Biochem. Biophys. Res. Commun. 275 (2000) 611-616] which results in the changes of regulatory properties of the latter enzyme. In the present paper, the evidence that aldolase binds to FBPase in living cell is presented. The colocalization experiment, in which aldolase was diffused into skinned fibres that had been pre-incubated with FBPase, has shown that aldolase in the presence of FBPase binds predominantly to the Z-line. The existence of a triple aldolase-FBPase-alpha-actinin complex was confirmed through a real-time interaction analysis using the BIAcore biosensor. The colocalization of FBPase and aldolase on alpha-actinin of the Z-line indicates the existence of glyconeogenic metabolon in vertebrates' myocytes. |
| Databáze: | OpenAIRE |
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