FEBS Letters | |
Does phosphorylase kinase control glycogen biosynthesis in skeletal muscle? | |
Heilmeyer, Ludwig M.G.2  Varsányi, Magdolna2  Meyer, Helmut E.2  Polishchuk, Sergey V.2  Brandt, Neil R.1  | |
[1] Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, FL 33101, USA;Abteilung für Biochemie Supramolekularer Systeme, Institut für Physiologische Chemie, Ruhr-Universität Bochum, 44780 Bochum, Germany | |
关键词: Glycogen biosynthesis; Glycogenin; Proglycogen; Skeletal muscle; Phosphorylase kinase; SR; sarcoplasmic reticulum; HSR; heavy SR vesicles; PVDF; polyvinylidene difluoride; SDS-PAGE; sodium dodecylsulfate polyacrylamide gel-electrophoresis; | |
DOI : 10.1016/0014-5793(95)00260-G | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Immunoblotting as well as enzyme assays demonstrate the presence of the self-glucosylating protein, glycogenin, in the protein-glycogen complex, in the sarcoplasmic reticulum and in phosphorylase kinase. In all three compartments glycogenin occurs in different, albeit, defined glucosylated forms, which upon deglucosylation are converted into a 42 kDa form. We suggest that phosphorylase kinase might have a dual function in glycogen biogenesis: firstly, control of glycogen degradation in the protein-glycogen complex via phosphorylation of glycogen phosphorylase b; secondly, regulation of glycogen biosynthesis on the sarcoplasmic reticular membranes via phosphorylation and thereby inhibition of glycogen synthase.
【 授权许可】
Unknown
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