Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line

Biochemical and Biophysical Research Communications

Volumn 311, Issue 2, 2003, Pages 294-299

  Rakus, D ^a   Mamczur, P ^a   Gizak, A ^a   Dus, D ^b   Dzugaj, A ^a  

^a UNIVERSITY OF WROC AW   (Poland)

^b INSTITUTE OF IMMUNOLOGY AND EXPERIMENTAL THERAPY   (Poland)

Author keywords

Aldolase A; Colocalization; Glyconeogenesis; Muscle FBPase; Myocyte; Z line

Indexed keywords

ALPHA ACTININ; FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATE ALDOLASE; MUSCLE ENZYME;

ANIMAL TISSUE; ARTICLE; BIOSENSOR; CONTROLLED STUDY; EVIDENCE BASED MEDICINE; INCUBATION TIME; MUSCLE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN LOCALIZATION; RAT; SKINNED MUSCLE FIBER; VERTEBRATE;

VERTEBRATA;

EID: 0242299766     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.209     Document Type: Article

References (22)

1. Skalecki K., Mularczyk W., Dzugaj A. Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle. Biochem. J. 310:1995;1029-1035.
2. Rakus D., Dzugaj A. Muscle aldolase decreases muscle FBPase sensitivity toward AMP inhibition. Biochem. Biophys. Res. Commun. 275:2000;611-616.
3. Rakus D., Zarzycki M., Dzugaj A. Rabbit muscle fructose-1,6- bisphosphatase is phosphorylated in vivo. Acta Biochim. Pol. 50:2003;115-121.
4. McLane J.A., Holoszy J.O. Glycogen synthesis from lactate in the three types of skeletal muscle. J. Biol. Chem. 254:1979;6548-6553.
5. Ryan C., Radziuk J. Distinguishable substrate pools for muscle glyconeogenesis in lactate-supplemented recovery from exercise. Am. J. Physiol. 269:1995;E538-550.
6. Gleeson T.T. Post-exercise lactate metabolism: a comparative review of sites, pathways, and regulation. Annu. Rev. Physiol. 58:1996;565-581.
7. Rakus D., Pasek M., Krotkiewski H., Dzugaj A. Muscle FBPase in a complex with muscle aldolase is insensitive to AMP inhibition. FEBS Lett. 547:2003;11-14.
8. Gizak A., Rakus D., Dzugaj A. Immunohistochemical localization of human fructose-1,6-bisphosphatase in subcellular structures of myocytes. Histol. Histopathol. 18:2003;135-142.
9. Penhoet E.E., Kochman M., Rutter W.J. Ioslation of fructose diphosphate aldolases A, B, and C. Biochemistry. 8:1969;4391-4395.
10. Rakus D., Skalecki K., Dzugaj A. Kinetic properties of pig (Sus scrofa domestica) and bovine (Bos taurus) D-fructose-1,6-bisphosphate 1-phosphohydrolase (F1,6BPase). Liver-like isozymes in mammalian lung tissue. Comp. Biochem. Physiol. B. 127:2000;123-134.
11. Rakus D., Tillmann H., Wysocki R., Ulaszewski S., Eschrich K., Dzugaj A. Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP. Biol. Chem. 384:2003;51-58.
12. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
13. Goding J.W. Conjugation of antibodies with fluorochromes: modifications to the standard methods. J. Immunol. Methods. 13:1976;215-226.
14. Kraft T., Hornemann T., Stolz M., Nier V., Wallimann T. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ. J. Muscle Res. Cell Motil. 21:2000;691-703.
15. Xu K.Y., Becker L.C. Ultrastructural localization of glycolytic enzymes on sarcoplasmic reticulum vesticles. J. Histochem. Cytochem. 46:1998;419-427.
16. Dolken G., Leisner E., Pette D. Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit. Histochemistry. 43:1975;113-121.
17. Sullivan D.T., MacIntyre R., Fuda N., Fiori J., Barrilla J., Ramizel L. Analysis of glycolytic enzyme colocalization in Drosophila flight muscle. J. Exp. Biol. 206:2003;2031-2038.
18. Lane R.D., Hegazy M.G., Reimann E.M. Subcellular localization of glycogen synthase with monoclonal antibodies. Biochem. Int. 18:1989;961-970.
19. Chowrashi P., Mittal B., Sanger J.M., Sanger J.W. Amorphin is phosphorylase; phosphorylase is an alpha-actinin-binding protein. Cell Motil. Cytoskeleton. 53:2002;125-135.
20. Pette D. Some aspects of supramolecular organization of glycogenolytic and glycolytic enzymes in muscle. Acta Histochem. Suppl. 14:1975;47-68.
21. Masters C.J., Reid S., Don M. Glycolysis-new concepts in an old pathway. Mol. Cell. Biochem. 76:1987;3-14.
22. Ovadi J., Srere P.A. Macromolecular compartmentation and channelling. Int. Rev. Cytol. 192:2000;255-280.