AER  Vol.1 No.4 , December 2013
Spinach aldolase interactions with rabbit, chicken, and fish muscle phosphofructokinase-1
ABSTRACT
Previous studies showed that rabbit muscle phosphofructokinase-1 (PFK-1) activity losses due to dilution, due to inhibition by ascorbate, and due to some lithium salts were prevented by rabbit muscle aldolase. Chicken PFK-1 and fish PFK-1 interacted with ascorbate and were inhibited, consistent with a previously proposed function that ascorbate facilitates glycogen in resting muscle by inhibiting glycolysis. This report shows that a plant enzyme, spinach aldolase, has the same ability to prevent rabbit muscle PFK-1 activity loses as rabbit muscle aldolase and in some instances it was a better protector from activity losses than rabbit aldolase. Spinach aldolase also protected chicken and fish PFK-1s from inhibitions by ascorbate and from activity losses due to dilution. Prevention of losses PFK-1 activities from animal species by a plant protein, spinach aldolase, suggests an evolutionary conservative relationship between PFK-1s and aldolases.

Cite this paper
Williams, A. , Abbott, A. , Chadwick, J. , Thomas, A. , Cruz, N. , Deng, A. , Ordinanza, L. , Tat, J. and Russell, P. (2013) Spinach aldolase interactions with rabbit, chicken, and fish muscle phosphofructokinase-1. Advances in Enzyme Research, 1, 121-131. doi: 10.4236/aer.2013.14013.
References
[1]   Liu, J., Zhang, X., Yang, F., Li, T., Wei, D. and Ren, Y. (2006) Antimetastatic effect of a lipophilic ascorbic acid derivative with antioxidation through inhibition of tumor invasion. Cancer Chemotherapy and Pharmacology, 57, 584-590. http://dx.doi.org/10.1007/s00280-005-0073-9

[2]   Russell, P., Williams, A., Marquez, K., Tahir, Z., Hosseinian, B. and Lam K. (2008) Some characteristics of Rabbit muscle phosphofruc-tokinase-1 inhibition by ascorbate. Journal of Enzyme Inhibition and Medicinal Chemistry, 23, 411-417. http://dx.doi.org/10.1080/14756360701611621

[3]   Russell, P.J., Williams, A., Amador, X. and Vargas, R. (2004) Aldolase and actin protect rabbit muscle lactate dehydrogenase from ascorbate inhibition. Journal of Enzyme Inhibition and Medicinal Chemistry, 19, 91-98. http://dx.doi.org/10.1080/14756360310001623309

[4]   Struneck, A., Patocka, J. and Sarek, M. (2005) How does lithium mediate its therapeutic effects? Journal of Applied Biomedicine, 3, 25-35.

[5]   Kajda, P.K. and Birch, N.J. (1981) Lithium inhibition of phosphofructokinase. Journal of Inorganic Biochemistry, 14, 275-278.

[6]   Nordenberg, J., Kaplansky, M., Beery, E., Klein, S. and Beitner, R. (1982) Effects of lithium on the activities of phosphofructokinase and phosphoglucomutase and on glucose-1,6-diphosphate levels in rate muscles and liver. Biochemical Pharmacology, 31, 1025-1031. http://dx.doi.org/10.1016/0006-2952(82)90338-0

[7]   Rodriguez-Gil, J.E., Fernandez, J.M., Barbera, A. and Guiovart, J.J. (2000) Lithium’s effects on rat liver glucose metabolism in vivo. Archives of Biochemistry and Biophysics, 375, 377-384. http://dx.doi.org/10.1006/abbi.1999.1679

[8]   Klein, P.S. and Melton, D.A. (1996) A molecular mechanism for the effect of lithium on development. Proceedings of the National Academy of Sciences of the United States of America, 93, 8455-8459. http://dx.doi.org/10.1073/pnas.93.16.8455

[9]   Mann, L., Heldman, E., Shabltiel, G., Belmaker, R.H. and Agam, G. (2008) Lithium preferentially inhibits adenyl cyclase V and VII isoforms. International Journal of Neuropsychopharmacology, 11, 533-539.

[10]   Kemp, R.G. (1975) Phosphofructokinase from rabbit skeletal muscle. In: Woods, W., Ed., Methods in Enzymology, Vol. 42C, Academic Press, New York, 71-77.

[11]   Russell, P.J., Williams, A., Abbott, A., DeRosales, B. and Vargas, R. (2006) Characteristics of rabbit muscle adenylate kinase inhibition by ascorbate. Journal of Enzyme Inhi-bition and Medicinal Chemistry, 21, 61-67. http://dx.doi.org/10.1080/14756360500043372

[12]   Morrissey, J.H. (1981) Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity. Analytical Biochemistry, 117, 307- 310. http://dx.doi.org/10.1016/0003-2697(81)90783-1

[13]   Anderson, R.L., Hanson, T.E. and Sapico, V.L. (1969) D-Fructose-1-phosphate kinase and D-fructose 6-phosphate from Aerobacter aerogenes. The Journal of Biological Chemistry, 244, 6280-6288.

[14]   Vassault, A. (1983) Methods of enzymatic analysis, enzymes I: Oxidoreductases, transferases Vol. III. Verlag Chemie, Basel, 118-126.

[15]   Lebherz, H.G., Lead-better, M.M. and Bradshaw, R.A. (1984) Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase. The Journal of Biological Chemistry, 259, 1011- 1017.

[16]   Wilson, K. and Walker, J. (2001) Principles and techniques of practical biochemistry. Cambridge University Press, Cambridge, 319-204.

[17]   Bradford, M.M. (1976) Determination of protein concentration in the manufacture and characterization of biopharmaceuticals. Analytical Biochemistry, 72, 248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3

[18]   Russell, P., Williams, A., Abbott, A., Chadwick, J., Ehya F., Flores, R. and Hardamon, C. (2010) Effect of lithium salts on lactate dehydrogenase, adenylate kinase, and 1-phosphofructokinase activities. Journal of Enzyme Inhibition and Medicinal Chemistry, 25, 551-556. http://dx.doi.org/10.3109/14756360903357627

[19]   Pelicano, H., Martin, D.S., Xu, R.-H. and Huang, P. (2006) Glycolysis inhibition for anticancer treatment. Oncogene, 25, 4633-4646. http://dx.doi.org/10.1038/sj.onc.1209597

[20]   Herling, A., König, M., Bulik, S. and Holzhütter, H.-G. (2011) Enzymatic features of the glucose metabolism in tumor cells. FEBS Journal, 278, 2436-2459. http://dx.doi.org/10.1111/j.1742-4658.2011.08174.x

[21]   Flurit, R., Ramasarma, T. and Horecker, B.L. (1967) Purification and properties of fructose diphosphate aldolase from spinach leaves. European Journal of Biochemistry, 1, 117-124.

[22]   Kruger, I. and Schnarrenberger, C. (1983) Purification, subunit structure and immunological comparison of fructose-bisphosphate aldolases from spinach and corn leaves. European Journal of Biochemistry, 136, 101-106. http://dx.doi.org/10.1111/j.1432-1033.1983.tb07711.x

[23]   Lebherz, H.G., Leadbetter, M.M. and Bradshaw, R.A. (1984) Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase. The Journal of Biological Chemistry, 259, 1011- 1017.

[24]   Rutter, W.J. (1964) Evolution of aldolases. Federation Proceedings, 23, 1248-1257.

[25]   Nikoulina, S.E., Ciaraldi, T.P., Abrams-Carter, L., Mudaliar, S., Park, K.S. and Henry, R.R. (1997) Regulation of glycogen synthase activity in cultured skeletal muscle cells from subjects with type II diabetes: Role of chronic hyperinsu-linemia and hyperglycemia. Diabetes, 46, 1017-1024. http://dx.doi.org/10.2337/diab.46.6.1017

[26]   Nikoulina, S.E., Ciaraldi, T.P., Carter, L., Mudaliar, S., Park, K.S. and Robert, R.H. (2001) Impaired muscle glycogen synthase in type 2 diabetes is associated with diminished phosphatidylinositol 3-kinase activation. The Journal of Clinical Endocrinology & Metabolism, 86, 4307-4314. http://dx.doi.org/10.1210/jc.86.9.4307

[27]   Shulman, G.I., Rothman, D.L., Jue, T., Stein, P., De-Fronzo, R.A. and Shulman, R.G. (1990) Quantitation of muscle glycogen synthesis in normal subjects and subjects with non-insulin-dependent diabetes by 13C nuclear magnetic resonance spectroscopy. The New England Journal of Medicine, 322, 223-228. http://dx.doi.org/10.1056/NEJM199001253220403

[28]   Henry, R.R., Ciaraldi, T.P., Abrams-Carter, L., Mudaliar, S., Park, K.S. and Nikoulina, S.E. (1996) Glycogen synthase activity is reduced in cultured skeletal muscle cells of non-insulin-dependent diabetes mellitus subjects. Biochemical and molecular mechanisms. Journal of Clinical Investigation, 98, 1231-1236. http://dx.doi.org/10.1172/JCI118906

[29]   Halse, R., Bonavaud, S.M., Armstrong, J.L., McCormack, J.G. and Yeaman, S.J. (2001) Control of glycogen synthesis by glucose, glycogen, and insulin in cultured human muscle cells. Diabetes, 50, 720-726. http://dx.doi.org/10.2337/diabetes.50.4.720

[30]   Chen, H., Karne, R.J., Hall, G., Campia, U., Panza, J.A., Cannon III, R.O., Wang, Y., Katz, A., Levine, M. and Quon, M.J. (2006) High-dose oral vitamin C partially replenishes vitamin C levels in patients with type 2 diabetes and low vitamin C levels but does not improve endothelial dysfunction or insulin resistance. American Journal of Physiology—Heart and Circulatory Physiology, 290, H137-H145. http://dx.doi.org/10.1152/ajpheart.00768.2005

[31]   Cunningham, J.J. (1998) The glucose/insulin system and vitamin C: Implication in insulin-dependent diabetes mellitus. Journal of the American College of Nutrition, 17, 105-108. http://dx.doi.org/10.1080/07315724.1998.10718734

[32]   Will, J.C. and Byers, T. (1996) Does diabetes mellitus increase the requirement for vitamin C? Nutrition Reviews, 54, 193-202. http://dx.doi.org/10.1111/j.1753-4887.1996.tb03932.x

 
 
Top