All Title Author
Keywords Abstract

Publish in OALib Journal
ISSN: 2333-9721
APC: Only $99

ViewsDownloads

Relative Articles

The Embryonic Transcriptome of the Red-Eared Slider Turtle (Trachemys scripta)

Characterization of Fructose-1,6-Bisphosphate Aldolase during Anoxia in the Tolerant Turtle, Trachemys scripta elegans: An Assessment of Enzyme Activity, Expression and Structure

Malondialdehyde Suppresses Cerebral Function by Breaking Homeostasis between Excitation and Inhibition in Turtle Trachemys scripta

Ecología reproductiva y cacería de la tortuga Trachemys scripta (Testudinata: Emydidae), en el área de la Depresión Momposina, norte de Colombia

First records of 5 allochthonous species and subspecies of turtles (Trachemys scripta troostii, Mauremys caspica, Mauremys rivulata, Pelodiscus sinensis, Testudo horsfieldii) and new records of subspecies Trachemys scripta elegans in Latvia

Infection status of the estuarine turtles Kinosternon integrum and Trachemys scripta with Gnathostoma binucleatum in Sinaloa, Mexico

Vasculariza??o arterial do trato gastrointestinal da Trachemys scripta elegans, Wied, 1838

Infection status of the estuarine turtles Kinosternon integrum and Trachemys scripta with Gnathostoma binucleatum in Sinaloa, Mexico Estado de la infección con Gnathostoma binucleatum de las tortugas estuarinas Kinosternon integrum y Trachemys scripta en Sinaloa, México

Ecología reproductiva y cacería de la tortuga Trachemys scripta (Testudinata: Emydidae), en el área de la Depresión Momposina, norte de Colombia

More...

Purification and Properties of White Muscle Lactate Dehydrogenase from the Anoxia-Tolerant Turtle, the Red-Eared Slider, Trachemys scripta elegans

DOI: 10.1155/2013/784973

Full-Text   Cite this paper   Add to My Lib

Abstract:

Lactate dehydrogenase (LDH; E.C. 1.1.1.27) is a crucial enzyme involved in energy metabolism in muscle, facilitating the production of ATP via glycolysis during oxygen deprivation by recycling NAD+. The present study investigated purified LDH from the muscle of 20?h anoxic and normoxic T. s. elegans, and LDH from anoxic muscle showed a significantly lower (47%) for L-lactate and a higher value than the normoxic form. Several lines of evidence indicated that LDH was converted to a low phosphate form under anoxia: (a) stimulation of endogenously present protein phosphatases decreased the of L-lactate of control LDH to anoxic levels, whereas (b) stimulation of kinases increased the of L-lactate of anoxic LDH to normoxic levels, and (c) dot blot analysis shows significantly less serine (78%) and threonine (58%) phosphorylation in anoxic muscle LDH as compared to normoxic LDH. The physiological consequence of anoxia-induced LDH dephosphorylation appears to be an increase in LDH activity to promote the reduction of pyruvate in muscle tissue, converting the glycolytic end product to lactate to maintain a prolonged glycolytic flux under energy-stressed anoxic conditions. 1. Introduction Lactate dehydrogenase (LDH; E.C. 1.1.1.27) is a critical enzyme involved in anaerobic metabolism. LDH catalyzes the following reversible reaction: In this capacity, LDH favors the pyruvate reducing direction in skeletal muscle tissue, converting the glycolytic end product to lactate and regenerating the NAD+ pools to maintain a prolonged glycolytic flux [1]. This process is especially critical to those organisms that enter periodically into hypoxic/anoxic environments, where maintaining NAD+/NADH balance is essential for ATP production. Under low oxygen insult, organisms often rely solely on the glycolytic pathway to produce ATP. The greatly reduced production of ATP via glycolysis, as compared to that of oxidative phosphorylation, results in difficult challenges for anoxia-tolerant organisms to overcome. Several of these organisms employ alternate anaerobic pathways to increase ATP yield and/or depress their metabolic rate to survive the low oxygen stress [2]. Furthermore, these organisms typically need to safeguard against the accumulation of acidic glycolytic end products such as lactate, which disrupts cellular homeostasis throughout prolonged exposure to anoxia [2]. Freshwater turtles, Trachemys scripta elegans, have demonstrated a remarkable ability to survive submerged in cold water for 4-5 months during the winter to escape freezing air temperatures. While submerged,

References

[1]  P. W. Hochachka and G. N. Somero, Biochemical Adaptation: Mechanism and Process in Physiological Evolution, Oxford University Press, New York, NY, USA, 2002.
[2]  K. B. Storey and J. M. Storey, “Oxygen limitation and metabolic rate depression,” in Functional Metabolism: Regulation and Adaptation, pp. 415–442, John Wiley & Sons, New York, NY, USA, 2004.
[3]  D. C. Jackson and G. R. Ultsch, “Physiology of hibernation under the ice by turtles and frogs,” Journal of Experimental Zoology A, vol. 313, no. 6, pp. 311–327, 2010.
[4]  D. C. Jackson, C. E. Crocker, and G. R. Ultsch, “Bone and shell contribution to lactic acid buffering of submerged turtles Chrysemys picta bellii at 3°C,” American Journal of Physiology, vol. 278, no. 6, pp. R1564–R1571, 2000.
[5]  S. P. J. Brooks and K. B. Storey, “Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta,” American Journal of Physiology, vol. 257, no. 2, pp. R278–R283, 1989.
[6]  R. A. V. Bell and K. B. Storey, “Regulation of liver glutamate dehydrogenase from an anoxia-tolerant freshwater turtle,” in HOAJ Biology, vol. 1, 2012.
[7]  N. J. Dawson and K. B. Storey, “An enzymatic bridge between carbohydrate and amino acid metabolism: regulation of glutamate dehydrogenase by reversible phosphorylation in a severe hypoxia-tolerant crayfish,” in Journal of Comparative Physiology B, vol. 182, pp. 331–340, 2012.
[8]  C. J. Ramnanan, D. C. McMullen, A. Bielecki, and K. B. Storey, “Regulation of sarcoendoplasmic reticulum Ca2+-ATPase (SERCA) in turtle muscle and liver during acute exposure to anoxia,” Journal of Experimental Biology, vol. 213, no. 1, pp. 17–25, 2010.
[9]  B. Lant and K. B. Storey, “Glucose-6-phosphate dehydrogenase regulation in anoxia tolerance of the freshwater crayfish Orconectes virilis,” Enzyme Research, vol. 2011, Article ID 524906, 2011.
[10]  J. A. Cooper, F. S. Esch, S. S. Taylor, and T. Hunter, “Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinase in vivo and in vitro,” Journal of Biological Chemistry, vol. 259, no. 12, pp. 7835–7841, 1984.
[11]  X. H. Zhong and B. D. Howard, “Phosphotyrosine-containing lactate dehydrogenase is restricted to the nuclei of PC12 pheochromocytoma cells,” Molecular and Cellular Biology, vol. 10, no. 2, pp. 770–776, 1990.
[12]  Z. J. Xiong and K. B. Storey, “Regulation of liver lactate dehydrogenase by reversible phosphorylation in response to anoxia in a freshwater turtle,” Comparative Biochemistry and Physiology B, vol. 163, no. 2, pp. 221–228, 2012.
[13]  S. P. J. Brooks, “A simple computer program with statistical tests for the analysis of enzyme kinetics,” BioTechniques, vol. 13, no. 6, pp. 906–911, 1992.
[14]  J. A. MacDonald and K. B. Storey, “Regulation of ground squirrel Na+K+-ATPase activity by reversible phosphorylation during hibernation,” Biochemical and Biophysical Research Communications, vol. 254, no. 2, pp. 424–429, 1999.
[15]  S. Al-Jassabi, “Purification and kinetic properties of skeletal muscle lactate dehydrogenase from the lizard Agama stellio stellio,” Biokhimiya, vol. 67, no. 7, pp. 948–952, 2002.
[16]  D. C. Jackson, “Lactate accumulation in the shell of the turtle Chrysemys picta bellii during anoxia at 3°C and 10°C,” Journal of Experimental Biology, vol. 200, no. 17, pp. 2295–2300, 1997.
[17]  D. C. Jackson, V. I. Toney, and S. Okamoto, “Lactate distribution and metabolism during and after anoxia in the turtle, Chrysemys picta bellii,” American Journal of Physiology, vol. 271, no. 2, pp. R409–R416, 1996.
[18]  M. Y. Yasykova, S. P. Petukhov, and V. I. Muronetz, “Phosphorylation of lactate dehydrogenase by protein kinase,” Biochemistry, vol. 65, no. 10, pp. 1192–1196, 2000.
[19]  J. Fan, T. Hitosugi, T. W. Chung et al., “Tyrosine phosphorylation of lactate dehydrogenase A is important for NADH/NAD+ redox homeostasis in cancer cells,” Molecular and Cellular Biology, vol. 31, pp. 4938–4950, 2011.
[20]  K. Seguro, T. Tamiya, T. Tsuchiya, and J. J. Matsumoto, “Effect of chemical modifications on freeze denaturation of lactate dehydrogenase,” Cryobiology, vol. 26, no. 2, pp. 154–161, 1989.
[21]  Y. Onishi, K. Hirasaka, I. Ishihara et al., “Identification of mono-ubiquitinated LDH-A in skeletal muscle cells exposed to oxidative stress,” Biochemical and Biophysical Research Communications, vol. 336, no. 3, pp. 799–806, 2005.
[22]  L. L. Manza, S. G. Codreanu, S. L. Stamer et al., “Global shifts in protein sumoylation in response to electrophile and oxidative stress,” Chemical Research in Toxicology, vol. 17, no. 12, pp. 1706–1715, 2004.
[23]  R. Geiss-Friedlander and F. Melchior, “Concepts in sumoylation: a decade on,” Nature Reviews Molecular Cell Biology, vol. 8, no. 12, pp. 947–956, 2007.

Full-Text

comments powered by Disqus