THE CATALYTIC PROPERTIES OF LACTATE DEHYDROGENASE IN SKELETAL MUSCLES AND LIVER OF THE MARSH FROG (PELOPHYLAX RIDIBUNDUS) DEPEND ON ITS ECOLOGICAL AND GEOGRAPHICAL LOCATION

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The marsh frog (Pelophylax ridibundus) has a widespread distribution range, which is due to a variety of adaptations that contribute to the development of tolerance to a wide range of physicochemical environmental factors. Of particular interest are the adaptations of these animals to different levels of oxygen in mid- and high-altitude conditions. In this work, a comparative analysis of the kinetic parameters of lactate dehydrogenase (LDH) in the liver of marsh frogs living in the mountainous and lowland regions of Dagestan was carried out. Animals caught in their habitats were decapitated, the liver and calf muscles were isolated, and they were placed in liquid nitrogen. In the laboratory, the selected tissues were homogenized and mitochondria-free cytosol was obtained by differential centrifugation, in which LDH activity was determined. It was found that LDH activity is significantly higher in the tissues of frogs from mountainous regions: by 42.4% in the muscles and 2.38 times in the liver (p < 0.05). The high efficiency of catalysis is ensured due to significant changes in the catalytic parameters of the enzyme: an increase in Vmax (50.9% in muscles and 70% in the liver (p < 0.05)) and a decrease in Km. (45.9% in muscles and 69% in liver, (p < 0.05)). A more pronounced difference, compared to muscles, between LDH activity in the liver of foothill and lowland populations of frogs suggests that the sensitivity of liver LDH to changes in oxygen tension is higher. The vector of a number of other kinetic parameters of LDH (Ki, Sopt, Δ) in the liver of animals from mountainous landscapes is absolutely opposite to that of skeletal muscles. High activity and modifications of the catalytic properties of LDH in the tissues of marsh frogs living in mid-mountain areas may play an important role in the adaptation of these animals to conditions of oxygen deficiency.

作者简介

Z. Rabadanova

Dagestan State University

编辑信件的主要联系方式.
Email: r.zukhra@yandex.ru
Russian Federation, Republic of Dagestan, Makhachkala

A. Dzhafarova

Dagestan State University

Email: r.zukhra@yandex.ru
Russian Federation, Republic of Dagestan, Makhachkala

参考

  1. Мазанаева ЛФ, Туниев БС (2011) Зоогеографический анализ герпетофауны Дагестана. Соврем герпетол 11 (1/2): 55–76. [Mazanaeva LF, Tuniev BS (2011) Zoogeographic analysis of the herpetofauna of Dagestan. Modern herpetol 11 (1/2): 55–76. (In Russ)].
  2. Niu Y, Zhang X, Xu X, Li 1, Zhang H, Wu, Storey BK, Chen Q (2022) Physiological and Biochemical Adaptations to High Altitude in Tibetan Frogs Nanorana parkeri. Front Physiol 13: 942037. https://doi.org/10.3389/fphys.2022.942037
  3. Yang W, Qi Y, Bi K, Fu J (2012) Toward understanding the genetic basis of adaptation to high-elevation life in poikilothermic species: A comparative transcriptomic analysis of two ranid frogs, Rana chensinensis and R. kukunoris. BMC Genomics 13: 588. https://doi.org/10.1186/1471-2164-13-588
  4. Ma M, Pu P, Niu Z, Zhang T, Wu J, Tang X, Chen Q (2023) A novel mechanism for high-altitude adaptation in hemoglobin of black-spotted frog (Pelophylax nigromaculatus). Front Ecol Evol 11. https://doi.org/10.3389/fevo.2023.1103406
  5. Kierans S, Taylor C (2020) Regulation of glycolysis by the hypoxia-inducible factor (HIF): implications for cellular physiology. J Physiol 599: 23–37. https://doi.org/10.1113/jp280572
  6. Zakhartsev M, Johansen T, Pörtner HO, Blust R (2004) Effects of temperature acclimation on lactate dehydrogenase of cod (Gadus morhua): genetic, kinetic and thermodynamic aspects. J Exp Biol 207 (1): 95–112. https://doi.org/10.1242/jeb.00708
  7. Qiu L, Gulotta M, Callender R (2007) Lactate dehydrogenase undergoes a substantial structural change to bind its substrate. Biophys J 93: 1677–1686. https://doi.org/10.1529/biophysj.107.109397
  8. Cantó C, Gerhart-Hines Z, Feige JN, Lagouge M, Noriega L, Milne JC, Elliott PJ, Puigserver P, Auwerx J (2009) AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458 (7241): 1056–1060. https://doi.org/10.1038/nature07813
  9. Rong Y, Wu W, Ni X, Kuang T, Jin D, Wang D, Lou W (2013) Lactate dehydrogenase A is overexpressed in pancreatic cancer and promotes the growth of pancreatic cancer cells. Tumor Biol 34: 1523–1530. https://doi.org/10.1007/s13277-013-0679-1
  10. Crawford R, Budas G, Jovanovic S, Ranki H, Wilson T, Davies A, Jovanovic A (2002) M-LDH serves as a sarcolemmal KATP channel subunit essential for cell protection against ischemia. EMBO J 15: 3936–3948. https://doi.org/10.1093/emboj/cdf388
  11. Lowry D, Rosembrough H, Farr A, Randall R (1951) Protein measurement with the folin Phenol Reagent. J Biol Chem 193 (1): 265–275. https://doi.org/10.1016/S0021-9258(19)52451-6
  12. Халилов РА, Джафарова АМ, Джабраилова РН, Хизриева СИ (2016) Кинетические характеристики лактатдегидрогеназы мозга крыс при гипотермии Нейрохимия 33 (2): 169–179. [Khalilov RA, Jafarova AM, Dzhabrailova RN, Khizrieva SI (2016) Kinetic characteristics of rat brain lactate dehydrogenase during hypothermia. Neurochemistry 33 (2): 169–179. (In Russ)].
  13. Webster K (2003) Evolution of the coordinate regulation of glycolytic enzyme genes by hypoxia. J Exp Biol 206 (17): 2911–2922. https://doi.org/10.1242/jeb.00516
  14. Spinicci K, Jacquet P, Powathil G, Stéphanou A (2022) Modeling the role of HIF in the regulation of metabolic key genes LDH and PDH: Emergence of Warburg phenotype. Comp Sys Onco 2: e1040. https://doi.org/10.1002/cso2.1040
  15. Bagnall J, Leedale J, Taylor S, Spiller D, White M, Sharkey K, Sée V (2014) Tight Control of Hypoxia-inducible Factor-α Transient Dynamics Is Essential for Cell Survival in Hypoxia. J Biol Chem 289 (9): 5549–5564. https://doi.org/10.1074/jbc.m113.500405
  16. Yang W, Qi Y, Lu B (2017) Gene expression variations in high-altitude adaptation: a case study of the Asiatic toad (Bufo gargarizans). BMC Genet 18 (62). https://doi.org/10.1186/s12863-017-0529-z
  17. Read J, Winter V, Eszes C, Sessions R, Brady R (2001) Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 43 (2): 175–185. https://doi.org/10.1002/1097-0134(20010501)43:2<175::aid-prot1029>3.0.co;2-#
  18. Brooks S, Storey K (1989) Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta. Am J Physiol 257(2):278–283. https://doi.org/10.1152/ajpregu.1989.257.2.R278
  19. Peng H, Deng H, Dyer R, Callender R (2014) Energy Landscape of the Michaelis Complex of Lactate Dehydrogenase: Relationship Catalytic Mech Biochem 53 (11): 1849–1857. https://doi.org/10.1021/bi500215a
  20. Унжаков А, Илюха В, Мацук Н, Белкин В (2007) Роль изоферментов лактатдегидрогеназы в адаптациях млекопитающих Карелии. Труды КарНЦ РАН 11: 118–126. [Unzhakov A, Ilyukha V, Matsuk N, Belkin V (2007) The role of lactate dehyde hydrogenase isoenzymes in adaptations of mammals in Karelia. Proc of KarRC RAS 11: 118–126. (In Russ)].
  21. Moyer F, Speaker C, Wright D (1968) Characteristics of lactate dehydrogenase isozymes in amphibians. N Y Acad Sci 151 (1): 650–669. https://doi.org/10.1111/j.1749-6632.1968.tb11925.x
  22. Enig M, Ramsay J, Eby D (1976) Effect of temperature on pyruvate metabolism in the frog: the role of lactate dehydrogenase isoenzymes. Comp Biochem Physiol. B. Comp Biochem 53 (2): 145–148. https://doi.org/10.1016/0305-0491(76)90025-0
  23. Puchulu-Campanella E, Chu H, Anstee D, Galan J, Tao W, Low P (2013) Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane. J Biol Chem 288 (2): 848–858. https://doi.org/10.1074/jbc.M112.428573
  24. Place S, Hofmann G (2005) Comparison of Hsc70 orthologs from polar and temperate notothenioid fishes: differences in prevention of aggregation and refolding of denatured proteins. Am J Physiol Regul Integr Comp Physiol 288: 1195–1202. https://doi.org/10.1152/ajpregu.00660.2004
  25. Yamamoto S, Storey KB (1988) Dissociation-association of lactate dehydrogenase isozymes: influences on the formation of tetramers versus dimers of M4-LDH and H4-LDH. Internat J Biochem 20 (11): 1261–1265. https://doi.org/10.1016/0020-711x(88)90229-7
  26. Döbeli H, Schoenenberger G (1983) Regulation of lactate dehydrogenase activity: reversible and isoenzyme-specific inhibition of the tetramerization process by peptides. Cell Mol Life Sci 39: 281–282. https://doi.org/10.1007/BF01955304
  27. Pörtner H (2002) Climate variations and the physiological basis of temperature dependent biogeography: systemic to molecular hierarchy of thermal tolerance in animals. Comp Biochem Physiol. A Mol Integrat Physiol 132 (4): 739–761. https://doi.org/10.1016/s1095-6433(02)00045-4
  28. Shahriari A, Dawson NJ, Bell RA, Storey KB (2013) Stable suppression of lactate dehydrogenase activity during anoxia in the foot muscle of littorina littorea and the potential role of acetylation as a novel postranslational regulatory mechanism. Enzyme Res 461374. https://doi.org/10.1155/2013/461374
  29. Abboud J, Storey KB (2013) Novel control of lactate dehydrogenase from the freeze tolerant wood frog: role of posttranslational modifications. Peer J 1 (12). https://doi.org/10.7717/peerj.12
  30. Lehninger A, Nelson D, Cox M (2005). Lehninger principles of biochemistry. New York: W.H. Freeman: 1119.

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