Effect of modulation of nitrogen oxide (II) synthesis under chronic normobaric hypoxia on the isoenzyme spectrum of rat epididimis lactate dehydrogenase
- Authors: Marsyanova Y.A.1, Zvyagina V.I.2, Solovykh D.A.2
-
Affiliations:
- Ryazan State Medical University named after academician I.P. Pavlov
- Ryazan State Medical University named after Academician I.P. Pavlov
- Issue: Vol 26, No 1 (2023)
- Pages: 49-54
- Section: Problems of experimental biology and medicine
- URL: https://journals.eco-vector.com/1560-9596/article/view/535308
- DOI: https://doi.org/10.29296/25877313-2023-01-09
- ID: 535308
Cite item
Abstract
Lactate dehydrogenase have a key role in providing energy to cells under physiological and hypoxic conditions. Changes in the activity of the enzyme can be facilitated by nitric oxide (II), regulating the expression of individual fractions of lactate dehydrogenase.
Aim. To study changes in the isoenzyme spectrum of rat epididymis lactate dehydrogenase under conditions of hypoxia and modulation of nitric oxide (II) synthesis.
Material and methods. Male rats (32) were divided into 4 groups (n=8): 1) chronic normobaric hypoxia; 2) control to group 1; 3) hypoxia together with modeling of nitric oxide deficiency; 4) hypoxia against the background of induction of NO synthesis. The mitochondrial fraction and non-mitochondrial cytoplasm of the head and tail of the epididymis were isolated for laboratory research. The zymogram was obtained by electrophoresis in 7% gel followed by detection by the precipitation reaction of the reduction of nitro blue tetrazolium. The overall activity of lactate dehydrogenase was assessed and the percentage of isoenzyme fractions was calculated. Fractions 1 and X of lactate dehydrogenase were analyzed, the results were considered statistically significant if p<0.05 when comparing two independent samples, and p<0.0167 when comparing three independent samples.
Results. Chronic normobaric hypoxia leads to a decrease in lactate dehydrogenase activity compared to the control group. At the same time, the share of the X-fraction of the enzyme and lactate dehydrogenase 1 increases. Modulation of nitric oxide (II) deficiency against the background of hypoxia increased the activity of the enzyme in the head of the epididymis, where a decrease in the studied fractions of lactate dehydrogenase was observed compared to the group of animals subjected only to hypoxia. Stimulation of the synthesis of nitric oxide (II) during hypoxia led to a decrease in the X-fraction, but an increase in the 1st fraction of lactate dehydrogenase in the head of the epididymis, in the tail of the epididymis, opposite changes were observed.
Conclusion. Hypoxia causes a change in the ratio of lactate dehydrogenase isoenzymes towards an increase in lactate dehydrogenase B and lactate dehydrogenase X, while a deficiency of nitric oxide (II) contributes to a decrease in lactate dehydrogenase X synthesis.
Keywords
Full Text
About the authors
Y. A. Marsyanova
Ryazan State Medical University named after academician I.P. Pavlov
Author for correspondence.
Email: yuliyamarsyanova@yahoo.com
ORCID iD: 0000-0003-4948-4504
SPIN-code: 4075-3169
Assistant, Department of Biological Chemistry with the Course of CLD FAPE
Russian Federation, RyazanV. I. Zvyagina
Ryazan State Medical University named after Academician I.P. Pavlov
Email: vizvyagina@yandex.ru
Ph.D., Associate Professor, Department of Biological Chemistry with the Course of CLD FAPE
Russian Federation, RyazanD. A. Solovykh
Ryazan State Medical University named after Academician I.P. Pavlov
Email: solovykh1234@mail.ru
Student
Russian Federation, RyazanReferences
- Khan A.A., Allemailem K.S., Alhumaydhi F.A., Gowder S.J.T., Rahmani A.H. The biochemical and clinical perspectives of lactate dehydrogenase: an enzyme of active metabolism. Endocr Metab Immune Disord Drug Targets. 2020; 20(6): 855–868.
- Wang H., Zhou Z., Xu M., Li J., Xiao J., Xu Z.Y., Sha J. A spermatogenesis-related gene expression profile in human spermatozoa and its potential clinical applications. J Mol Med (Berl). 2004; 82(5): 317–24.
- Zhao D., Kogut M.H., Genovese K.J., Hsu C.Y., Lee J.T., Farnell Y.Z. Altered expression of lactate dehydrogenase and mono-carboxylate transporter involved in lactate metabolism in broiler wooden breast. Poult Sci. 2020; 99(1): 11–20.
- Blanco A. On the functional significance of LDH X. Johns Hopkins Med J. 1980; 146(6): 231–5.
- Odet F., Duan C., Willis W.D., Goulding E.H., Kung A., Eddy E.M., Goldberg E. Expression of the gene for mouse lactate dehydrogenase C (LDHC) is required for male fertility. Biology of Reproduction. 2008; 79(1): 26–34.
- Odet F., Gabel S., London R.E., Goldberg E., Eddy E.M. Glycolysis and mitochondrial respiration in mouse LDHC-null sperm. Biology of Reproduction. 2013; 88(4): 95, 1–7.
- Nakamura M., Okinaga Sh., Arai K. Metabolism of pachytene primary spermatocytes from rat testes: pyruvate maintenance of adenosine triphosphate level. Biology of Reproduction. 1984; 30(5): 1187–1197.
- Cui Z., Chen Y., Hu M., Lin Y., Zhang S., Kong L., Chen Y. Diagnostic and prognostic value of the cancertestis antigen lactate dehydrogenase C4 in breast cancer. Clin Chim Acta. 2020; 503: 203–209.
- Koslowski M, Türeci O, Bell C., Krause P., Lehr H.A., Brunner J., Seitz G., Nestle F.O., Huber C., Sahin U. Multiple splice variants of lactate dehydrogenase C selectively expressed in human cancer. Cancer Res. 2002; 62(22): 6750–6755.
- Naik A., Decock J. Targeting of lactate dehydrogenase C dysregulates the cell cycle and sensitizes breast cancer cells to DNA damage response targeted therapy. Mol Oncol. 2022; 16(4): 885–903.
- Meiser H., Schulz R. Detection and localization of two constitutive NOS isoforms in bull spermatozoa. Anat. Histol. Embryol. 2003; 32: 321–325.
- Wierońska J.M., Cieślik P., Kalinowski L. Nitric oxide-dependent pathways as critical factors in the consequences and recovery after brain ischemic hypoxia. Biomolecules. 2014; 11(8): 1097.
- Урясьев О.М., Шаханов А.В., Канатбекова Ж.К. Оксид азота и регуляторы его синтеза при хронической обструктивной болезни легких. Российский медико-биологический вестник им. академика И.П. Павлова. 2021; 29(3): 427–434 (Urjas'ev O.M., Shahanov A.V., Kanatbekova Zh.K. Oksid azota i reguljatory ego sinteza pri hronicheskoj obstruktivnoj bolezni legkih. Rossijskij mediko-biologicheskij vestnik im. akademika I.P. Pavlova. 2021; 29(3): 427–434).
- Марсянова Ю.А., Звягина В.И. Влияние сукцината на некоторые показатели биоэнергетического обмена в семенных пузырьках и эпидидимисе у самцов крыс в условиях хронической гипоксии. Вопросы биологической, медицинской и фармацевтической химии. 2021; 24(2): 49–54 (Marsjanova Ju.A., Zvjagina V.I. Vlijanie sukcinata na nekotorye pokazateli biojenergeticheskogo obmena v semennyh puzyr'kah i jepididimise u samcov krys v uslovijah hronicheskoj gipoksii. Voprosy biologicheskoj, medicinskoj i farmacevticheskoj himii. 2021; 24(2): 49–54).
- Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with Folin phenol reagent. J. Biol. Chem. 1951; 193(1): 265–275.