Morphological changes and expression of caspases in cattle kidneys in age-related maner

Keywords: caspase-3, caspase-6, caspase-8, kidneys, morphometry, cattle

Abstract

Background. Due to the high metabolic load, cow kidneys are particularly susceptible to industrial factors and undergo morphological changes, including cell death. Current literature lacks data on caspases in the kidneys of cattle of different age groups. This article presents morphological analysis and immunohistochemical staining results to detect caspase-3, -6, and -8 in the kidneys of cattle of different age groups.

Purpose. Evaluate morphological changes in the kidneys of cattle of different ages and their relationship with the expression of caspases.

Materials and methods. The study was conducted at the Ural Scientific Research Veterinary Institute – structural subdivision of Ural Federal Research Center of the Ural Branch of the Russian Academy of Sciences. To study morphological changes in the kidneys, postmortem specimens were collected from animals aged 2.5–10 months, 2–5 years, and 6–8 years. Immunohistochemical staining of the specimens with antibodies to caspases-3, -6, and -8 was performed to assess the intensity of apoptosis in the organ. The number and area of renal corpuscles, the area of the renal glomerulus and the space of the Bowman-Shumlyansky capsule, the proportion of area occupied by these cells within the renal corpuscle, and the proportion of damaged renal corpuscles were measured.

Results. The development of pathological processes in the kidneys of cattle begins at an early age. Morphometric analysis of kidney specimens revealed age-related pathological changes associated with high levels of caspase expression, particularly the effector caspases 3 and 6.

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Author Biographies

Irina M. Petrova, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

Laboratory Assistant at the Department of Animal Genomics and Selection

Maksim V. Bytov, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

Postgraduate Student, Junior Researcher at the Department of Animal Genomics and Selection

Ekaterina A. Tsepeleva, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

Laboratory Assistant at the Department of Animal Genomics and Selection

Sergey L. Khatsko, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

Laboratory Assistant at the Department of Animal Genomics and Selection

Lyudmila I. Drozdova, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

DSc in Veterinary, Professor, Leading Researcher at the Department of Ecology and Non-Contagious Animal Pathology

Irina A. Shkuratova, Ural Federal Agrarian Scientific Research Center, Ural Branch of the Russian Academy of Sciences

Corresponding Member of Russian Academy of Sciences, DSc in Veterinary, Professor, Chief Researcher at the Department of Ecology and Non-Contagious Animal Pathology

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Ding, Z., Zhao, J., & Gao, K. (2022). Total extract of Abelmoschus manihot L. alleviates uric acid-induced renal tubular epithelial injury via inhibition of caspase-8/caspase-3/NLRP3/GSDME signaling. Frontiers in Pharmacology, 13, 907–980. https://doi.org/10.3389/fphar.2022.907980. EDN: https://elibrary.ru/ZIHPSM.

Havasi, A., & Borkan, S. C. (2011). Apoptosis and acute kidney injury. Kidney International, 80(1), 29–40. https://doi.org/10.1038/ki.2011.120.

Kaushal, G. P. (2003). Role of caspases in renal tubular epithelial cell injury. Seminars in Nephrology, 23(5), 425–431. https://doi.org/10.1016/s0270-9295(03)00086-x.

Lebherz-Eichinger, D., Krenn, C. G., & Roth, G. A. (2013). Keratin 18 and heat-shock protein in chronic kidney disease. Advances in Clinical Chemistry, 62, 123–149. https://doi.org/10.1016/b978-0-12-800096-0.00003-2.

Ruchaud, S., Korfali, N., & Earnshaw, W. C. (2002). Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. The EMBO Journal, 21(8), 1967–1977. https://doi.org/10.1093/emboj/21.8.1967. EDN: https://elibrary.ru/LTIXYT.

Sanz, A. B., Sanchez-Niño, M. D., & Ramos, A. M. (2023). Regulated cell death pathways in kidney disease. Nature Reviews Nephrology, 19, 281–299. https://doi.org/10.1038/s41581-023-00694-0. EDN: https://elibrary.ru/ETNIVJ.

Slee, E. A., Adrain, C., & Martin, S. J. (2001). Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. The Journal of Biological Chemistry, 276(10), 7320–7326. https://doi.org/10.1074/jbc.M008363200.

Torres, V. E., & Harris, P. C. (2009). Autosomal dominant polycystic kidney disease: the last 3 years. Kidney International, 76(2), 149–168. https://doi.org/10.1038/ki.2009.128.

Vaidya, S., & Hardy, J. A. (2011). Caspase-6 latent state stability relies on helical propensity. Biochemistry, 50(16), 3282–3287. https://doi.org/10.1021/bi2001664.

Wang, E., Chiou, Y. Y., & Hsieh-Li, H. M. (2017). Overexpression of exogenous kidney-specific Ngal attenuates progressive cyst development and prolongs lifespan in a murine model of polycystic kidney disease. Kidney International, 91(2), 412–422. https://doi.org/10.1016/j.kint.2016.09.005.

Xia, W., Li, Y., & Wu, M. (2021). Gasdermin E deficiency attenuates acute kidney injury by inhibiting pyroptosis and inflammation. Cell Death & Disease, 12(2), 139. https://doi.org/10.1038/s41419-021-03431-2. EDN: https://elibrary.ru/OEJEMW.

Yang, B., Lan, S., Dieudé, M., Sabo-Vatasescu, J. P., & Hébert, M. J. (2018). Caspase-3 is a pivotal regulator of microvascular rarefaction and renal fibrosis after ischemia-reperfusion injury. Journal of the American Society of Nephrology: JASN, 29(7), 1900–1916. https://doi.org/10.1681/ASN.2017050581.

Yang, C., Kaushal, V., & Haun, R. (2008). Transcriptional activation of caspase-6 and -7 genes by cisplatin-induced p53 and its functional significance in cisplatin nephrotoxicity. Cell Death & Differentiation, 15, 530–544. https://doi.org/10.1038/sj.cdd.4402287.

Zhang, H., Deng, Z., & Deng, F. (2024). CHIP drives proteasomal degradation of NUR77 to alleviate oxidative stress and intrinsic apoptosis in cisplatin-induced nephropathy. Communications Biology, 7(1), 1403. https://doi.org/10.1038/s42003-024-07118-0. EDN: https://elibrary.ru/YFRPDB.

Abstract views: 53

Published
2027-02-28
How to Cite
Petrova, I., Bytov, M., Tsepeleva, E., Khatsko, S., Drozdova, L., & Shkuratova, I. (2027). Morphological changes and expression of caspases in cattle kidneys in age-related maner. Siberian Journal of Life Sciences and Agriculture, 19(1), 4001-4019. https://doi.org/10.12731/2658-6649-2027-19-1-1756
Section
Human and animal physiology