Masoumeh Moradi-Ozarlou1, Sana Moshari2, Hamed Rezaei Agdam2, Amir Nomanzadeh3, Simineh Shahmohamadlou3, Mazdak Razi4. 1. Department of Pathobiology, Faculty of Veterinary Medicine, University of Tabriz, Tabriz, Iran. Electronic address: moradimasoumeh1985@gmail.com. 2. Department of Basic Sciences, Faculty of Veterinary Medicine, Urmia University, Urmia, Iran; RASTA Specialized Research Institute (RSRI), West Azerbaijan Science and Technology Park (WASTP), Urmia, Iran. 3. RASTA Specialized Research Institute (RSRI), West Azerbaijan Science and Technology Park (WASTP), Urmia, Iran. 4. Department of Basic Sciences, Faculty of Veterinary Medicine, Urmia University, Urmia, Iran. Electronic address: Mazdak.razi@gmail.com.
Abstract
AIMS: Current study was conducted to uncover the effect of high-fat diet (HFD)-induced obesity on heat shock proteins 70-2a and 90 expression levels and to investigate the network between these proteins with PCNA expression, endocrine status of testicular tissue and nucleotide backbone damages. MAIN METHODS: For this purpose, 20 mature male Wistar rats were divided into two groups of control and HFD-received obese animals (n = 10/group). After 8 weeks from obesity approval, the animals were euthanized. The expression levels of Hsp70-2a, Hsp90 and PCNA were analyzed by qRT-PCR and immunohistochemical staining techniques. The Leydig cell distribution/mm2 of interstitial tissue, serum level of testosterone, testicular total antioxidant capacity (TAC), and mRNA and DNA damage were investigated. KEY FINDINGS: The obese (HFD-received) animals represented a remarkable (p < 0.05) increment in the mRNA levels of hsp70-2a and Hsp90, and the percentages of Hsp70-2a+ and Hsp90+ cells/seminiferous tubules with the same criteria. The PCNA mRNA level and the percentage of PCNA+ cells were decreased in the obese (HFD-received) group. The obesity, significantly decreased testicular TAC and with no effect on the Leydig cell distribution, but by reducing their steroidogenic activity resulted in a remarkable (p < 0.05) reduction in serum testosterone level. Finally, severe mRNA and DNA damage were revealed in the obese (HFD-received) group. SIGNIFICANCE: Therefore, considering massive testicular DNA damage in the obese (HFD-received) animals, we can conclude that an increased expression of Hsp70-2a and Hsp90 with no harmony with PCNA could not properly maintain the cellular DNA integrity and/or appropriately finalize the DNA repair process.
AIMS: Current study was conducted to uncover the effect of high-fat diet (HFD)-induced obesity on heat shock proteins 70-2a and 90 expression levels and to investigate the network between these proteins with PCNA expression, endocrine status of testicular tissue and nucleotide backbone damages. MAIN METHODS: For this purpose, 20 mature male Wistar rats were divided into two groups of control and HFD-received obese animals (n = 10/group). After 8 weeks from obesity approval, the animals were euthanized. The expression levels of Hsp70-2a, Hsp90 and PCNA were analyzed by qRT-PCR and immunohistochemical staining techniques. The Leydig cell distribution/mm2 of interstitial tissue, serum level of testosterone, testicular total antioxidant capacity (TAC), and mRNA and DNA damage were investigated. KEY FINDINGS: The obese (HFD-received) animals represented a remarkable (p < 0.05) increment in the mRNA levels of hsp70-2a and Hsp90, and the percentages of Hsp70-2a+ and Hsp90+ cells/seminiferous tubules with the same criteria. The PCNA mRNA level and the percentage of PCNA+ cells were decreased in the obese (HFD-received) group. The obesity, significantly decreased testicular TAC and with no effect on the Leydig cell distribution, but by reducing their steroidogenic activity resulted in a remarkable (p < 0.05) reduction in serum testosterone level. Finally, severe mRNA and DNA damage were revealed in the obese (HFD-received) group. SIGNIFICANCE: Therefore, considering massive testicular DNA damage in the obese (HFD-received) animals, we can conclude that an increased expression of Hsp70-2a and Hsp90 with no harmony with PCNA could not properly maintain the cellular DNA integrity and/or appropriately finalize the DNA repair process.