ERK1/2 regulates heat stress-induced lactate production via enhancing the expression of HSP70 in immature boar Sertoli cells
| Autor: | Chun-Lian Yu, Xian-Zhong Wang, Wei-Rong Yang, Hong-Yan Luo, Jia-Yao Guan, Ting-Ting Liao |
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| Rok vydání: | 2018 |
| Předmět: |
Male
0301 basic medicine MAP Kinase Signaling System Swine Lactate dehydrogenase A Biochemistry 03 medical and health sciences chemistry.chemical_compound Lactate dehydrogenase Nitriles Testis Butadienes medicine Animals HSP70 Heat-Shock Proteins Lactic Acid Phosphorylation Heat shock education Original Paper education.field_of_study Sertoli Cells Glucose Transporter Type 3 L-Lactate Dehydrogenase biology Glucose transporter Cell Biology Sertoli cell Lactic acid Hsp70 Cell biology Isoenzymes 030104 developmental biology medicine.anatomical_structure chemistry biology.protein Lactate Dehydrogenase 5 Heat-Shock Response Signal Transduction GLUT3 |
| Zdroj: | Cell Stress and Chaperones. 23:1193-1204 |
| ISSN: | 1466-1268 1355-8145 |
| DOI: | 10.1007/s12192-018-0925-y |
| Popis: | Lactate produced by Sertoli cells plays an important role in spermatogenesis, and heat stress induces lactate production in immature boar Sertoli cells. Extracellular signaling regulated kinase 1 and 2 (ERK1/2) participates in heat stress response. However, the effect of ERK1/2 on heat stress-induced lactate production is unclear. In the present study, Sertoli cells were isolated from immature boar testis and cultured at 32 °C. Heat stress was induced in a 43 °C incubator for 30 min. Proteins and RNAs were detected by western blotting and RT-PCR, respectively. Lactate production and lactate dehydrogenase (LDH) activity were detected using commercial kits. Heat stress promoted ERK1/2 phosphorylation, showing a reducing trend with increasing recovery time. In addition, heat stress increased heat shock protein 70 (HSP70), glucose transporter 3 (GLUT3), and lactate dehydrogenase A (LDHA) expressions, enhanced LDH activity and lactate production at 2-h post-heat stress. Pretreatment with U0126 (1 × 10(−6) mol/L), a highly selective inhibitor of ERK1/2 phosphorylation, reduced HSP70, GLUT3, and LDHA expressions and decreased LDH activity and lactate production. Meanwhile, ERK2 siRNA1 reduced the mRNA level of ERK2 and weakened ERK1/2 phosphorylation. Additionally, ERK2 siRNA1 reduced HSP70, GLUT3, and LHDA expressions decreased LDH activity and lactate production. Furthermore, HSP70 siRNA3 downregulated GLUT3 and LDHA expressions and decreased LDH activity and lactate production. These results show that activated ERK1/2 increases heat stress-induced lactate production by enhancing HSP70 expression to promote the expressions of molecules related to lactate production (GLUT3 and LDHA). Our study reveals a new insight in reducing the negative effect of heat stress in boars. |
| Databáze: | OpenAIRE |
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