| Title: | ERK1/2 regulates heat stress-induced lactate production via enhancing the expression of HSP70 in immature boar Sertoli cells |
| Author(s): | Guan JY; Liao TT; Yu CL; Luo HY; Yang WR; Wang XZ; |
| Address: | "Chongqing Key Laboratory of Forage and Herbivore, College of Animal Science and Technology, Southwest University, Beibei, Chongqing, 400716, People's Republic of China. College of Resource and Environment, Southwest University, Beibei, Chongqing, 400716, People's Republic of China. Chongqing Key Laboratory of Forage and Herbivore, College of Animal Science and Technology, Southwest University, Beibei, Chongqing, 400716, People's Republic of China. xianzhong_wang@aliyun.com" |
| DOI: | 10.1007/s12192-018-0925-y |
| ISSN/ISBN: | 1466-1268 (Electronic) 1355-8145 (Print) 1355-8145 (Linking) |
| Abstract: | "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 degrees C. Heat stress was induced in a 43 degrees 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 x 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" |
| Keywords: | Animals Butadienes/pharmacology Glucose Transporter Type 3/metabolism HSP70 Heat-Shock Proteins/*metabolism *Heat-Shock Response Isoenzymes/metabolism L-Lactate Dehydrogenase/metabolism Lactate Dehydrogenase 5 Lactic Acid/*metabolism MAP Kinase Signaling; |
| Notes: | "MedlineGuan, Jia-Yao Liao, Ting-Ting Yu, Chun-Lian Luo, Hong-Yan Yang, Wei-Rong Wang, Xian-Zhong eng Research Support, Non-U.S. Gov't Netherlands 2018/06/27 Cell Stress Chaperones. 2018 Nov; 23(6):1193-1204. doi: 10.1007/s12192-018-0925-y. Epub 2018 Jun 26" |
