Isobaric tags for relative and absolute quantification-based proteomic analysis of testis biopsies in rhesus monkeys treated with transient scrotal hyperthermia
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Meng Rao1,2,*, Sha Ma3,*, Shifu Hu1, Hui Lei1, Yanqing Wu1, Yanfei Zhou4, Wei Xia1,5 and Changhong Zhu1,5
1Family Planning Research Institute, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China
2Department of Reproduction and Genetics, The First Affiliated Hospital of Kunming Medical University, Kunming, China
3Wuhan Women and Children's Health Care Center of Hubei Province, Wuhan, China
4Changsha Hospital for Maternal and Child Health Care, Changsha, China
5Reproductive Medicine Center, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China
*These authors have contributed equally to this work
Wei Xia, email: firstname.lastname@example.org
Yanfei Zhou, email: email@example.com
Keywords: heat stress, spermatogenesis, rhesus monkeys, iTRAQ, proteomics
Received: April 26, 2017 Accepted: July 29, 2017 Published: September 08, 2017
This study aimed to examine the cellular and molecular events that occur in rhesus monkey testes after scrotal hyperthermia. Eight male adult rhesus monkeys were subjected to scrotal hyperthermia at 43°C for 30 min daily for 6 consecutive days. Sperm concentration, reproductive hormones, and testis histology were examined before hyperthermia (day 0), and at 8, 15, 30, 45, 60, 75, and 90 days after the initiation of hyperthermia. iTRAQ-based proteomic analysis was conducted on testicular tissues collected on days 0, 8, and 60 to identify differentially expressed proteins at the early and recovery stages of testicular damage. The sperm concentration was significantly decreased at days 30 and 45 after treatment (p < 0.01) and recovered to baseline at day 60. When compared with day 0, 101 and 24 differentially expressed proteins were identified at days 8 and 60 after heat treatment, respectively. The molecular functions of the differentially expressed proteins at day 8 were mainly nucleic acid binding, unfolded protein binding, nucleotide binding, and nucleoside phosphate binding. Spliceosome was enriched as the most significant pathway at day 8. CIRBP, PSIP1, Sam68, and Decorin were validated and found to be consistent with the proteomic data, indicating the reliability of the proteomic profiles identified in this study. In summary, we suggest that the proteins identified in this study may play important roles in heat-induced spermatogenic impairment. Some of these proteins, such as CIRBP, PSIP1, Sam68, and Decorin, may be early molecular targets responsible for spermatogenesis suppression induced by heat treatment.
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