期刊
AQUACULTURE
卷 530, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.aquaculture.2020.735791
关键词
Fish reproduction; Hormone; Maturation; Spermatozoa; Spermiation; Proteomics
资金
- National Science Centre, Poland [2016/21/B/NZ9/03620]
- Institute of Animal Reproduction and Food Research, Polish Academy of Sciences
Hormonal stimulation of carp sperm resulted in increased sperm viability, movement trajectory parameters, and ATP level, but no significant changes in motility, velocity, or reactive oxygen species levels. The study identified changes in abundance of 48 proteins and 12 phosphoproteins, mainly related to cilium assembly, energy metabolism, protein folding, and signal transduction in spermatozoa.
Hormonal stimulation of spermiation is the most commonly used method for carp kept in captivity. Recent studies have suggested that hormonal stimulation of carp resulted in changes of the seminal plasma proteome. However information regarding proteome changes in spermatozoa upon hormonal stimulation is lacking. Here, we aimed to compare the sperm quality parameters and spermatozoa proteomes of hormonally stimulated (injected with Ovopel) and nonstimulated (injected with PBS) males using a 2D-DIGE approach. Hormonal stimulation was accompanied by increases in sperm viability, sperm movement trajectory parameters and ATP level. No differences were observed in the percentage of sperm motility, velocity or the number of reactive oxygen species (ROS)-positive cells. Hormonal stimulation caused changes in abundance of 48 proteins and 12 phosphoproteins. The majority of these proteins are involved in cilium assembly and organization, energy metabolism, protein folding and signal transduction. The changes in phosphorylation status strongly suggest that sperm maturation is controlled through signal transduction via phosphorylation of the flagellar motile apparatus. For the first time, our results allowed a comprehensive characterization of carp spermatozoa proteins associated with final maturation after hormonal stimulation and allowed a better understanding of the complex mechanisms underlying hormone action in the male reproductive tract. The data have been deposited to the ProteomeXchange with identifier PXD011049.
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