<abstract xmlns="http://www.w3.org/1999/xhtml">

<p>Sperm functions may be influenced by seminal plasma (SP) proteins with affinity to zinc ions. The aim of the study was to isolate and characterise zinc-binding proteins (ZnBPs) from stallion SP using proteomic tools. Zinc-binding proteins were isolated from the SP of eight stallions by zinc-affinity chromatography. They were analysed in the SDS-PAGE system, and peptide extracts were prepared. Samples of ZnBPs isolated from stallion SP were injected onto the nLC-1000 nanoflow HPLC system coupled via a nano-electrospray ion source to the Orbitrap Elite FTMS mass spectrometer (Thermo Fisher Scientific). Raw MS data were analysed using MaxQuant software with label-free quantification (LFQ). Protein sequences were obtained from the UniProt database. Forty-seven proteins in ZnBPs were annotated in a gene ontology (GO) analysis. The LFQ intensity analysis of individual proteins revealed that ZnBPs comprised mainly clusterin (CLU, 27%), serin protease inhibitor F1 (SERPINF1, 13%), actin, cytoplasmic 1 (ACTB, 9%), nucleobindin 2 (NUCB2, 8%) and polymeric immunoglobulin receptor (PIGR, 6%). This is the first proteomic study to analyse ZnBPs in stallion SP. The present findings show that ZnBPs in stallion SP could play an important role in the regulation of sperm function.</p>
</abstract>

Sperm functions may be influenced by seminal plasma (SP) proteins with affinity to zinc ions. The aim of the study was to isolate and characterise zinc-binding proteins (ZnBPs) from stallion SP using proteomic tools. Zinc-binding proteins were isolated from the SP of eight stallions by zinc-affinity chromatography. They were analysed in the SDS-PAGE system, and peptide extracts were prepared. Samples of ZnBPs isolated from stallion SP were injected onto the nLC-1000 nanoflow HPLC system coupled via a nano-electrospray ion source to the Orbitrap Elite FTMS mass spectrometer (Thermo Fisher Scientific). Raw MS data were analysed using MaxQuant software with label-free quantification (LFQ). Protein sequences were obtained from the UniProt database. Forty-seven proteins in ZnBPs were annotated in a gene ontology (GO) analysis. The LFQ intensity analysis of individual proteins revealed that ZnBPs comprised mainly clusterin (CLU, 27%), serin protease inhibitor F1 (SERPINF1, 13%), actin, cytoplasmic 1 (ACTB, 9%), nucleobindin 2 (NUCB2, 8%) and polymeric immunoglobulin receptor (PIGR, 6%). This is the first proteomic study to analyse ZnBPs in stallion SP. The present findings show that ZnBPs in stallion SP could play an important role in the regulation of sperm function.

Zinc-binding proteins in stallion seminal plasma as potential sperm function regulators

Department of Animal Biochemistry and Biotechnology, Faculty of Animal Bioengineering

University of Warmia and Mazury in Olsztyn

Laboratory of the EIT+ Mass Spectrometry Research Centre

Department of Animal Anatomy, Faculty of Veterinary Medicine

Department of Human Histology and Embryology, School of Medicine, Collegium Medicum

Department of Gamete and Embryo Biology, Institute of Animal Reproduction and Food Research

Annals of Animal Science

This work is licensed under the Creative Commons Attribution 4.0 International License.

Sperm functions may be influenced by seminal plasma (SP) proteins with affinity to zinc ions. The aim of the study was to isolate and characterise zinc-binding...

Zinc-binding proteins in stallion seminal plasma as potential sperm function regulators

Publié en ligne: 19 juil. 2022

Pages: 961 - 976

Reçu: 28 mai 2021

Accepté: 11 janv. 2022

DOI: https://doi.org/10.2478/aoas-2022-0015

Mots clés
proteins, zinc-binding, zinc, seminal plasma, stallion

© 2022 Marzena Mogielnicka-Brzozowska et al., published by Sciendo

This work is licensed under the Creative Commons Attribution 4.0 International License.

Zinc-binding proteins in stallion seminal plasma as potential sperm function regulators

Publié en ligne: 19 juil. 2022

Pages: 961 - 976

Reçu: 28 mai 2021

Accepté: 11 janv. 2022

DOI: https://doi.org/10.2478/aoas-2022-0015

Mots clésproteins, zinc-binding, zinc, seminal plasma, stallion

© 2022 Marzena Mogielnicka-Brzozowska et al., published by Sciendo

This work is licensed under the Creative Commons Attribution 4.0 International License.

Mots clés
proteins, zinc-binding, zinc, seminal plasma, stallion