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PMID: 25034516 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Seminal plasma proteins of adult boars and correlations with sperm parameters.

Theriogenology ·Vol. 82 ·No. 5 ·2014-09-15 ·Pages 697-707

González-Cadavid V, Martins JA, Moreno FB, Andrade TS, Santos AC, Monteiro-Moreira AC, Moreira RA, Moura AA

Abstract

The present study was conducted to identify the major seminal plasma protein profile of boars and its associations with semen criteria. Semen samples were collected from 12 adult boars and subjected to evaluation of sperm parameters (motility, morphology, vitality, and percent of cells with intact acrosome). Seminal plasma was obtained by centrifugation, analyzed by two-dimensional SDS-PAGE, and proteins identified by mass spectrometry (electrospray ionization quadrupole time-of-flight). We tested regression models using spot intensities related to the same proteins as independent variables and semen parameters as dependent variables (P ≤ 0.05). One hundred twelve spots were identified in the boar seminal plasma gels, equivalent to 39 different proteins. Spermadhesin porcine seminal protein (PSP)-I and PSP-II, as well as spermadhesins AQN-1, AQN-3 and AWN-1 represented 45.2 ± 8% of the total intensity of all spots. Other proteins expressed in the boar seminal plasma included albumin, complement proteins (complement factor H precursor, complement C3 precursor and adipsin/complement factor D), immunoglobulins (IgG heavy chain precursor, IgG delta heavy chain membrane bound form, IgG gamma-chain, Ig lambda chain V-C region PLC3, and CH4 and secreted domains of swine IgM), IgG-binding proteins, epididymal-specific lipocalin 5, epididymal secretory protein E1 precursor, epididymal secretory glutathione peroxidase precursor, transferrin, lactotransferrin and fibronectin type 1 (FN1). On the basis of the regression analysis, the percentage of sperm with midpiece defects was related to the amount of CH4 and secreted domains of swine IgM and FN1 (r² = 0.58, P = 0.006), IgG-binding protein (r² = 0.41, P = 0.024), complement factor H precursor (r² = 0.61, P = 0.014) and lactadherin (r² = 0.45, P = 0.033). The percentage of sperm with tail defects was also related to CH4 and secreted domains of swine IgM and FN1 (r² = 0.40, P = 0.034), IgG-binding protein (r² = 0.35, P = 0.043) and lactadherin (r² = 0.74, P = 0.001). Sperm motility, in turn, had association with the intensities of spots identified as lactadherin (r² = 0.48, P = 0.027). In conclusion, we presently describe the major proteome of boar seminal plasma and significant associations between specific seminal plasma proteins and semen parameters. Such relationships will serve as the basis for determination of molecular markers of sperm function in the swine species.

Keywords
Proteomics Semen parameter Seminal plasma Swine
MeSH Terms
Animals Gene Expression Regulation/physiology Male Semen/chemistry,metabolism Semen Analysis/veterinary Seminal Plasma Proteins/genetics,metabolism Spermatozoa/physiology Swine/physiology
Chemicals
Seminal Plasma Proteins
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
González-Cadavid Verónica
Department of Animal Science, Federal University of Ceará, Ceará, Brazil.
Martins Jorge A M
Department of Animal Science, Federal University of Ceará, Ceará, Brazil.
Moreno Frederico B
School of Pharmacy, University of Fortaleza, Fortaleza, Brazil.
Andrade Tiago S
Xerez Comercial Swine Unit, Maranguape, Ceará, Brazil.
Santos Antonio C L
Department of Animal Science, Federal University of Ceará, Ceará, Brazil.
Monteiro-Moreira Ana Cristina O
School of Pharmacy, University of Fortaleza, Fortaleza, Brazil.
Moreira Renato A
School of Pharmacy, University of Fortaleza, Fortaleza, Brazil.
Moura Arlindo A
Department of Animal Science, Federal University of Ceará, Ceará, Brazil. Electronic address: [email protected].
Article Info
Journal
Theriogenology
Abbr.
Theriogenology
ISSN
1879-3231
Published
2014-09-15
Epub
2014-00-12
Pages
697-707
Language
English
Region
United States
NLM ID
0421510
Subset
IM
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