<abstract xmlns="http://www.w3.org/1999/xhtml"><p> Seminal plasma (SP) proteins participate in the process of fertilization by binding to the sperm membrane, particularly to the phosphorylcholine-containing lipids. This study aimed to identify and characterize non-phosphorylcholine-binding and phosphorylcholine-binding proteins (nPch- BPs and PchBPs, respectively) of canine SP. The nPchBPs and PchBPs were isolated from canine SP by affinity chromatography. Electrophoretic studies revealed that the nPchBPs and PchBPs occurred in their native state as high-molecular-weight aggregates. Immunofluorescent staining showed preferential binding of nPchBPs to the sperm acrosome membrane, whereas PchBPs coating was uniformly distributed on the sperm post-acrosomal membrane, mid-piece and tail regions. Analysis with mass spectrometry confirmed that canine prostate specific esterase (CPSE) is a component of the nPchBPs and PchBPs, which is implicated in key mechanisms of protein-coating on the sperm plasma membrane surface. In addition, proteins of known binding properties such as prostaglandin-H2 D-isomerase and lipocalin-like 1 protein, identified in canine SP, might have a specific role in the fertilization-associated processes.</p></abstract>

Seminal plasma (SP) proteins participate in the process of fertilization by binding to the sperm membrane, particularly to the phosphorylcholine-containing lipids. This study aimed to identify and characterize non-phosphorylcholine-binding and phosphorylcholine-binding proteins (nPch- BPs and PchBPs, respectively) of canine SP. The nPchBPs and PchBPs were isolated from canine SP by affinity chromatography. Electrophoretic studies revealed that the nPchBPs and PchBPs occurred in their native state as high-molecular-weight aggregates. Immunofluorescent staining showed preferential binding of nPchBPs to the sperm acrosome membrane, whereas PchBPs coating was uniformly distributed on the sperm post-acrosomal membrane, mid-piece and tail regions. Analysis with mass spectrometry confirmed that canine prostate specific esterase (CPSE) is a component of the nPchBPs and PchBPs, which is implicated in key mechanisms of protein-coating on the sperm plasma membrane surface. In addition, proteins of known binding properties such as prostaglandin-H2 D-isomerase and lipocalin-like 1 protein, identified in canine SP, might have a specific role in the fertilization-associated processes.

Identification and characterization of non-phosphorylcholine-binding and phosphorylcholine-binding proteins of canine seminal plasma

Annals of Animal Science

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Seminal plasma (SP) proteins participate in the process of fertilization by binding to the sperm membrane, particularly to the phosphorylcholine-containing...

Identification and characterization of non-phosphorylcholine-binding and phosphorylcholine-binding proteins of canine seminal plasma

Article Category: The biology, physiology, reproduction, and health

Publié en ligne: 01 août 2017

Pages: 771 - 786

Reçu: 10 nov. 2016

Accepté: 08 mai 2017

DOI: https://doi.org/10.1515/aoas-2017-0005

Mots clés
seminal plasma, non-phosphorylcholine-binding proteins, phosphorylcholine-binding proteins, canine

© by Marzena Mogielnicka-Brzozowska

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Identification and characterization of non-phosphorylcholine-binding and phosphorylcholine-binding proteins of canine seminal plasma

Article Category: The biology, physiology, reproduction, and health

Publié en ligne: 01 août 2017

Pages: 771 - 786

Reçu: 10 nov. 2016

Accepté: 08 mai 2017

DOI: https://doi.org/10.1515/aoas-2017-0005

Mots clésseminal plasma, non-phosphorylcholine-binding proteins, phosphorylcholine-binding proteins, canine

© by Marzena Mogielnicka-Brzozowska

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Mots clés
seminal plasma, non-phosphorylcholine-binding proteins, phosphorylcholine-binding proteins, canine