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Heparin-binding proteins of canine seminal plasma

Heparin-binding proteins (HBP) from seminal plasma have been expected to participate in modulation of the acrosomal reaction, and have been correlated with fertility in some species. However, they have not been described in the dog. The aim of this study was to document the HBPs of canine seminal pl...

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Autores principales: de Souza, Fabiana Ferreira, Martins, Maria Isabel Mello, Fernandes, Carlos Eurico dos Santos, Ribolla, Paulo Eduardo Martins, Lopes, Maria Denise
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103112/
https://www.ncbi.nlm.nih.gov/pubmed/16769106
http://dx.doi.org/10.1016/j.theriogenology.2006.02.016
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author de Souza, Fabiana Ferreira
Martins, Maria Isabel Mello
Fernandes, Carlos Eurico dos Santos
Ribolla, Paulo Eduardo Martins
Lopes, Maria Denise
author_facet de Souza, Fabiana Ferreira
Martins, Maria Isabel Mello
Fernandes, Carlos Eurico dos Santos
Ribolla, Paulo Eduardo Martins
Lopes, Maria Denise
author_sort de Souza, Fabiana Ferreira
collection PubMed
description Heparin-binding proteins (HBP) from seminal plasma have been expected to participate in modulation of the acrosomal reaction, and have been correlated with fertility in some species. However, they have not been described in the dog. The aim of this study was to document the HBPs of canine seminal plasma. Six pooled samples of seminal plasma from three crossbred dogs were used. The HBPs were isolated by heparin affinity chromatography and the fractions recovered were pooled. One-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was carried out on 12 and 18% vertical minigels. The stained gels were scanned and the molecular weight (kDa) values for each band within a lane were calculated by image analysis software. The electrophoresis analysis of the pooled eluded fractions identified 19 bands, with molecular weights varying from 61.5 to 5.2 kDa. Previous studies, using one-dimensional SDS-PAGE, identified two bands (67 and 58.6 kDa), which were positively correlated with some semen parameters (sperm motility, sperm vigor, percentage of morphologically normal sperm and plasma membrane integrity). The 61.5 kDa band detected in the present study apparently corresponded to the 58.6 kDa band identified previously. Canine seminal plasma contained HBP; since HBP modulate the acrosome reaction in other species, they may have the same function in the dog. Further studies are necessary to better characterize this protein and determine if it is associated with fertility in the dog.
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spelling pubmed-71031122020-03-31 Heparin-binding proteins of canine seminal plasma de Souza, Fabiana Ferreira Martins, Maria Isabel Mello Fernandes, Carlos Eurico dos Santos Ribolla, Paulo Eduardo Martins Lopes, Maria Denise Theriogenology Article Heparin-binding proteins (HBP) from seminal plasma have been expected to participate in modulation of the acrosomal reaction, and have been correlated with fertility in some species. However, they have not been described in the dog. The aim of this study was to document the HBPs of canine seminal plasma. Six pooled samples of seminal plasma from three crossbred dogs were used. The HBPs were isolated by heparin affinity chromatography and the fractions recovered were pooled. One-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was carried out on 12 and 18% vertical minigels. The stained gels were scanned and the molecular weight (kDa) values for each band within a lane were calculated by image analysis software. The electrophoresis analysis of the pooled eluded fractions identified 19 bands, with molecular weights varying from 61.5 to 5.2 kDa. Previous studies, using one-dimensional SDS-PAGE, identified two bands (67 and 58.6 kDa), which were positively correlated with some semen parameters (sperm motility, sperm vigor, percentage of morphologically normal sperm and plasma membrane integrity). The 61.5 kDa band detected in the present study apparently corresponded to the 58.6 kDa band identified previously. Canine seminal plasma contained HBP; since HBP modulate the acrosome reaction in other species, they may have the same function in the dog. Further studies are necessary to better characterize this protein and determine if it is associated with fertility in the dog. Elsevier Inc. 2006-10 2006-06-12 /pmc/articles/PMC7103112/ /pubmed/16769106 http://dx.doi.org/10.1016/j.theriogenology.2006.02.016 Text en Copyright © 2006 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
de Souza, Fabiana Ferreira
Martins, Maria Isabel Mello
Fernandes, Carlos Eurico dos Santos
Ribolla, Paulo Eduardo Martins
Lopes, Maria Denise
Heparin-binding proteins of canine seminal plasma
title Heparin-binding proteins of canine seminal plasma
title_full Heparin-binding proteins of canine seminal plasma
title_fullStr Heparin-binding proteins of canine seminal plasma
title_full_unstemmed Heparin-binding proteins of canine seminal plasma
title_short Heparin-binding proteins of canine seminal plasma
title_sort heparin-binding proteins of canine seminal plasma
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7103112/
https://www.ncbi.nlm.nih.gov/pubmed/16769106
http://dx.doi.org/10.1016/j.theriogenology.2006.02.016
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