Effect of zinc-binding proteins of seminal plasma on motility and acrosome integrity of canine spermatozoa stored at 5°C

2013 ◽  
Vol 13 ◽  
pp. 26-27
Author(s):  
M. Mogielnicka-Brzozowska ◽  
L. Fraser ◽  
A. Dziekońska ◽  
K. Tołścik ◽  
R. Strzeżek ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Zinc Binding ◽  
Acrosome Integrity

scholarly journals Proteins of the canine seminal plasma

2016 ◽  
Vol 46 (5) ◽  
pp. 901-908 ◽  
Author(s):  
Annice Aquino-Cortez ◽  
Lúcia Daniel Machado da Silva ◽  
Airton Alencar de Araújo ◽  
Erika da Silva Bezerra de Menezes ◽  
Arlindo de Alencar Araripe Noronha Moura
Keyword(s):  
Alkaline Phosphatase ◽  
Seminal Plasma ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Sperm Quality ◽  
Zinc Binding ◽  
Heparin Binding ◽  
Reproductive Disorders ◽  
The Matrix ◽  
Peroxidase Enzymes

ABSTRACT: Studies have been performed to identify the proteins present in canine seminal plasma (SP) and relate them to sperm quality as well as to discover molecular markers of reproductive tract diseases. There is evidence that heparin-binding proteins, zinc-binding proteins, and lactoferrin as well as the matrix metalloproteinase, superoxide dismutase, catalase, and glutathione peroxidase enzymes are associated with canine sperm quality. Other studies indicate that prolactin and enzymes like arginine esterase, acid phosphatase, and alkaline phosphatase could be successfully used as biomarkers of reproductive disorders. Thus, the present literature review aims to address aspects related to proteins of the canine SP, their influence on fertility, and their importance as biomarkers of reproductive disorders.

Proteomic Characterization of Zinc-Binding Proteins of Canine Seminal Plasma

2015 ◽  
Vol 50 (6) ◽  
pp. 1017-1021 ◽  
Author(s):  
M Mogielnicka-Brzozowska ◽  
N Kowalska ◽  
L Fraser ◽  
W Kordan
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Zinc Binding

scholarly journals Effect of seminal plasma zinc–binding proteins on motility and membrane integrity of canine spermatozoa stored at 5°C

2014 ◽  
Vol 58 (1) ◽  
pp. 163-168 ◽  
Author(s):  
Marzena Mogielnicka-Brzozowska ◽  
Anna Dziekońska ◽  
Rafał Strzeżek ◽  
Michał Załęcki ◽  
Anna Majewska ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Membrane Damage ◽  
Membrane Integrity ◽  
Control Sample ◽  
Incubation Mixture ◽  
Zinc Binding ◽  
Surface Binding ◽  
Positive Effects ◽  
Straight Line

AbstractSperm surface binding sites for non-zinc-binding proteins (nZnBPs) and zinc-binding proteins (ZnBPs) were studied by the fluorescence technique with biotin-labelled proteins. The nZnBPs binding pattern was unspecific, no characteristic sites on plasmalemma were found. ZnBPs were attached mainly to the acrosomal region of sperm head and to the sperm flagellum. ZnBPs added to the incubation mixture of the canine spermatozoa allowed the preservation of higher values for total motility, progressive motility, curvilinear line velocity, straight line velocity, and beat cross frequency (P < 0.05), both at time 0 and after 1 h incubation at 5ºC. The addition of nZnBPs to the incubation mixture caused only weak positive effects when compared with control sample (PBS). A higher percentage of canine-ejaculated spermatozoa with intact membranes were observed when ejaculate was incubated with ZnBPs in comparison to control sample stored with PBS (P < 0.05) or nZnBPs (P < 0.05). Spermatozoa diluted with ZnBPs and nZnBPs exhibited a higher percentage of cells with active mitochondria when compared with control, both at time 0 and after 1 h; however, no statistical differences were observed. Our results emphasise the role of seminal plasma protein in securing the correct quantity and availability of zinc ions as a component regulating the motility of canine spermatozoa. The protective effect of ZnBPs against the cooling effect may be due to their ability of preventing sperm membrane damage.

scholarly journals Zinc-binding proteins from boar seminal plasma -- isolation, biochemical characteristics and influence on spermatozoa stored at 4°C.

2011 ◽  
Vol 58 (2) ◽  
Author(s):  
Marzena Mogielnicka-Brzozowska ◽  
Paweł Wysocki ◽  
Jerzy Strzeżek ◽  
Władysław Kordan
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Binding Proteins ◽  
Control Sample ◽  
Zinc Binding ◽  
Shielding Effect ◽  
Sperm Plasma Membrane ◽  
Native Electrophoresis ◽  
Seminal Plasma Proteins ◽  
Fast Flow

Affinity chromatography on Chelating Sepharose Fast Flow Gel-Zn(2+) was used for fractionation of boar seminal plasma proteins. Approximately 30% of total boar seminal plasma proteins showed affinity for zinc ions (ZnBP fraction). Native electrophoresis (PAGE) of ZnBP revealed six protein fractions which separated into 27 bands under denaturing conditions (SDS/PAGE). Two-dimensional electrophoresis (2D PAGE) showed 148 polypeptides with isoelectric points mostly in the basic and neutral pH range. The zinc-binding proteins comprise mainly 10-20 kDa polypeptides which are probably members of the spermadhesin family. ZnBP present in the incubation mixture of spermatozoa stored for 1 or 24 h at 4 °C allowed preservation of a higher percentage of cells exhibiting linear motility in comparison to a control sample stored in PBS. Presented results indicate that proteins binding Zn(2+) ions have a shielding effect on the sperm plasma membrane and acrosome of spermatozoa, protecting these structures against consequences of cold shock.

scholarly journals The antigenic character of zinc-binding proteins and their localization in boar reproductive tract--a preliminary study.

2013 ◽  
Vol 60 (2) ◽  
Author(s):  
Marzena Mogielnicka-Brzozowska ◽  
Leyland Fraser ◽  
Jerzy Strzeżek ◽  
Władysław Kordan
Keyword(s):  
Seminal Plasma ◽  
Indirect Immunofluorescence ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Protein Complexes ◽  
Zinc Binding ◽  
Immunofluorescence Technique ◽  
Double Immunodiffusion ◽  
Antigenic Protein ◽  
Indirect Immunofluorescence Technique

In this study immunoelectrophoretic and double immunodiffusion analyses were used to investigate the antigenic character of zinc-binding proteins (ZnBPs), whereas the indirect immunofluorescence technique was used to identify their origin in boar reproductive tract. The mmunoelectrophoretic analysis of ZnBPs of the seminal plasma resulted in the appearance of three antigenic protein complexes, while specific immunoreactivity patterns of the anti-ZnBP serum were detected by double immunodiffusion analysis. Indirect immunofluorescence technique confirmed that ZnBPs were secreted by different reproductive tract tissues, suggesting their contributions to the seminal plasma.

Human Epididymis Protein 4 Quantification and Interaction Network Analysis in Seminal Plasma

2019 ◽  
Vol 26 (6) ◽  
pp. 458-465
Author(s):  
Krishna Kant ◽  
Anil K. Tomar ◽  
Pankaj Sharma ◽  
Bishwajit Kundu ◽  
Sarman Singh ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Interaction Network ◽  
Prostatic Acid Phosphatase ◽  
Regulatory Subunit ◽  
Plasma Samples ◽  
Human Seminal Plasma ◽  
Human Epididymis Protein 4 ◽  
Human Epididymis ◽  
Core Proteins

Background: A well-known tissue marker of ovarian cancer, Human Epididymis protein 4 (HE4) is the member of whey acidic four-disulfide core proteins family. Purified from human seminal plasma and characterized as a cross-class protease inhibitor, HE4 was proposed to shield spermatozoa against proteolytic factors. However, its exact biological function is unknown. Proteins usually function in conjunction with other proteins in the system and thus, identification and analysis of protein networks become essential to decode protein functions. Objective: This study was performed to explore possible role(s) of HE4 in reproductive physiology via identification of its interactome in human seminal plasma. Methods: HE4 binding proteins were identified through co-immunoprecipitation and MALDITOF/ MS analysis. Also, HE4 was quantified by ELISA in fertile and infertile human seminal plasma samples. Results: Ten HE4 binding proteins were identified, viz. protein phosphatase 1 regulatory subunit 21, protein kinase CLK3, Ankyrin repeat domain-containing protein36A, prostatic acid phosphatase, KIF5C, Spectrin repeat containing, nuclear envelope 1, isoform CRAf, tropomyosin 4, vezatin, utrophin and fibronectin1. This interaction network suggests that HE4 plays multiple roles, specifically in capacitation, sperm motility and maturation. Further, HE4 concentration in human seminal plasma samples was determined by Elisa. Higher HE4 expression in normozoospermia compared to azoospermia and asthenozoospermia affirms its importance in fertilization. Conclusion: Based on identified interactome, it is plausible that HE4 plays a crucial role in fertilization, specifically in sperm maturation, motility and capacitation.

scholarly journals Heparin-binding proteins of canine seminal plasma

2006 ◽  
Vol 66 (6-7) ◽  
pp. 1606-1609 ◽  
Author(s):  
Fabiana Ferreira de Souza ◽  
Maria Isabel Mello Martins ◽  
Carlos Eurico dos Santos Fernandes ◽  
Paulo Eduardo Martins Ribolla ◽  
Maria Denise Lopes
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Heparin Binding

Zinc- and copper-binding proteins in the plasma of winter flounder (Pseudopleuronectes americanus)

1980 ◽  
Vol 58 (4) ◽  
pp. 609-613 ◽  
Author(s):  
P. E. Fletcher ◽  
G. L. Fletcher
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Egg Yolk ◽  
Winter Flounder ◽  
Zinc Binding ◽  
Copper Binding ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins were isolated from the plasma of winter flounder using gel filtration chromatography. A single copper-binding protein fraction of molecular weight 170 000 was isolated from the plasma of both sexes.In male and female flounder over 95% of the plasma zinc was associated with a zinc-binding protein(s) with a molecular weight of 76 000. In male flounder the remaining zinc appeared to be bound to a protein(s) of molecular weight 186 000. In female flounder the remaining 5% of the zinc was associated with two zinc-binding fractions with apparent molecular weights of 186 000 and 340 000 – 370 000.Extracts of plasma vitellogenin and egg yolk proteins revealed significant quantities of zinc and copper. It is hypothesized that the female specific zinc-binding protein (340 000 – 370 000) was vitellogenin.

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