Characteristics of selected seminal plasma proteins and their application in the improvement of the reproductive processes in mammals

2011 ◽  
Vol 14 (3) ◽  
pp. 489-499 ◽  
Author(s):  
M. Mogielnicka-Brzozowska ◽  
W. Kordan
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Acrosome Reaction ◽  
Reproductive Tract ◽  
Chromatin Condensation ◽  
Female Reproductive Tract ◽  
Sperm Chromatin ◽  
Heparin Binding ◽  
Seminal Plasma Proteins ◽  
Reproductive Processes

Characteristics of selected seminal plasma proteins and their application in the improvement of the reproductive processes in mammals Understanding the biochemical processes associated with ovum fertilization and knowledge about the structure and function of individual substances participating in these processes is crucial for the development of biotechnological methods to improve reproduction of animals and humans. Among many components of seminal plasma, proteins and peptides play a specific role in regulation of the fertilization process, particularly through their ability to bind various types of ligands such as polysaccharides, lipids and ions. Heparin-binding proteins regulate capacitation and acrosome reaction processes. Affinity of plasma proteins to mannans of the fallopian tube epithelium facilitates formation of spermatozoa reservoirs in the female reproductive tract. Ability to bind phosphorylcholine is one of the conditions for the coating of the seminal plasma proteins on the sperm membrane and also determines the formation of oligomeric forms of certain proteins. Zinc binding by seminal plasma proteins regulates sperm chromatin condensation state. It also affects motility of these cells and acrosome reaction. The interspecies analysis indicates significant structural and functional similarities, especially for the proteins with low molecular weight. Fertility associated proteins (FAPs) have been determined in the bull, stallion, boar, ram and dog. The contents of these proteins correlate with the indicators of the fertilizing abilities of sperm. In humans, several seminal plasma proteins were found which serve as diagnostic markers of spermatogenesis, seminiferous epithelium state, and azoospermia. To determine the semen ability for preservation, measurement of some seminal plasma protein content may also be used. Addition of specific plasma proteins to a spermatozoa solution undergoing the process of preservation may be used to retain the features of the cells responsible for efficient fertilization.

scholarly journals Ram seminal plasma and its functional proteomic assessment

Reproduction ◽  
2019 ◽  
Vol 157 (6) ◽  
pp. R243-R256 ◽  
Author(s):  
T Leahy ◽  
J P Rickard ◽  
N C Bernecic ◽  
X Druart ◽  
S P de Graaf
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Reproductive Tract ◽  
Reproductive Technologies ◽  
Female Reproductive Tract ◽  
Sperm Function ◽  
Seminal Plasma Proteins ◽  
Ram Sperm

Ejaculation results in the confluence of epididymal spermatozoa with secretions of the accessory sex glands. This interaction is not a prerequisite for fertilisation success, but seminal factors do play a crucial role in prolonging the survival of spermatozoa bothin vitroandin vivoby affording protection from handling induced stress and some selective mechanisms of the female reproductive tract. Reproductive biologists have long sought to identify specific factors in seminal plasma that influence sperm function and fertility in these contexts. Many seminal plasma proteins have been identified as diagnostic predictors of sperm function and have been isolated and appliedin vitroto prevent sperm damage associated with the application of artificial reproductive technologies. Proteomic assessment of the spermatozoon, and its surroundings, has provided considerable advances towards these goals and allowed for greater understanding of their physiological function. In this review, the importance of seminal plasma will be examined through a proteomic lens to provide comprehensive analysis of the ram seminal proteome and detail the use of proteomic studies that correlate seminal plasma proteins with ram sperm function and preservation ability.

Seminal plasma proteins inhibit in vitro- and cooling-induced capacitation in boar spermatozoa

2010 ◽  
Vol 22 (6) ◽  
pp. 893 ◽  
Author(s):  
Melissa L. Vadnais ◽  
Kenneth P. Roberts
Keyword(s):  
Mass Spectrometry ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Acrosome Reaction ◽  
Heparin Binding ◽  
Total Proteins ◽  
Binding Properties ◽  
Seminal Plasma Proteins ◽  
Boar Spermatozoa

Dilute boar seminal plasma (SP) has been shown to inhibit in vitro capacitation and cooling-induced capacitation-like changes in boar spermatozoa, as assessed by the ability of the spermatozoa to undergo an ionophore-induced acrosome reaction. We hypothesised that the protein component of SP is responsible for this effect. To test this hypothesis, varying concentrations of total SP protein or SP proteins fractionated by heparin binding were assayed for their ability to inhibit in vitro capacitation, as well as cooling- and cryopreservation-induced capacitation-like changes. In vitro capacitation and cooling-induced capacitation-like changes were prevented by 10% whole SP, as well as by total proteins extracted from SP at concentrations greater than 500 μg mL−1. No amount of SP protein was able to prevent cryopreservation-induced capacitation-like changes. Total SP proteins were fractionated based on their heparin-binding properties and the heparin-binding fraction was shown to possess capacitation inhibitory activity at concentrations as low as 250 µg mL−1. The proteins in the heparin-binding fraction were subjected to mass spectrometry and identified. The predominant proteins were three members of the spermadhesin families, namely AQN-3, AQN-1 and AWN, and SP protein pB1. We conclude that one or more of these heparin-binding SP proteins is able to inhibit in vitro capacitation and cooling-induced capacitation-like changes, but not cryopreservation-induced capacitation-like changes, in boar spermatozoa.

scholarly journals Heparin- and Zn2+-binding proteins from boar seminal plasma.

1999 ◽  
Vol 46 (4) ◽  
pp. 935-939 ◽  
Author(s):  
D Hołody ◽  
J Strzezek
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Molecular Mass ◽  
Seminal Plasma ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
Heparin Binding ◽  
Sds Page ◽  
Protein Components

Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn2+-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn2+-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn2+-ions were classified as spermadhesins. Three fractions binding exclusively Zn2+ were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.

scholarly journals The importance of bovine seminal plasma proteins in the sperm function and fertility

SPERMOVA ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 83-95
Author(s):  
María Alejandra Cardozo ◽  
◽  
Jaime Antonio Cardozo ◽  
Fabian Rueda
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Acrosome Reaction ◽  
Protein Identification ◽  
Seminal Plasma Proteins ◽  
Biotechnological Processes ◽  
And Oxidative Stress ◽  
Social Sectors ◽  
Sperm Functions

Bovine livestock is one of the most important economic and social sectors for many countries. In this sense, the development of strategies to improve reproductive bull fertility and reproduction rates is relevant. It's highlighted the role of seminal plasma proteins (SPP) in reproductive fertility, so it has found close relationships among studies on the structure and biological activity of SPP, with seminal quality, including viability, sperm motility, and morphology. In addition, they have been found to regulate sperm functions such as capacitation, acrosome reaction, and they are even related to protecting sperm against thermal and oxidative stress. Moreover, the methods of separation and protein identification and their contribution to characterizing the bovine SP proteome should be also highlighted. In this sense, the most recent studies have been directed towards developing supplements with SPP that improve quality sperm subjected to cryopreservation processes. Research has begun and should forward to establish how the networks or sets of proteins are related to the functioning and fertility of sperm, the search for biomarkers of fertility, and the use of proteins in biotechnological processes, to increase efficiency reproductive.

Aggregated Forms of Bull Seminal Plasma Proteins and Their Heparin-Binding Activity

2004 ◽  
Vol 69 (3) ◽  
pp. 616-630 ◽  
Author(s):  
Petra Jelínková ◽  
Helena Ryšlavá ◽  
Jiří Liberda ◽  
Věra Jonáková ◽  
Marie Tichá
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Sodium Dodecyl ◽  
Reversed Phase ◽  
Binding Activity ◽  
Size Exclusion ◽  
Heparin Binding ◽  
Aggregation State ◽  
Seminal Plasma Proteins

Heparin-binding activity of bull seminal plasma proteins was shown to be dependent on their aggregation state. The protein fraction interacting with immobilized heparin was characterized by large polydispersity in the region of molecular weight of 60 000-10 000, while that not retained on the affinity carrier was present as aggregates with molecular weight >100 000. Components of heparin-binding and non-heparin-binding fractions were separated by RP HPLC (reversed-phase HPLC) and analyzed by SDS (sodium dodecyl sulfate) electrophoresis and N-terminal sequencing. Size exclusion chromatography of whole seminal plasma and heparin-binding proteins in the presence of D-fructose (as a component of seminal plasma) showed that the region of molecular weights of protein-associated forms was shifted to lower values. An increase of heparin-binding activity of bull proteins, as determined by ELBA (Enzyme-Linked Binding Assay), correlates with a decrease of their aggregation state. The modulation of the aggregation state of bull proteins by seminal plasma components and, in this way, also of their heparin-binding properties suggests possible mechanisms for capacitation mediated by these proteins.

Effect of glycosylation on the heparin-binding capability of boar and stallion seminal plasma proteins

1995 ◽  
Vol 711 (1) ◽  
pp. 167-173 ◽  
Author(s):  
Juan J. Calvete ◽  
Markus Reinert ◽  
Libia Sanz ◽  
Edda Töpfer-Petersen
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Heparin Binding ◽  
Seminal Plasma Proteins ◽  
Binding Capability

Functional attributes of seminal proteins in bull fertility: A systematic review

Reproduction ◽  
2021 ◽  
Author(s):  
Arabela Guedes de Azevedo Viana ◽  
Iara Magalhães Ribeiro ◽  
Renner Philipe Rodrigues Carvalho ◽  
Erdogan Memili ◽  
Arlindo Alencar Moura ◽  
...  
Keyword(s):  
Systematic Review ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Protein Isoforms ◽  
Heparin Binding ◽  
Protein Biomarkers ◽  
Functional Attributes ◽  
Fertilizing Ability ◽  
Seminal Plasma Proteins ◽  
Sperm Fertilizing Ability

Proteomic approaches have been widely used in reproductive studies to uncover protein biomarkers of bull fertility. Seminal plasma is one of the most relevant sources of these proteins that may influence sperm physiology. Nonetheless, there are still gaps in existing knowledge in the functional attributes of seminal proteins. Thus, we reviewed the relationships between seminal plasma proteins and bull fertility by conducting a systematic review with data obtained from 71 studies. This review showed that the associations between fertility improvement with the use of total seminal plasma proteins are still controversial. None of the studies explored the sperm fertilizing ability following these interactions. By contrast, the exposure to a single protein, such as osteopontin, binder of sperm proteins, and heparin binding proteins, can increment sperm motility, capacitation, and fertilizing ability by modulating intracellular calcium concentrations, removing lipids from sperm membranes, and regulating the acrosome reaction. Variations in protein analyses and the protein contents and their abundances between animals contributed to the difficulty of establishing protein biomarkers of fertilizing potential of the bull sperm. Indeed, the heterogenicity of methodologies was a limitation of this review. Standardized methods of seminal protein analyses, as well as sperm endpoints, may minimize such discrepancies. In conclusion, potential biomarkers of sperm parameters are still to be established. Future studies should evaluate protein isoforms and how they interact with sperm to ascertain their biological functions.

Genetic Polymorphism of Boar Seminal Plasma Proteins

1993 ◽  
Vol 64 (3) ◽  
pp. 221-227
Author(s):  
Soichi TSUJI ◽  
Masatoshi ASAO ◽  
Hiroshi KUSUNOKI ◽  
Takao OISHI
Keyword(s):  
Genetic Polymorphism ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Seminal Plasma Proteins
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