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

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.

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Sperm-associated seminal plasma proteins - a novel approach for the evaluation of sperm fertilizing ability of stallions?

Pferdeheilkunde Equine Medicine ◽

10.21836/pem19990608 ◽

1999 ◽

Vol 15 (6) ◽

pp. 531-537 ◽

Cited By ~ 2

Author(s):

A Reineke ◽

Heß,O ◽

A Schambony ◽

A M Petrounkina ◽

H Bader ◽

...

Keyword(s):

Seminal Plasma ◽

Plasma Proteins ◽

Novel Approach ◽

Fertilizing Ability ◽

Seminal Plasma Proteins ◽

Sperm Fertilizing Ability

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

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc20040616 ◽

2004 ◽

Vol 69 (3) ◽

pp. 616-630 ◽

Cited By ~ 2

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.

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

Reproduction Fertility and Development ◽

10.1071/rd09274 ◽

2010 ◽

Vol 22 (6) ◽

pp. 893 ◽

Cited By ~ 27

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.

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255 SEMINAL PLASMA PROTEINS: FUNCTIONAL ATTRIBUTES AND POTENTIAL MARKERS OF FERTILITY

Reproduction Fertility and Development ◽

10.1071/rdv28n2ab255 ◽

2016 ◽

Vol 28 (2) ◽

pp. 259

Author(s):

A. A. Moura

Keyword(s):

Seminal Plasma ◽

Plasma Proteins ◽

Seminal Fluid ◽

Technological Development ◽

Shotgun Proteomics ◽

Reproductive Technologies ◽

Early Embryo ◽

Domestic Species ◽

Functional Attributes ◽

Seminal Plasma Proteins

Mammalian seminal plasma is a complex milieu containing, mostly, secretions of the epididymides and accessory sex glands. After ejaculation, proteins of the seminal fluid interact with sperm and participate in several events, including sperm motility, protection against immune reactions, oxidative processes and microorganisms, interaction with the oviduct epithelium, capacitation, acrosome reaction, and fertilization. Given these aspects, the present talk is focused on seminal plasma proteins and cross-species comparisons of their functional attributes. Experiments that will be presented used gel-based and shotgun proteomics. Binder of sperm proteins are major components of ruminant seminal plasma, while spermadhesins are predominant in the boar and deer (Mazama gouazoubira; Mazama nemorivag) seminal fluid. Annexins (rabbits), clusterin (peccaries: Pecari tajacu), and arginine esterase (coatis: Nasua nasua; dogs) are the most abundant proteins in seminal fluid of other species. Such diversity may reflect differences in how paternal factors modulate fertility. Studies have also reported empirical associations between seminal proteins, sperm freezability, and fertility indexes in ruminants and other domestic species. As evidenced by experiments using IVF, mainly in the bovine, specific seminal proteins influence the fertilizing capacity of both epididymal and ejaculated sperm, as well as early embryo development. In summary, fundamental knowledge gathered by studies of seminal plasma proteome can be used to identify molecular markers of fertility. Availability of such markers will potentially improve the outcome of artificial reproductive technologies. Diversity of seminal plasma composition, however, represents challenges for discovery of fertility markers in unique species. Seminal plasma proteins may also be related to new phenotypes, such as bull differences in sperm survival after sexation. This research was funded in part by the Brazilian Research Councils (CAPES and CNPq) and Ceara State Foundation for Scientific and Technological Development (FUNCAP).

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

Journal of Chromatography A ◽

10.1016/0021-9673(95)00011-b ◽

1995 ◽

Vol 711 (1) ◽

pp. 167-173 ◽

Cited By ~ 24

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

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

Polish Journal of Veterinary Sciences ◽

10.2478/v10181-011-0074-z ◽

2011 ◽

Vol 14 (3) ◽

pp. 489-499 ◽

Cited By ~ 17

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.

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