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Seminal Plasma Proteins

About: Seminal Plasma Proteins is a research topic. Over the lifetime, 535 publications have been published within this topic receiving 17843 citations.


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TL;DR: The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vESicle protein may serve as the physiological substrate for the protease.
Abstract: A 33-kD glycoprotein, known as the "prostate-specific antigen," was purified to homogeneity from human seminal plasma. The prostatic protein was identified as a serine protease, and its NH2-terminal sequence strongly suggests that it belongs to the family of glandular kallikreins. The structural protein of human seminal coagulum, the predominant protein in seminal vesicle secretion, was rapidly cleaved by the prostatic enzyme, which suggests that this seminal vesicle protein may serve as the physiological substrate for the protease. The prostatic enzyme hydrolyzed arginine- and lysine-containing substrates with a distinct preference for the former. All synthetic substrates tested were poor substrates for the enzyme. Synthetic Factor XIa substrate (pyro-glutamyl-prolyl-arginine-p-nitroanilide), and the synthetic kallikrein substrate (H-D-prolyl-phenylalanyl-arginine-p-nitroanilide) were hydrolyzed with maximum specific activities at 23 degrees C of 79 and 34 nmol/min per mg and Km values of 1.0 and 0.45 mM, respectively. Synthetic substrates for plasmin, chymotrypsin, and elastase were either not hydrolyzed by the enzyme at all, or only hydrolyzed very slowly.

773 citations

Journal ArticleDOI
TL;DR: Comparisons of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronECTin and the lactofermin in human seminal fluid originate from the seminalVesicles and the ampullae.
Abstract: The comparison of measurements of fibronectin and lactoferrin in ejaculates from vasectomized men, subjects with functional deficiency or aplasia of the seminal vesicles, and reference subjects provided evidence that both the fibronectin and the lactoferrin in human seminal fluid originate from the seminal vesicles and the ampullae. The fibronectin is incorporated in the framework of the seminal gel formed during the immediate postejaculatory phase, whereas the lactoferrin remains in solution. In the seminal gel fibronectin is linked to its predominant structural protein, a high molecular weight seminal vesicle protein (semenogelin). Both the gel-bound fibronectin and semenogelin are progressively fragmented and solubilized by the abundant prostatic kallikrein-like protease (prostate-specific antigen) during and after seminal gel liquefaction. Lactoferrin remains essentially unaffected by the seminal proteases.

368 citations

Journal ArticleDOI
TL;DR: Bull seminal plasma contains fertility-associated proteins that are predictive of bull fertility, according to a regression model developed to predict bull fertility using the four fertility- associated protein densities.
Abstract: This study was undertaken to determine whether bovine seminal plasma contained protein markers associated with bull fertility, and whether these markers were of value in predicting bull fertility. Seminal plasma was obtained from 35 Holstein bulls of known fertility. Two-dimensional PAGE of seminal plasma samples indicated that two proteins (26 kDa, pI 6.2; 55 kDa, pI 4.5) predominated in higher-fertility bulls, and two proteins (16 kDa, pI 4.1; 16 kDa, pI 6.7) predominated in lower-fertility bulls. Densitometry data for these proteins in individual samples were combined for bulls grouped by fertility level. Average density of the 26-kDa protein was significantly greater in seminal plasma of high-fertility bulls, and high-fertility seminal plasma also contained more of the 55-kDa protein than that of average- and below average-fertility bulls. Below average- and low-fertility bull seminal plasma had significantly more of both 16-kDa proteins than that of average- and high-fertility bulls. A regression model was developed to predict bull fertility using the four fertility-associated protein densities. A plot of actual bull fertility versus that calculated by this model was linear and positively correlated (r = 0.89). These findings indicate that bull seminal plasma contains fertility-associated proteins that are predictive of bull fertility.

367 citations

Journal ArticleDOI
TL;DR: A novel proteomic method that uses whole-organism isotopic labeling to detect transferred Sfps in mated female D. melanogaster and identifies 63 proteins, which were previously unknown to function in reproduction, and confirmed the transfer of dozens of predicted Sfps.
Abstract: Across diverse taxa, seminal fluid proteins (Sfps) transferred at mating affect the reproductive success of both sexes. Such reproductive proteins often evolve under positive selection between species; because of this rapid divergence, Sfps are hypothesized to play a role in speciation by contributing to reproductive isolation between populations. In Drosophila, individual Sfps have been characterized and are known to alter male sperm competitive ability and female post-mating behavior, but a proteomic-scale view of the transferred Sfps has been missing. Here we describe a novel proteomic method that uses whole-organism isotopic labeling to detect transferred Sfps in mated female D. melanogaster. We identified 63 proteins, which were previously unknown to function in reproduction, and confirmed the transfer of dozens of predicted Sfps. Relative quantification of protein abundance revealed that several of these novel Sfps are abundant in seminal fluid. Positive selection and tandem gene duplication are the prevailing forces of Sfp evolution, and comparative proteomics with additional species revealed lineage-specific changes in seminal fluid content. We also report a proteomic-based gene discovery method that uncovered 19 previously unannotated genes in D. melanogaster. Our results demonstrate an experimental method to identify transferred proteins in any system that is amenable to isotopic labeling, and they underscore the power of combining proteomic and evolutionary analyses to shed light on the complex process of Drosophila reproduction.

324 citations

Journal ArticleDOI
TL;DR: Citation Rodríguez‐Martínez H, Kvist U, Ernerudh J, Sanz L, Calvete JJ: Seminal Plasma Proteins: What Role Do They Play?
Abstract: Problem Semen is a heterogenous and complex cell suspension in a protein-rich fluid with different functions, some of them well known, others still obscure. Method of study This paper reviews, comparatively, our current knowledge on the growing field of proteomics of the SP and its relevance in relation to the in vivo situation, for the sake of reproductive biology, diagnostics and treatment. Results Ejaculated spermatozoa, primarily bathing in cauda epididymal fluid, are (in vitro) bulky, exposed to most, if not all, secretions from the accessory sexual glands. In vivo, however, not all spermatozoa are necessarily exposed to all secretions from these glands, because sperm cohorts are delivered in differential order and bathe in seminal plasma (SP) with different concentrations of constituents, including peptides and proteins. Proteins are relevant for sperm function and relate to sperm interactions with the various environments along the female genital tract towards the oocyte vestments. Specific peptides and proteins act as signals for the female immune system to modulate sperm rejection or tolerance, perhaps even influencing the relative intrinsic fertility of the male and/or couple by attaining a status of maternal tolerance towards embryo and placental development. Conclusions Proteins of the seminal plasma have an ample panorama of action, and some appear responsible for establishing fertility.

319 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20222
202114
202019
201920
201814
201725