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Seminal vesicle secretory protein 7, PATE4, is not required for sperm function but for copulatory plug formation to ensure fecundity†.

ABSTRACT: Seminal vesicle secretions (SVSs), together with spermatozoa, are ejaculated into the female reproductive tract. SVS7, also known as PATE4, is one of the major SVS proteins found in the seminal vesicle, copulatory plug, and uterine fluid after copulation. Here, we generated Pate4 knockout (-/-) mice and examined the detailed function of PATE4 on male fecundity. The morphology and weight of Pate4-/- seminal vesicles were comparable to the control. Although Pate4-/- cauda epididymal spermatozoa have no overt defects during in vitro fertilization, Pate4-/- males were subfertile. We found that the copulatory plugs were smaller in the vagina of females mated with Pate4-/- males, leading to semen leakage and a decreased sperm count in the uterus. When the females mated with Pate4-/- males were immediately re-caged with Pate4+/+ males, the females had subsequent productive matings. When the cauda epididymal spermatozoa were injected into the uterus and plugged artificially [artificial insemination (AI)], Pate4-/- spermatozoa could efficiently fertilize eggs as compared to wild-type spermatozoa. We finally examined the effect of SVSs on AI, and observed no difference in fertilization rates between Pate4+/+ and Pate4-/- SVSs. In conclusion, PATE4 is a novel factor in forming the copulatory plug that inhibits sequential matings and maintains spermatozoa in the uterus to ensure male fecundity.

SUBMITTER: Noda T

PROVIDER: S-EPMC6483057 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Seminal vesicle secretory protein 7, PATE4, is not required for sperm function but for copulatory plug formation to ensure fecundity†.

Noda Taichi T Fujihara Yoshitaka Y Matsumura Takafumi T Oura Seiya S Kobayashi Sumire S Ikawa Masahito M

Biology of reproduction 20190401 4

Seminal vesicle secretions (SVSs), together with spermatozoa, are ejaculated into the female reproductive tract. SVS7, also known as PATE4, is one of the major SVS proteins found in the seminal vesicle, copulatory plug, and uterine fluid after copulation. Here, we generated Pate4 knockout (-/-) mice and examined the detailed function of PATE4 on male fecundity. The morphology and weight of Pate4-/- seminal vesicles were comparable to the control. Although Pate4-/- cauda epididymal spermatozoa ha ...[more]

PMID: 30452524

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Project description:Seminal vesicle autoantigen (SVA) is a 19 kDa glycoprotein purified from mouse seminal vesicle secretion. It was quantified to be 0.9% (w/v) in the seminal vesicle fluid. We examined its distribution in the accessory sexual gland, characterized its binding sites on the sperm surface and assessed its effect on sperm motility. It was immunolocalized on the epithelium of the primary and secondary folds in the tissue. Mouse spermatozoa collected from caudal epididymis were devoid of SVA. A cytochemical study illustrated the presence of SVA-binding region on the entire cells. The cytochemical staining intensity for the binding of SVA to spermatozoa remained even when the cells were pretreated with protease digestion, acid or heat at 100 degrees C for 10 min. Moreover, the SVA-sperm binding could be inhibited by the dispersed sperm lipid. The specificity of interaction between (125)I-SVA and phospholipids was studied by TLC overlay techniques. The radiolabelled protein showed strong binding to purified phosphatidylcholine and phosphatidylserine and weak binding to purified sphingomyelin, lysophosphatidylcholine and phosphatidylethanolamine, but did not interact with phosphatidic acid, lysophosphatidic acid or phosphatidylinositol. Among the lipids extracted from spermatozoa, SVA showed strong binding to phosphatidylcholine and weak binding to sphingomyelin and neutral lipids. The assay for SVA-sperm binding with (125)I-SVA determined the IC(50) as being (3.89+/-0.65)x10(-5) M(-1), which is compatible with an apparent dissociation constant of (9.10+/-0.02)x10(-5) M(-1) estimated by fitting the data of phosphatidylcholine-perturbed SVA fluorescence to a modified Scatchard plot. SVA showed an ability to suppress sperm motility. The average path velocity, straight-line velocity and curvilinear velocity of sperm were not detectable by computer-assisted sperm assay after incubation of the cells in the presence of 0.3% SVA at 37 degrees C for more than 40 min.

Dataset Information

Seminal vesicle secretory protein 7, PATE4, is not required for sperm function but for copulatory plug formation to ensure fecundity†.

Publications

Seminal vesicle secretory protein 7, PATE4, is not required for sperm function but for copulatory plug formation to ensure fecundity†.

Similar Datasets

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