Zinc‐protein from rat prostate fluid binds epididymal spermatozoa

Sansone, Giovanni; Abrescia, Paolo

doi:10.1002/jez.1402590313

Cited by 4 publications

(4 citation statements)

References 39 publications

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“…It has yet to be established whether zinc ions control this activity. Correlations between zinc concentrations and protein concentrations and ApA indicate the presence of zinc proteins in fish seminal plasma, as described in mammals ( Sansone & Abrescia 1991). Strong correlation of seminal plasma zinc concentration with ApA and protein concentration was also found in our earlier experiment in which the characteristics of semen obtained by stripping from 17 males were compared.…”

Section: Discussionmentioning

confidence: 70%

Characterization of rainbow trout milt collected with a catheter: semen parameters and cryopreservation success

Głogowski

Kwaśnik

Piros

et al. 2000

Aquaculture Research

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Collection of fish milt by stripping risks the danger of milt contamination by urine. This may seriously influence milt characteristics and quality, including usefulness for cryopreservation. Urine contamination of milt may be avoided by using a catheter for sperm collection. The objectives of this study were to provide basic characteristics of milt collected with a catheter, to test the usefulness of this milt for cryopreservation, and to correlate characteristics of fresh and cryopreserved semen with sperm fertility rates. Milt from 25 rainbow trout Oncorhynchus mykiss (Walbaum) males were used. All samples were cryopreserved using the pellet method within 1 h of collection, using 0.6 m sucrose and 10% dimethyl sulphoxide (DMSO) as an extender. Catheterization resulted in semen of very good motility (> 90% motile spermatozoa) and high fertilization rates after cryopreservation (mean fertilization rate 81.8 ± 13.3% of control, at a sperm/egg ratio of 2.4 ± 0.3 × 106). Osmolality of seminal plasma and concentrations of sodium, potassium and magnesium ions had low variability, which suggests that they are important for creating a stable environment for sperm storage in the sperm duct. Higher variability of certain seminal plasma characteristics, such as protein concentration and antiproteinase activity, suggests that these characteristics are related to individual semen features of particular males. A strong correlation of seminal plasma zinc concentration with protein concentration may reflect an importance of zinc in semen biology. Cryopreservation caused a significant release of protein and acid phosphatase from spermatozoa. Our results did not reveal any single characteristic of semen collected by catheter that could be used as a powerful predictor of cryopreservation success, presumably because all samples were of high quality.

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Section: Discussionmentioning

confidence: 70%

Characterization of rainbow trout milt collected with a catheter: semen parameters and cryopreservation success

Głogowski

Kwaśnik

Piros

et al. 2000

Aquaculture Research

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“…In this regard, evidence indicates the presence of high concentrations of Zn 2þ in the rat epididymis [28] that might be involved in sperm maturation [29], and crystallographic studies revealed the existence of Zn 2þ -binding sites in several snake venom CRISPs [30][31][32]. However, whereas it has been reported that Zn 2þ in seminal plasma can interact with the sperm surface either as a free ion or associated with proteins [33,34], little is known about the participation of Zn 2þ in the association of proteins with sperm within the epididymis.…”

Section: Introductionmentioning

confidence: 99%

Evidence for the Involvement of Zinc in the Association of CRISP1 with Rat Sperm During Epididymal Maturation

Maldera

Vasen

Ernesto

et al. 2011

Biology of Reproduction

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Rat epididymal protein CRISP1 (cysteine-rich secretory protein 1) associates with sperm during maturation and participates in fertilization. Evidence indicates the existence of two populations of CRISP1 in sperm: one loosely bound and released during capacitation, and one strongly bound that remains after this process. However, the mechanisms underlying CRISP1 binding to sperm remain mostly unknown. Considering the high concentrations of Zn(2+) present in the epididymis, we investigated the potential involvement of this cation in the association of CRISP1 with sperm. Caput sperm were coincubated with epididymal fluid in the presence or absence of Zn(2+), and binding of CRISP1 to sperm was examined by Western blot analysis. An increase in CRISP1 was detected in sperm exposed to Zn(2+), but not if the cation was added with ethylenediaminetetra-acetic acid (EDTA). The same results were obtained using purified CRISP1. Association of CRISP1 with sperm was dependent on epididymal fluid and Zn(2+) concentrations and incubation time. Treatment with NaCl (0.6 M) removed the in vitro-bound CRISP1, indicating that it corresponds to the loosely bound population. Flow cytometry of caput sperm exposed to biotinylated CRISP1/avidin-fluorescein isothiocyanate revealed that only the cells incubated with Zn(2+) exhibited an increase in fluorescence. When these sperm were examined by epifluorescence microscopy, a clear staining in the tail, accompanied by a weaker labeling in the head, was observed. Detection of changes in the tryptophan fluorescence emission spectra of CRISP1 when exposed to Zn(2+) supported a direct interaction between CRISP1 and Zn(2+). Incubation of either cauda epididymal fluid or purified CRISP1 with Zn(2+), followed by native-PAGE and Western blot analysis, revealed the presence of high-molecular-weight CRISP1 complexes not detected in fluids treated with EDTA. Altogether, these results support the involvement of CRISP1-Zn(2+) complexes in the association of the loosely bound population of CRISP1 with sperm during epididymal maturation.

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“…In contrast, seminal vesicle secretions that are known to participate in capacitation in mice [16][17][18] and bulls [19,20] are added to the cell surfaces after ejaculation by binding to sperm plasma membrane phospholipid head groups. In rats, there is evidence that seminal vesicle proteins are added to the sperm surface [21,22], possibly by transglutaminase activity in semen [23], and a prostate-derived protein binds to rat spermatozoa [24]. Thus, addition of proteins and glycoproteins derived from different parts of the duct to sperm surfaces occurs throughout the male excurrent duct system.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Capacitation-Associated Tyrosine Phosphorylation Signaling in Rat Sperm by Epididymal Protein Crisp-11

Roberts

Wamstad

Ensrud

et al. 2003

Biology of Reproduction

132

105

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Ejaculated sperm are unable to fertilize an egg until they undergo capacitation. Capacitation results in the acquisition of hyperactivated motility, changes in the properties of the plasma membrane, including changes in proteins and glycoproteins, and acquisition of the ability to undergo the acrosome reaction. In all mammalian species examined, capacitation requires removal of cholesterol from the plasma membrane and the presence of extracellular Ca2+ and HCO3-. We designed experiments to elucidate the conditions required for in vitro capacitation of rat spermatozoa and the effects of Crisp-1, an epididymal secretory protein, on capacitation. Protein tyrosine phosphorylation, a hallmark of capacitation in sperm of other species, occurs during 5 h of in vitro incubation, and this phosphorylation is dependent upon HCO3-, Ca2+, and the removal of cholesterol from the membrane. Crisp-1, which is added to the sperm surface in the epididymis in vivo, is lost during capacitation, and addition of exogenous Crisp-1 to the incubation medium inhibits tyrosine phosphorylation in a dose-dependent manner, thus inhibiting capacitation and ultimately the acrosome reaction. Inhibition of capacitation by Crisp-1 occurs upstream of the production of cAMP by the sperm.

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Zinc‐protein from rat prostate fluid binds epididymal spermatozoa

Cited by 4 publications

References 39 publications

Characterization of rainbow trout milt collected with a catheter: semen parameters and cryopreservation success

Characterization of rainbow trout milt collected with a catheter: semen parameters and cryopreservation success

Evidence for the Involvement of Zinc in the Association of CRISP1 with Rat Sperm During Epididymal Maturation

Inhibition of Capacitation-Associated Tyrosine Phosphorylation Signaling in Rat Sperm by Epididymal Protein Crisp-11

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