Zinc and magnesium in bull and boar spermatozoa

Arver, Stefan; Eliasson, R.

doi:10.1530/jrf.0.0600481

Cited by 21 publications

(11 citation statements)

References 10 publications

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“…Spermatozoa of the starfish (Asterias) and other invertebrates release considerable amounts of zinc when first activated by dilution in seawater (Fujii et al, 1955). Mammalian spermatozoa contain substantial amounts of zinc (Lindholmer and Eliasson, 1972;Arver and Eliasson, 1980;Srivastava et a1., 1983). Chelation of zinc by serum albumin could thus be a key event regulating capacitation (Johnsen and Eliasson, 1978a).…”

Section: 33bmentioning

confidence: 99%

Animal in Vitro Fertilization and Embryo Development

Bavister

1986

Manipulation of Mammalian Development

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Section: 33bmentioning

confidence: 99%

Animal in Vitro Fertilization and Embryo Development

Bavister

1986

Manipulation of Mammalian Development

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“…This was confirmed by the finding that a hypertonic salt solution was able to remove the in vitro-associated CRISP1 from the immature cells. Considering evidence suggesting that bovine and porcine sperm lose Zn 2þ when washed with saline solution [49], the release of the in vitro-and the in vivo-associated CRISP1 from sperm exposed to high ionic strength could be explained by the loss of Zn 2þ from the cells caused by the saline treatment. Interestingly, both the loosely bound population of CRISP1 [20] and Zn 2þ [50,51] are released from sperm during capacitation, opening the possibility that removal of CRISP1 during capacitation could also be a result of the loss of Zn 2þ described as one of the initial steps in the capacitation process [50].…”

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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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“…The seminal plasma contains abundant concentrations of different amino acids, peptides, lipids, fatty acids and various osmolytes, and it is an important source of cations [2]. In boar seminal plasma, for example, the concentration of Zn 2+ is surprisingly high (0.3–0.7 m m ) [3,4], reaching the spermatozoa at ejaculation [5]. Seminal plasma also contains a large number of different proteins that exert multiple effects on sperm function, including a diversity of enzymes, hormones, growth factors and transport proteins [6].…”

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confidence: 99%

Analysis of the stability of the spermadhesin PSP‐I/PSP‐II heterodimer

et al. 2005

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Proteins are designed to have a particular activity in a specific environment, and their fold and assembly are intimately related to this physiological function. Information on the organization of the protein structure, however, is usually acquired in simple buffer systems, far removed from the complex conditions encountered in intracellular and extracellular spaces and fluids. Besides the crucial influence of the local concentration of macromolecules, the presence of co-solutes may have a decisive effect on protein conformation and stability [1].Seminal plasma is a composite fluid, comprising secretions from the testes, epididymis and accessory sex glands. It is not merely a vehicle for the ejaculated sperm but it is also involved in numerous activities in the male and female reproductive tract, ensuring the viability and fertilizing capacity of spermatozoa. The seminal plasma contains abundant concentrations of different amino acids, peptides, lipids, fatty acids and various osmolytes, and it is an important source of cations [2]. In boar seminal plasma, for example, the concentration of Zn 2+ is surprisingly high

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Zinc and magnesium in bull and boar spermatozoa

Cited by 21 publications

References 10 publications

Animal in Vitro Fertilization and Embryo Development

Animal in Vitro Fertilization and Embryo Development

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

Analysis of the stability of the spermadhesin PSP‐I/PSP‐II heterodimer

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