Capacitation of Mammalian Spermatozoa

Barros, C.

doi:10.1007/978-1-4684-2892-6_1

Cited by 86 publications

(33 citation statements)

References 55 publications

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“…In some experiments, Minimal Capacitation Medium (MCM) was used. The composition of this medium was: 102-9 mM-NaCl, 1 -7 mM-CaCl2, 25 mM-NaHC03, 20 mM-sodium lactate, and 0-25 mM-sodium pyruvate (Barros, 1974). Osmolality of this medium was about 302 mosmol/kg and the pH 7-9-8-2.…”

Section: ¡)mentioning

confidence: 97%

Is a Ca2+ -ATPase involved in Ca2+ regulation during capacitation and the acrosome reaction of guinea-pig spermatozoa?

Roldán

Fleming²

1989

Reproduction

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Summary. The Ca2+-ATPase antagonists quercetin and ethacrynic acid accelerated the onset of the acrosome reaction in guinea-pig spermatozoa incubated in the continuous presence of Ca2+, whereas furosemide had no effect, and sodium orthovanadate only affected sperm motility. When spermatozoa were preincubated in a 'Ca2+ -free' medium, quercetin and ethacrynic acid shortened capacitation time: spermatozoa incubated for 1 h in 100\p=n-\200 \g=m\M-ethacrynic acid showed 60\p=n-\80%acrosome reactions when Ca2+ was added. Such spermatozoa were able to fertilize zona-free hamster eggs. Our results therefore point to the possible involvement of a Ca2+-ATP in the regulation of intracellular Ca2+ in spermatozoa. Cysteine and dithiothreitol, both disulphide reducing agents, prevented the effects of quercetin and ethacrynic acid, suggesting that sulphydryl groups may be important for the expression of Ca2+-ATPase activity. Lysophosphatidylserine (LS) also prevented the stimulatory effect of ethacrynic acid, an effect similar to that shown by LS on lysophosphatidylcholine (LC). It is argued that both LS and LC could exert their action through an effect on the Ca2 +-ATPase.

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Section: ¡)mentioning

confidence: 97%

Is a Ca2+ -ATPase involved in Ca2+ regulation during capacitation and the acrosome reaction of guinea-pig spermatozoa?

Roldán

Fleming²

1989

Reproduction

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“…One of these events is spermatozoon capacitation, which encompasses a number of modifi cations that take place as sperm travel along the female reproductive tract and that involve a number of structural and biochemical changes in the spermatozoon (Barros, 1974;Go and Wolf, 1985;Hyne et al, 1985;Llanos, 1989;Fraser, 1995). These changes include an increase in plasma membrane fl uidity, a decrease in the level of plasma cholesterol content (Go and Wolf, 1985;Cross, 1998), an increase in intracellular concentrations of calcium and cAMP (Yanagimachi and Usui, 1974; Yanagimachi, 1982; Visconti Visconti et al, 1995;Visconti and Kopf, 1998), phosphorylation of tyrosine residues in proteins (Visconti et al, 1995;Leclerc et al, 1996), and a shift in the patterns of spermatozoon movement and motility (Yanagimachi, 1970).…”

Section: Capacitationmentioning

confidence: 99%

Modulation of spermatozoon acrosome reaction

Vigil¹,

Orellana²,

Cortés³

2011

Biol. Res.

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Spermatozoon acrosome reaction is an exocytotic event of the utmost importance for the development of mammalian fertilisation. Current evidence shows that the triggering of the acrosome reaction (AR) could be regulated by the action of diverse compounds, namely, metabolites, neurotransmitters and hormones. The aim of the present review is to describe the modulating effects of several compounds that have been classifi ed as inductors or inhibitors of acrosome reaction. Among AR inductors, it is necessary to mention progesterone, angiotensin II, atrial natriuretic peptide, cathecolamines, insulin, leptin, relaxin and other hormones. Regarding the inhibitors, oestradiol and epidermal growth factor are among the substances that retard AR. It is worth mentioning that gamma-aminobutyric acid, a neurotransmitter known to be an inhibitor in the central nervous system, has been shown to induce AR. The multiple hormones located in the fl uids of the female reproductive tract are also likely to act as subtle regulators of AR, constituting a fundamental aspect for the development of successful fertilisation. Finally, it is necessary to emphasise that the study of regulation exerted by hormones and other compounds on AR is essential for further understanding of mammalian reproductive biology, especially spermatozoon physiology.

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“…A modified Krebs-Ringer-bicarbonate (m-KRB) solution (Toyoda, Yokoyama & Hoshi, 1971) was changed by altering the pH from 7-4 to 8-0 (Aonuma, Okabe & Kawai, 1976) The fusion of spermatozoa to zona-free ova has been studied in mice (Pavlok & McLaren, 1972;Wolf, Inoue & Stark, 1976) and many other mammals (Yanagimachi, 1978), and the results indicate that plasma membrane in the post-equatorial segment is important for fusion. A change of membrane fluidity in the postnuclear cap region during capacitation has also been reported (Barros & Franklin, 1968;Barros, 1974;Barros & Berrios, 1977;Barros & Herrera, 1977;Yanagimachi, 1978). It is therefore likely that Zn2+ inhibits the membrane change in this region.…”

Section: Materials and General Methodsmentioning

confidence: 65%

Zinc effects on mouse spermatozoa and in-vitro fertilization

Aonuma¹,

Okabe²,

Kikuchi³

et al. 1981

Reproduction

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Summary. The fertilizing ability of mouse epididymal and capacitated spermatozoa was tested by mixing with normal or zona-free ova. In the presence of Zn2+, the epididymal spermatozoa failed not only to penetrate the zona pellucida but also to fuse with zone-free ova, while no effect was observed on capacitated spermatozoa.Zn2+ also inhibited fertilization with spermatozoa preincubated in Ca2+-free medium. However, shortly after the addition of Ca2+ to the preincubated spermatozoa, Zn2+ lost its fertilization inhibitory activity.

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Capacitation of Mammalian Spermatozoa

Cited by 86 publications

References 55 publications

Is a Ca2+ -ATPase involved in Ca2+ regulation during capacitation and the acrosome reaction of guinea-pig spermatozoa?

Is a Ca2+ -ATPase involved in Ca2+ regulation during capacitation and the acrosome reaction of guinea-pig spermatozoa?

Modulation of spermatozoon acrosome reaction

Zinc effects on mouse spermatozoa and in-vitro fertilization

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