Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa

Sara Rubinstein; Yehudit Lax; Yael Shalev; Haim Breitbart

doi:10.1016/0167-4889(95)00007-F

Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa

Sara Rubinstein, Yehudit Lax, Yael Shalev, Haim Breitbart

Department of Management

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The influence of spermine on the acrosomal exocytosis of capacitated bovine spermatozoa was studied. Dual effect of spermine was observed, depending on its concentration. It was shown that 10 μ,M spermine stimulated acrosomal exocytosis and prostaglandin F_2α production, whereas higher concentrations of spermine inhibited these processes. Acrosomal exocytosis induced by spermine was inhibited by staurosporine, a specific protein kinase C (PKC) inhibitor, indicating that PKC may be involved in this stimulation. Also, acrosomal exocytosis induced by the PKC activator phorbol 12-myristate- l3-acetate was inhibited by 10 mM spermine. Therefore, these data indicate that spermine is involved in signal transduction events leading to exocytosis. We suggest that the concentration-dependent reversal of the stimulatory action of spermine could be explained by the existence of two binding sites for spermine: high affinity sites involved in inducing acrosomal exocytosis by low spermine concentration and low affinity sites mediating inhibition of acrosomal exocytosis by high concentration of spermine.

Original language	English
Pages (from-to)	196-200
Number of pages	5
Journal	Biochimica et Biophysica Acta - Molecular Cell Research
Volume	1266
Issue number	2
DOIs	https://doi.org/10.1016/0167-4889(95)00007-F
State	Published - 1995

Bibliographical note

Funding Information:
This work was supported by a grant from the Ihel Foundation to H.B. We thank Avrille Goldreich for language editing and typing this manuscript.

Keywords

BAEE
EGF
PGF
PKA
PKC
PLC
PMA
STP
bezoylarginine ethyl ester
dbcAMP
dibutyryl cyclic AMP
epidermal growth factor
phorbol 12-myristate13-acetate
phospholipase C
prostaglandin F
protein kinase A
protein kinase C
staurosporin

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10.1016/0167-4889(95)00007-F

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title = "Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa",

abstract = "The influence of spermine on the acrosomal exocytosis of capacitated bovine spermatozoa was studied. Dual effect of spermine was observed, depending on its concentration. It was shown that 10 μ,M spermine stimulated acrosomal exocytosis and prostaglandin F2α production, whereas higher concentrations of spermine inhibited these processes. Acrosomal exocytosis induced by spermine was inhibited by staurosporine, a specific protein kinase C (PKC) inhibitor, indicating that PKC may be involved in this stimulation. Also, acrosomal exocytosis induced by the PKC activator phorbol 12-myristate- l3-acetate was inhibited by 10 mM spermine. Therefore, these data indicate that spermine is involved in signal transduction events leading to exocytosis. We suggest that the concentration-dependent reversal of the stimulatory action of spermine could be explained by the existence of two binding sites for spermine: high affinity sites involved in inducing acrosomal exocytosis by low spermine concentration and low affinity sites mediating inhibition of acrosomal exocytosis by high concentration of spermine.",

keywords = "BAEE, EGF, PGF, PKA, PKC, PLC, PMA, STP, bezoylarginine ethyl ester, dbcAMP, dibutyryl cyclic AMP, epidermal growth factor, phorbol 12-myristate13-acetate, phospholipase C, prostaglandin F, protein kinase A, protein kinase C, staurosporin",

author = "Sara Rubinstein and Yehudit Lax and Yael Shalev and Haim Breitbart",

note = "Funding Information: This work was supported by a grant from the Ihel Foundation to H.B. We thank Avrille Goldreich for language editing and typing this manuscript.",

year = "1995",

doi = "10.1016/0167-4889(95)00007-F",

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T1 - Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa

AU - Rubinstein, Sara

AU - Lax, Yehudit

AU - Shalev, Yael

AU - Breitbart, Haim

N1 - Funding Information: This work was supported by a grant from the Ihel Foundation to H.B. We thank Avrille Goldreich for language editing and typing this manuscript.

PY - 1995

Y1 - 1995

N2 - The influence of spermine on the acrosomal exocytosis of capacitated bovine spermatozoa was studied. Dual effect of spermine was observed, depending on its concentration. It was shown that 10 μ,M spermine stimulated acrosomal exocytosis and prostaglandin F2α production, whereas higher concentrations of spermine inhibited these processes. Acrosomal exocytosis induced by spermine was inhibited by staurosporine, a specific protein kinase C (PKC) inhibitor, indicating that PKC may be involved in this stimulation. Also, acrosomal exocytosis induced by the PKC activator phorbol 12-myristate- l3-acetate was inhibited by 10 mM spermine. Therefore, these data indicate that spermine is involved in signal transduction events leading to exocytosis. We suggest that the concentration-dependent reversal of the stimulatory action of spermine could be explained by the existence of two binding sites for spermine: high affinity sites involved in inducing acrosomal exocytosis by low spermine concentration and low affinity sites mediating inhibition of acrosomal exocytosis by high concentration of spermine.

AB - The influence of spermine on the acrosomal exocytosis of capacitated bovine spermatozoa was studied. Dual effect of spermine was observed, depending on its concentration. It was shown that 10 μ,M spermine stimulated acrosomal exocytosis and prostaglandin F2α production, whereas higher concentrations of spermine inhibited these processes. Acrosomal exocytosis induced by spermine was inhibited by staurosporine, a specific protein kinase C (PKC) inhibitor, indicating that PKC may be involved in this stimulation. Also, acrosomal exocytosis induced by the PKC activator phorbol 12-myristate- l3-acetate was inhibited by 10 mM spermine. Therefore, these data indicate that spermine is involved in signal transduction events leading to exocytosis. We suggest that the concentration-dependent reversal of the stimulatory action of spermine could be explained by the existence of two binding sites for spermine: high affinity sites involved in inducing acrosomal exocytosis by low spermine concentration and low affinity sites mediating inhibition of acrosomal exocytosis by high concentration of spermine.

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KW - dibutyryl cyclic AMP

KW - epidermal growth factor

KW - phorbol 12-myristate13-acetate

KW - phospholipase C

KW - prostaglandin F

KW - protein kinase A

KW - protein kinase C

KW - staurosporin

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JF - Biochimica et Biophysica Acta - Molecular Cell Research

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Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa

Abstract

Bibliographical note

Keywords

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