Abstract
Mammalian sperm gain the ability to fertilize an egg successfully by the capacitation process. An unregulated capacitation process causes sperm to undergo a spontaneous acrosome reaction (AR) and resulting in loss of their fertilization activity. Thus, functional sperm activation is tightly regulated by a capacitation and suppression (decapacitation) mechanism. Factors, such as platelet-activating factor (PAF) present in both sperm and the female genital tract, are able to stimulate sperm capacitation. Seminal plasma is thought to have the ability to suppress sperm capacitation; however, the regulatory mechanisms of seminal plasma protein on sperm capacitation are not well understood. Recently, we demonstrated that seminal vesicle autoantigen (SVA), a major seminal vesicle secretory protein, is able to suppress mouse sperm capacitation. To further study the suppression spectra of SVA on sperm capacitation, we investigated the effect of SVA on PAF-induced mouse sperm capacitation-related signals. Here, we demonstrate that SVA decreases the [Ca2+], to suppress the PAF's effects on [Ca2+] i, the cAMP level, protein tyrosine phosphorylation, and capacitation. The inhibition of PAF-induced protein tyrosine phosphorylation and capacitation by SVA can be reversed by cAMP agonists. Characterization of the interactions of SVA with PAF by TLC overlay and tryptophan fluorescence spectrum analyses indicates that SVA is capable of binding PAF with an apparent dissociation constant Kd>50 μM. Together with these results, we demonstrate that SVA deceases [Ca2+], and cross-talks with PAF-induced intracellular signals to regulate mouse sperm capacitation.
| Original language | English |
|---|---|
| Pages (from-to) | 941-951 |
| Number of pages | 11 |
| Journal | Journal of Cellular Biochemistry |
| Volume | 100 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - Mar 1 2007 |
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Keywords
- Capacitation
- Seminal plasma protein
- Sperm
ASJC Scopus subject areas
- Biochemistry
- Cell Biology
Cite this
Suppression effect of seminal vesicle autoantigen on platelet-activating factor-induced mouse sperm capacitation. / Huang, Yen Hua; Chen, Yee Hsiung; Lin, Chun Mao; Ciou, Yi Yun; Kuo, Shin Peih; Chen, Chien Tsu; Shih, Chwen Ming; Chang, E-E.
In: Journal of Cellular Biochemistry, Vol. 100, No. 4, 01.03.2007, p. 941-951.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Suppression effect of seminal vesicle autoantigen on platelet-activating factor-induced mouse sperm capacitation
AU - Huang, Yen Hua
AU - Chen, Yee Hsiung
AU - Lin, Chun Mao
AU - Ciou, Yi Yun
AU - Kuo, Shin Peih
AU - Chen, Chien Tsu
AU - Shih, Chwen Ming
AU - Chang, E-E
PY - 2007/3/1
Y1 - 2007/3/1
N2 - Mammalian sperm gain the ability to fertilize an egg successfully by the capacitation process. An unregulated capacitation process causes sperm to undergo a spontaneous acrosome reaction (AR) and resulting in loss of their fertilization activity. Thus, functional sperm activation is tightly regulated by a capacitation and suppression (decapacitation) mechanism. Factors, such as platelet-activating factor (PAF) present in both sperm and the female genital tract, are able to stimulate sperm capacitation. Seminal plasma is thought to have the ability to suppress sperm capacitation; however, the regulatory mechanisms of seminal plasma protein on sperm capacitation are not well understood. Recently, we demonstrated that seminal vesicle autoantigen (SVA), a major seminal vesicle secretory protein, is able to suppress mouse sperm capacitation. To further study the suppression spectra of SVA on sperm capacitation, we investigated the effect of SVA on PAF-induced mouse sperm capacitation-related signals. Here, we demonstrate that SVA decreases the [Ca2+], to suppress the PAF's effects on [Ca2+] i, the cAMP level, protein tyrosine phosphorylation, and capacitation. The inhibition of PAF-induced protein tyrosine phosphorylation and capacitation by SVA can be reversed by cAMP agonists. Characterization of the interactions of SVA with PAF by TLC overlay and tryptophan fluorescence spectrum analyses indicates that SVA is capable of binding PAF with an apparent dissociation constant Kd>50 μM. Together with these results, we demonstrate that SVA deceases [Ca2+], and cross-talks with PAF-induced intracellular signals to regulate mouse sperm capacitation.
AB - Mammalian sperm gain the ability to fertilize an egg successfully by the capacitation process. An unregulated capacitation process causes sperm to undergo a spontaneous acrosome reaction (AR) and resulting in loss of their fertilization activity. Thus, functional sperm activation is tightly regulated by a capacitation and suppression (decapacitation) mechanism. Factors, such as platelet-activating factor (PAF) present in both sperm and the female genital tract, are able to stimulate sperm capacitation. Seminal plasma is thought to have the ability to suppress sperm capacitation; however, the regulatory mechanisms of seminal plasma protein on sperm capacitation are not well understood. Recently, we demonstrated that seminal vesicle autoantigen (SVA), a major seminal vesicle secretory protein, is able to suppress mouse sperm capacitation. To further study the suppression spectra of SVA on sperm capacitation, we investigated the effect of SVA on PAF-induced mouse sperm capacitation-related signals. Here, we demonstrate that SVA decreases the [Ca2+], to suppress the PAF's effects on [Ca2+] i, the cAMP level, protein tyrosine phosphorylation, and capacitation. The inhibition of PAF-induced protein tyrosine phosphorylation and capacitation by SVA can be reversed by cAMP agonists. Characterization of the interactions of SVA with PAF by TLC overlay and tryptophan fluorescence spectrum analyses indicates that SVA is capable of binding PAF with an apparent dissociation constant Kd>50 μM. Together with these results, we demonstrate that SVA deceases [Ca2+], and cross-talks with PAF-induced intracellular signals to regulate mouse sperm capacitation.
KW - Capacitation
KW - Seminal plasma protein
KW - Sperm
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U2 - 10.1002/jcb.21050
DO - 10.1002/jcb.21050
M3 - Article
VL - 100
SP - 941
EP - 951
JO - Journal of Cellular Biochemistry
JF - Journal of Cellular Biochemistry
SN - 0730-2312
IS - 4
ER -