Biochemical and Immunological Characterization of the Acrosome Reaction-Inducing Substance (ARIS) of HFF

Miska, W.; Fehl, P.; Henkel, Ralf

doi:10.1006/bbrc.1994.1203

Cited by 30 publications

(22 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…a, different from control (no treatment), P < 0.01; b, different from ZP, P < 0.01. it is 1.3 mg/ml (Yuan et al, 1998). The effective concentration in the cumulus matrix (surrounding the oocyte) may be even higher because steroid-binding globulin contained in the matrix increases acrosomal exocytosis induced by progesterone (Miska et al, 1994). Thus, our observation that progesterone may trigger exocytosis in guinea pig spermatozoa at physiological concentrations underscores the significance of this agonist during fertilization.…”

Section: Discussionmentioning

confidence: 56%

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

Shi¹,

Chen²,

Yao³

et al. 2005

Journal Cellular Physiology

View full text Add to dashboard Cite

We investigated, using guinea-pig spermatozoa as a model, whether phospholipase A2 (PLA2) is involved in progesterone or zona pellucida (ZP)-stimulated acrosomal exocytosis, if progesterone enhances ZP-induced activation of PLA2, and mechanisms underlying PLA2 regulation. Spermatozoa were capacitated and labeled in low Ca2+ medium with [14C]choline chloride or [14C]arachidonic acid, washed, and then exposed to millimolar Ca2+ and progesterone and/or ZP. Each agonist stimulated decrease of phosphatidylcholine (PC) and release of arachidonic acid and lysoPC, indicative of PLA2 activation. Aristolochic acid (a PLA2 inhibitor) abrogated lipid changes and exocytosis, indicating that these lipid changes are essential for exocytosis. Exposure of spermatozoa to submaximal concentrations of both progesterone and ZP resulted in a synergistic increase of arachidonic acid and lysoPC releases, and exocytosis, suggesting that, under natural conditions, both agonists interact to bring about acrosomal exocytosis. Progesterone-induced PLA2 activation appears to be mediated by a GABA(A)-like receptor, because bicuculline (a GABA(A) receptor antagonist) blocked arachidonic acid release and exocytosis. In agreement with this, GABA mimicked progesterone actions. ZP-induced activation of PLA2 seemed to be transduced via G(i) proteins because pertussis toxin blocked arachidonic acid release and acrosomal exocytosis. PLA2 may be regulated by PKC because progesterone- or ZP-induced release of arachidonic acid was blocked by the PKC inhibitors staurosporine or chelerythrine chloride. PLA2 could also be regulated by the cAMP-PKA pathway; inclusion of the PKA inhibitor 14-22 amide or H-89 led to a reduction in arachidonic acid release or exocytosis after progesterone or ZP. Taken together, these results suggest that PLA2 plays an essential role in progesterone or ZP-stimulated exocytosis with progesterone priming ZP action.

show abstract

Section: Discussionmentioning

confidence: 56%

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

Shi¹,

Chen²,

Yao³

et al. 2005

Journal Cellular Physiology

View full text Add to dashboard Cite

show abstract

“…A number of other, non-physiological agonists can elicit the acrosomal exocytosis in spermatozoa, e.g. corticosteroidbinding protein [47], Epidermal Growth Factor [48] and immunoglobulins [49].…”

Section: Non-specific Induction Of Acrosomal Exocytosismentioning

confidence: 99%

The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro

Chapman

Kessopoulou

Andrews

et al. 1998

Biochemical Journal

View full text Add to dashboard Cite

Human gamete interaction is of fundamental biological importance, yet the molecular interactions between spermatozoa and the zona pellucida are poorly understood. Surprisingly, the role of the polypeptide backbone of zona pellucida glycoprotein 3 (ZP3), the putative ligand for spermatozoa activation, has been largely overlooked. Purified recombinant human ZP3 was expressed in Escherichia coli as a C-terminal fusion to the dimeric glutathione S-transferase (GST) from Schistosoma japonicum and was shown to induce acrosomal exocytosis in live, capacitated human spermatozoa. The level of exocytosis is comparable with that obtained using purified, glycosylated, recombinant human ZP3 [van Duin, M., Polman, J. E. M., DeBreet, I. T. M., Van Ginneken, K., Bunschoten, H., Grootenhuis, A., Brindle, J. and Aitken, R. J. (1994). Biol Reprod. 51, 607-617]. These data imply that the polypeptide chain of human ZP3 contributes to recognition of spermatozoa during acrosomal exocytosis in vitro.

show abstract

“…Second, there is no indication that a high concentration of progesterone (up to 1 mM) affects cell viability [48]. Third, spermatozoa may, after all, be acutely exposed to a high concentration of progesterone on the cell surface [49]. In a parallel experiment, spermatozoa were subjected to similar treatments and were subsequently examined for occurrence of exocytosis.…”

Section: Resultsmentioning

confidence: 99%

Bicarbonate/CO₂ induces rapid activation of phospholipase A₂ and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone

Roldán

Vázquez

1996

FEBS Letters

View full text Add to dashboard Cite

We tested whether capacitation, a phenomenon that renders spermatozoa capable of undergoing acrosomal exocytosis, may be completed rapidly after a short exposure to bicarbonatelCO2. We found that, in the presence of Ca 2+, a 10-min exposure of boar spermatozoa to bicarbonate led to a partial activation of phospholipase A2, primed spermatozoa for a major subsequent activation of this enzyme upon stimulation with progesterone and furthermore rendered spermatozoa capable of undergoing exocytosis in response to this steroid. These results suggest that capacitation may be completed in a relatively short period of time and open up new possibilities for unravelling molecular mechanisms underlying this process.

show abstract

Biochemical and Immunological Characterization of the Acrosome Reaction-Inducing Substance (ARIS) of HFF

Cited by 30 publications

References 0 publications

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro

Bicarbonate/CO₂ induces rapid activation of phospholipase A₂ and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone

Contact Info

Product

Resources

About

Biochemical and Immunological Characterization of the Acrosome Reaction-Inducing Substance (ARIS) of HFF

Cited by 30 publications

References 0 publications

Progesterone primes zona pellucida‐induced activation of phospholipase A2 during acrosomal exocytosis in guinea pig spermatozoa

Progesterone primes zona pellucida‐induced activation of phospholipase A2 during acrosomal exocytosis in guinea pig spermatozoa

The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro

Bicarbonate/CO2 induces rapid activation of phospholipase A2 and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone

Contact Info

Product

Resources

About

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

Progesterone primes zona pellucida‐induced activation of phospholipase A₂ during acrosomal exocytosis in guinea pig spermatozoa

Bicarbonate/CO₂ induces rapid activation of phospholipase A₂ and renders boar spermatozoa capable of undergoing acrosomal exocytosis in response to progesterone