Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-10T15:14:26.042Z Has data issue: false hasContentIssue false
  • English
  • Français

Localisation of two classes of acetylcholine receptor-like molecules in sperms of different animal species

Published online by Cambridge University Press:  26 September 2008

B. Baccetti ,
A.G. Burrini ,
G. Collodel ,
C. Falugi ,
E. Moretti  and
P. Piomboni
B. Baccetti*
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
A.G. Burrini
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
G. Collodel
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
C. Falugi
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
E. Moretti
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
P. Piomboni
Affiliation:
Institute of General Biology, University of Siena and Centre for Study of Germinal Cells, CNR, and Institute of Comparative Anatomy, Genoa University, Italy.
*
B.Baccetti, Centre for the Study of Germinal Cells, CNR, via Tommaso Pendola 62, I-53100 Siena, Italy. Telephone: 0577-284173. Fax: 0577-263509.
Get access Rights & Permissions [Opens in a new window]

Summary

The distribution of different classes of acetylcholine (ACh) receptor-like molecules in sperms of different invertebrate and vertebrate species is described. ACh receptor molecules belong to one of two classes: muscarinic receptors (mAChRs), associated with signal transduction mechanisms in the inner domain of the cell, and nicotinic receptors (nAChRs), capable of opening Na+ channels when activated by the ligand. Molecules immunologically related to mAChRs and to ACh can be identified by specific antibodies, and revealed by immunofluorescent or immunogold staining; the nicotinic receptor-like molecules are localised as curare-sensitive affinity sites for α-bungarotoxin. In all species studied, both classes of receptors were found, with a similar distribution. Muscarinic-like molecules were found mainly in the sperm head regions of most species; such a localisation may be correlated to a function in sperm–egg interaction, for instance in the regulation of the block to polyspermy. Nicotinic-like molecules are present mainly in the tail and in the post-acrosomal region of most animals, thus confirming their function in the regulation of sperm propulsion, but are also present at the acrosomal region of most species. The distribution patterns of the different classes of molecules indicate that both may be in sperm–egg interactions, in addition to their known function in the regulation of sperm propulsion.

Keywords

AcetylcholineCytochemistryImmunocytochemistryMuscarinic receptorNicotinic receptorSperm
Type
Article
Information
Zygote , Volume 3 , Issue 3 , August 1995 , pp. 207 - 217
Copyright
Copyright © Cambridge University Press 1995

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Berridge, M.J., & Irvine, R.F. (1984). Inositol triphosphate, a novel second messenger in cellular signal transduction. Nature 312, 315–21.CrossRefGoogle Scholar
Birdsall, N.J.M., & Hulme, E.C. (1976). Biochemical studies on muscarinic acetylcholine receptors. J. Neurochem. 27, 7–16.Google Scholar
Bishop, M.R., Rama Sastry, B.V., & Stavinhoa, W.B. (1977). Identification of acetylcholine and propionylcholine in bull spermatozoa by integrated prolysis, gas chromatography and mass spectrometry. Biochim. Biophys. Acta 500, 440–4.CrossRefGoogle Scholar
Burznikov, G.A. (1990). Neurotransmitters in Embryogenesis, vol. 1. Series ed. Turpaev, T.M.. (Physiology and General Biology, section F of Soviet Scientific Reviews.) London: Harwood Academic Publications.Google Scholar
Coons, A.H., Leduc, E.H., & Connelly, J.M. (1955). Studies on antibody production. I. A method for histochemical demonstration of specific antibody and its application to a study of the hyperimmune rabbit. J. Exp. Med. 102, 49–59.CrossRefGoogle Scholar
Eusebi, F., Mangia, F., & Alfei, L. (1979). Acetylcholine-elicited responses in primary and secondary mammalian oocytes disappear after fertilization. Nature 277, 651–3.Google Scholar
Eusebi, F., Pasetto, N., & Siracusa, G. (1984). Acetylcholine receptors in human oocytes. J. Physiol. (Lond.) 346, 321–30.Google Scholar
Falugi, C. (1993). Localization and possible role of molecules associated with the cholinergic system during ‘non nervous’ developmental events. Eur. J. Histochem. 37, 287–94.Google Scholar
Falugi, C., Borgiani, G., Faraldi, G., Tafliafierro, G., Toso, F. & Drews, U. (1991). Localization and possible functions of neurotransmitter systems in sperms of different animal species. In Comparative Spermatology, 20 Years After, vol. 75, ed. Baccetti, B pp. 475–8. New York: Raven Press.Google Scholar
Falugi, C., Pieroni, M., Drews, U., Stengel, P., & Lammerding-Koppel, M. (1992). Possible functions of the ‘embryonic’ cholinergic system present in gametes at fertilization. In Echinoderm Research, ed. Liaci, L. Scalera & Canicatti, C.. pp. 161–4. Rotterdam: A.A. Balkema.Google Scholar
Falugi, C., Pieroni, M. & Moretti, E. (1993). Cholinergic molecules and sperm functions. J. Submicrosc. Cytol. Pathol. 25, 63–9.Google Scholar
Faraldi, G., Falugi, C., Mauceri, A. & Fasulo, S. (1995). Localization of signal molecules during amphibian ovogenesis. Anim. Biol., in press.Google Scholar
Florman, H.M., & Storey, B.T. (1982). Characterization of cholinomimetic agents that inhibit in vitro fertilization of the mouse: evidence for a sperm-specific binding site. J. Androl. 3, 157–64.Google Scholar
Fraser, L.R., & Monks, N.G. (1990). Cyclic nucleotides and mammalian sperm capacitation. J. Reprod. Fertil. 42 (Suppl), 9–21.Google Scholar
Harrison, R.A., & Roldan, R.S. (1990). Phosphoinositides and their products in the mammalian sperm acrosome reaction. J. Reprod. Fertil. 42 (Suppl.), 51–67.Google Scholar
Ibanez, C.F., Pelto-Huikko, M., Soder, O., Ritzen, E.M., Hersh, L.B., Hokfelt, T. & Persson, H. (1991). Expression of choline acetyltransferase mRNA in spermatogenic cells results in an accumulation of the enzyme in the postacrosomal region of mature spermatozoa. Proc. Natl. Acad. Sci. USA 88, 3676–80.Google Scholar
Jaffe, L.A. (1990). First messenger at fertilization. J. Reprod. Fertil. 42 (suppl), 107–16.Google ScholarPubMed
Kopf, G.S. (1990). Zona pellucida-mediated signal transduction in mammalian spermatozoa. J. Reprod. Fertil. 42 (Suppl.), 33–49.Google Scholar
Kusano, K. (1978). Comparative electrophysiological study on the oocyte membrane ‘neuro-receptors;’. Biol. Bull. 155, 450.Google Scholar
Minganti, A., Falugi, C., Raineri, M., Pestarino, M. (1981). Acetylcholinesterase in the embryonic development: an invitation to a hypothesis. Acta Embryol. Morphol. Exp., N S. 2, 30–1.Google Scholar
Nelson, L. (1978). Chemistry and neurochemistry of sperm motility control. Fed. Proc. 37, 2543–7.Google Scholar
Nelson, L. (1990). Pesticide perturbation of sperm cell function. Bull. Environ. Contam. Toxicol. 45, 876–82.Google Scholar
Nelson, L., McGrady, V., & Fangboner, M.E. (1970). Control of flagellar movement. In Comparative Spermatology, ed. Baccetti, B., pp. 465–78. Rome/New York: Accad. Naz. Lineci/Academic Press.Google Scholar
Ott, P., & Brodbeck, U. (1978). Multiple molecular forms of acetylcholinesterase from human erythrocyte membranes: interconversion and subunit composition of forms separated by density gradient centrifugation in a zonal rotor. Eur. J. Biochem. 88, 119–25.CrossRefGoogle Scholar
Ozaki, H. (1974). Localisation and multiple forms of acetylcholinesterase in sea urchin embryos. Dev. Growth Differ. 16, 245–57.Google Scholar
Sastry, B.V.R., Bishop, M.R., & Sen, T.K. (1979). Distribution of α-bungarotoxin-binding proteins in fractions from bull spermatozoa. Biochem. Pharmacol. 28, 1271–4.CrossRefGoogle ScholarPubMed
Schofield, P.R., Darlison, M.G., Fujita, N., Burt, D.R., Stepheson, F.A., Rodriguez, H., Rhee, L.M., Ramachandran, J., Reale, V., Glencorse, T.A., Seeburg, P.H. & Barnard, E.A. (1987). Sequence and functional expression of the GABA receptor shows a ligand-gated receptor super-family. Nature 328, 221–7.Google Scholar
Visconti, P.E., Moore, G.D., Bailey, J.L., Leclere, P., Connors, S.A., Pan, D., Olds-Clarke, P. & Kopf, G.S. (1995). Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by cAMP-dependent pathway. Development 121, 1139–50.Google Scholar
Williams, C.J., Schultz, R.M., & Kopf, G.S. (1992). Role of G proteins in mouse egg activation: stimulatory effects of acelylcholine on the ZP2 to ZP2f conversion and pro-nuclear formation in eggs expressing a functional ml muscarinic receptor. Dev. Biol. 151, 288–96.CrossRefGoogle Scholar
Young, R.J., & Laing, J.C. (1991). The binding characteristics of cholinergic sites in rabbit spermatozoa. Mol. Reprod. Dev. 28, 55–61.CrossRefGoogle ScholarPubMed