Extraction and quantification of acrosin, β-N-acetylglucosaminidase, and arylsulfatase-A from equine ejaculated spermatozoa

Journal of Experimental Zoology

Volumn 279, Issue 3, 1997, Pages 301-308

  Brandon Jr , C I ^a   Srivastava, P N ^a   Heusner, G L ^a   Fayrer Hosken, R A ^b  

^a UNIVERSITY OF GEORGIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUCOSAMINIDASE; ACROSIN; CEREBROSIDE SULFATASE;

ACROSOME; ANIMAL; ARTICLE; CELL MEMBRANE; COMPARATIVE STUDY; EJACULATION; ENZYMOLOGY; HORSE; KINETICS; MALE; METABOLISM; SPERMATOZOON; ULTRASTRUCTURE;

ACETYLGLUCOSAMINIDASE; ACROSIN; ACROSOME; ANIMALS; CELL MEMBRANE; CEREBROSIDE-SULFATASE; EJACULATION; HORSES; KINETICS; MALE; SPERMATOZOA;

ANIMALIA; EQUIDAE; EQUUS CABALLUS; MAMMALIA;

EID: 1842414818     PISSN: 0022104X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-010X(19971015)279:3<301::AID-JEZ11>3.0.CO;2-C     Document Type: Article

References (56)

1. Akruk, S.R., W.J. Humphreys, and W.L. Williams (1979) In vitro capacitation of ejaculated rabbit spermatozoa. Differentiation, 13:125-131.
2. Allison, A.C., and E.F. Hartree (1970) Lysosomal enzymes in the acrosome and their possible role in fertilization. J. Reprod. Fertil., 21:501-515.
3. Anderson, R.A., S.A. Beyler, S.R. Mack, and L.J.D. Zaneveld (1981) Characterization of a high molecular weight form of human acrosin. Biochem. J., 199:307-316.
4. Barros, C., J.M. Bedford, L.E. Franklin, C.R. Austin (1967) Membrane vesiculation as a feature of the mammalian acrosome reaction. J. Cell Biol., 34:C1-C5.
5. Bearpark, T.M., and J.L. Stirling (1978) A difference in the specificities of human liver N-acetyl-beta-hexosaminidases A and B detected by their activities towards glycosaminoglycan oligosaccharides. Biochem. J., 173:997-1000.
6. Bedford, J.M. (1983) Significance of the need for sperm capacitation before fertilization in eutherian mammals. Biol Reprod, 28:108-120.
7. Berutti, G. (1980) Multiple forms of boar, bull, and human acrosin. Arch. Androl., 5:267-277.
8. Berutti, G. (1981) Multiple forms of bovine acrosin: Purification and characterization. Comp. Biochem. Physiol., 69B: 323-328.
9. Bhattacharyya, A.K., and L.J.D. Zaneveld (1978) Release of acrosin inhibitor from human spermatozoa. Fertil. Steril., 30:70-78.
10. Bhattacharyya, A.K., and L.J.D. Zaneveld (1982) The sperm head. In: Biochemistry of Mammalian Reproduction. L.J.D. Zaneveld and R.T. Chatterton, eds. John Wiley & Sons, New York, pp. 119-152.
11. Braden, A.W.H. (1952) Structural characteristics of the mammalian zona pellucida. Aust. J. Sci. Res., 5:460-471.
12. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72:248-254.
13. Brown, C.R. (1982) Effects of ram sperm acrosin on the investments of sheep, pig, mouse and gerbil eggs. J. Reprod. Fertil., 64:457-462.
14. Dudkiewicz, A.B. (1984) Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. Biol. Reprod., 30:1005-1014.
15. Dunbar, B.S., N.J. Wardrip, and J.L. Hedrick (1980) Isolation, physiochemical properties, and macromolecular composition of zona pellucida from porcine oocytes. Biochem, 19:356-365.
16. Elce, J.S., and E.J. McIntyre (1982) Purification of bovine and human acrosin. Can. J. Biochem., 60:8-14.
17. Farooqui, A.A. (1976) Effect of neuraminidase on the multiple forms of arylulfatase B. Biochimie, 58:759-761.
18. Farooqui, A.A., and P.N. Srivastava (1979) Isolation, characterization and the role of rabbit testicular arylsulfatase A in fertilization. Biochem. J., 181:331-337.
19. Farooqui, A.A., and P.N. Srivastava (1980) Isolation of β-N-acetylhexosaminidase from rabbit semen and its role in fertilization. Biochem. J., 197:827-834.
20. Fluharty, A.L., R.L. Stevens, R.T. Miller, and H. Kihara (1974) Sulfoglycerogalactolipid from rat testis: A substrate for pure human arylsulfatase A. Biochem. Biophys. Res. Comm. 61:348-354.
21. Froman, D.P., R.P. Amann, R.M. Riek, and T.T. Olar (1984) Acrosin activity of canine spermatozoa as an index of cellular damage. J. Reprod. Fertil., 70:301-308.
22. Goodpasture, J.C., J.M. Reddy, and L.J.D. Zaneveld (1981) Acrosin, proacrosin and acrosin inhibitor of guinea pig spermatozoa capacitated and acrosome-reacted in vitro. Biol. Reprod., 25:44-55.
23. Graham, F.R.B., and A.B. Roy (1973) Sulphatase A as a glycoprotein. Biochem. Biophys. Acta, 329:88-92.
24. Guraya, R.B.L. (1974) Morphology, histochemistry, and biochemistry of human oogenesis and ovulation. Int. Rev. Cytol., 37:121-151.
25. Gwatkin, R.B. (1978) Cell-cell interaction in mammalian fertilization. Birth Defects, 14:363-376.
26. Hayashi, S. (1977) Study on the degradation of glycosaminoglycans by canine liver lysosomal enzymes I. J. Biochem. (Toyko), 82:1287-1295.
27. Hayashi, S. (1978) Study on the degradation of glycosaminoglycans by canine liver lysosmal enzymes II. J. Biochem. (Toyko), 83:149-157.
28. Ho, J.J.L., and S. Meizel (1975) Multiple molecular forms of avian acrosin: Differences in their kinetic properties. FEBS Letters, 56:115-119.
29. Jauhiainen, A., and T. Vanha-Perttula (1986) β-N-acetylglucosaminidase in the reproductive organs and seminal plasma of the bull. J. Reprod. Fertil., 76:239-250.
30. Miller, D.J., X. Gong, and B.D. Shur (1993) Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida. Development, 118:1279-1289.
31. Morton, D.B. (1977) Immunoenzymatic studies on acrosin and hyaluronidase in ram spermatozoa. In: Immunobiology of Gametes. M. Edidin and M.H. Johnson, eds. pp. 115-147.
32. Ninjoor, V., and P.N. Srivastava (1985) Partial purification and characterization of an alkaline proteinase from the rabbit testis. Gam/ Res., 11:69-82.
33. Peterson, R.N., L. Russell, D. Bundman, And M. Fruend (1980) Sperm-egg interaction: Evidence for boar sperm plasma membrane receptors for porcine zona pellucida. Science, 207:73-74.
34. Pickett, B.W., and D.G. Black (1973) Procedures for preparation, collection, evaluation, and insemination of stallion semen. Fort Collins, Colorado State University, #935.
35. Polakoski, K.L., L.J.D. Zaneveld, and W.L. Williams (1971) An acrosin-acrosin inhibitor complex in ejaculated boar sperm. Biochem. Biophys. Res. Commun., 45:381.
36. Robinson, D., and J.L. Stirling (1968) N-acetyl-β-glucosaminidase in human spleen. Biochem. J., 107:321-337.
37. Schill, W.B. (1973) Acrosin activity in human spermatozoa: Methodological investigations. Arch. Dermatol. Forsch., 248:257.
38. Schill, W.B. (1974) Quantitative determination of acrosin activity in human spermatozoa. Fertil. Steril., 25:703-712.
39. Srivastava, P.N. (1973) Removal of acrosomes of ram and rabbit spermatozoa. J. Reprod. Fert., 33:323-326.
40. Srivastava, S.K., Y.C. Awasthi, A. Yoshida, and E. Beutler (1974a) Studies in human β-D-N-acetylhexosaminidase I. Purification and properties. J. Biol. Chem., 249: 2043-2048.
41. Srivastava, P.N., J.F. Munnell, C.H. Yang, and C.W. Foley (1974b) Sequential release of acrosomal membranes and acrosomal enzymes of ram spermatozoa. J. Reprod. Fert., 36:363-372.
42. Srivastava P.N., S.R. Akruk, and W.L. Williams (1979) Dissolution of rabbit zona by sperm acrosomal extract: Effect of calcium. J. Exp. Zool., 207:521-529.
43. Srivastava, P.N., and V. Nonjoor (1982) Isolation of rabbit testicular cathepsin D and its role in the activation of proacrosin. Biochem. Biophys. Res. Comm., 109:63-69.
44. Stambaugh, R., and J. Buckley (1969) Identification and subcellular localization of the enzymes effecting penetration of the zona pellucida by rabbit spermatozoa. J. Reprod. Fertil. 19:423.
45. Stambaugh, R., and J. Buckley (1970) Comparative studies of the acrosomal enzymes of rabbit, rhesus monkey, and human spermatozoa. Biol. Reprod., 3:257.
46. Tallman, J.F., R.O. Brady, J.M. Quirk, M. Villalba, and A.E. Gal (1974) Isolation and relationship of human hexosaminidases. J. Biol. Chem., 249:3489-3499.
47. Varner, D.D., C.R. Ward, B.T. Storey, and R.M. Kenney (1987) Induction and characterization of acrosome reaction in equine spermatozoa. Am. J. Vet. Res., 48:1383-1389.
48. Yamato, K., S. Handa, and T. Yamakawa (1974) Purification of arylsulfatase A from boar testis and its activities toward seminolipid and sulfatide. J. Biochem., 75:1241-1247.
49. Yang, C.H., and P.N. Srivastava (1974) Purification and properties of arylsulfatases from rabbit sperm acrosomes. Proc. Soc. Exp. Biol. Meth., 145:721-725.
50. Yang, C.H., and P.N. Srivastava (1975a) Purification and properties of hyaluronidase from bull sperm. J. Biol. Chem., 250:79-83.
51. Yang, C.H., and P.N. Srivastava (1975b) Purification of bull sperm hyaluronidase by concanavalin A sepharose affinity chromatography. Biochem. Biophys. Acta, 391: 382-387.
52. Yang, C.H., and P.N. Srivastava (1976) Purification and properties of arylsulphatase A from rabbit testis. Biochem. J., 159:133-142
53. Zaneveld, L.J.D., P.N. Srivastava, and W.L. Williams (1969) Relationship of a trypsin-like enzyme in rabbit spermatozoa to capacitation. J. Reprod. Fertil., 20:337-339.
54. Zaneveld, L.J.D., R.T. Robertson, and W.L. Williams (1970) Synthetic enzyme inhibitors as antifertility agents. FEBS Letters, 1:345.
55. Zaneveld, L.J.D., R.M. Dragoje, and G.F.B. Schumacher (1972) Acrosomal proteinase and proteinase inhibitor of human spermatozoa. Science, 177:702.
56. Zaneveld, L.J.D., K.L. Polakoski, and W.L. Williams (1973) A proteinase and proteinase inhibitor of mammalian sperm acrosomes. Biol. Reprod., 9:219-225.