Trypsin/acrosin inhibitor activity of rat and guinea pig caltrin proteins. Structural and functional studies

Biology of Reproduction

Volumn 63, Issue 1, 2000, Pages 42-48

  Winnica, Daniel E ^a   Novella, Maria L ^a   Dematteis, Andrea ^a   Coronel, Carlos E ^a,b  

^a UNIVERSIDAD NACIONAL DE CÓRDOBA   (Argentina)

^b FACULTAD DE CIENCIAS MÉDICAS   (Argentina)

Author keywords

Calcium; Male reproductive tract; Seminal vesicles; Sperm capacitation acrosome reaction

Indexed keywords

ACROSIN; TRYPSIN;

ACROSOME; ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; ENZYME INHIBITION; FERTILIZATION; GUINEA PIG; NONHUMAN; PRIORITY JOURNAL; SEMINAL VESICLE; SWINE;

ANIMALIA; BOVINAE; CAVIA PORCELLUS; MAMMALIA; SUS SCROFA;

EID: 0033919067     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod63.1.42     Document Type: Article

References (46)

1. Tschesche H, Kupfer S, Klauser R, Fink E, Fritz H. Structure, biochemistry and comparative aspects of mammalian seminal plasma acrosin inhibitors. Protides Biol Fluids 1976; 23:255-266.
2. Poirier GR, Jackson J. Isolation and characterization of two proteinase inhibitors from the male reproductive tract of mice. Gamete Res 1981; 4:555-569.
3. Mills JS, Needham M, Parker MG. A secretory protease inhibitor requires androgens for its expression in male sex accessory tissues but is expressed constitutively in pancreas. EMBO J 1987; 6:3711-3717.
4. Jonáková V, Cechová D, Meloun B, Veselesky L. An acrosin inhibitor from boar seminal vesicle fluid immunologically related to the trypsinkallikrein inhibitor (kunitz). Biol Chem Hoppe-Seyler 1988; 369:43-49.
5. Pillai MC, Meizel S. Trypsin inhibitors prevent the progesterone-initiated increase in intracellular calcium required for the human sperm acrosome reaction. J Exp Zool 1991; 258:384-393.
6. Brucker C, Lipford GB. The human sperm acrosome reaction: physiology and regulatory mechanisms. An update. Hum Reprod Update 1995; 1:51-62.
7. Saling PM. Involvement of trypsin-like activity in binding of mouse spermatozoa to zonae pellucidae. Proc Natl Acad Sci U S A 1981; 78:6231-6235.
8. Liu DY, Baker G. Inhibition of acrosin activity with a trypsin inhibitor blocks human sperm penetration of the zona pellucida. Biol Reprod 1993; 48:340-348.
9. Llanos M, Vigil P, Salgado MA, Morales P. Inhibition of the acrosome reaction by trypsin inhibitors and prevention of penetration of spermatozoa through the human zona pellucida. J Reprod Fertil 1993; 97: 173-178.
10. Mendoza C, Moos J, Tesarik J. Progesterone action on the human sperm surface is potentiated by an egg-associated acrosin activator. FEBS Lett 1993; 326:149-152.
11. Okamura N, Onoe S, Kawakura K, Tajima Y, Sugita Y. Effects of membrane-bound trypsin-like proteinase and seminal proteinase inhibitors on the bicarbonate-sensitive adenylate cyclase in porcine sperm plasma membranes. Biochem Biophys Acta 1990; 1035:83-89.
12. Rufo GA Jr, Singh JP, Babcock DF, Lardy HA. Purification and characterization of calcium transport inhibitor protein from bovine seminal plasma. J Biol Chem 1982; 257:4627-4632.
13. Lewis RV, San Agustin J, Kruggel W, Lardy HA. The structure of caltrin, the calcium-transport inhibitor of bovine seminal plasma. Proc Natl Acad Sci U S A 1985; 82:6490-6491.
14. San Agustin J, Hughes P, Lardy HA. Properties and function of caltrin, the calcium transport-inhibitor of bull seminal plasma. FASEB J 1987; 1:60-66.
15. San Agustin J, Lardy HA. Bovine seminal plasma constituents modulate the activity of caltrin, the calcium-transport regulating protein of bovine spermatozoa. J Biol Chem 1990; 265:6860-6867.
16. Lardy HA, San Agustin J, CoroneL C. Caltrin: a versatile regulator of calcium transport in spermatozoa. In: Kleinkauf H, von Döhren H, Jaenicke L (eds.), The Roots of Modern Biochemistry. New York: Walter de Gruyter and Co.; 1988; 759-763.
17. Coronel CE, San Agustin J, Lardy HA. Purification and structure of caltrin-like proteins from seminal vesicle of the guinea pig. J Biol Chem 1990; 265:6854-6859.
18. Coronel CE, Winnica DE, Novella ML, Lardy HA. Purification, structure and characterization of caltrin proteins from seminal vesicle of the rat and mouse. J Biol Chem 1992; 267:20909-20915.
19. Coronel CE, Novella ML, Winnica DE, Lardy HA. Purification and parcial sequence of a 15 kDa caltrin protein from rat seminal vesicle. In: Program of the 8th International Symposium on Spermatology; 1998; Montreal, Canada. Abstract P3-06.
20. Chen LY, Lin YH, Lai ML, Chen YH. Developmental profile of a caltrin-like protease inhibitor, P12, in mouse seminal vesicle and characterization of its binding sites on sperm surface. Biol Reprod 1998; 59:1498-1505.
21. Coronel CE, Lardy HA. Functional properties of caltrin proteins from seminal vesicle of the guinea pig. Mol Reprod Dev 1992; 33:74-80.
22. Lai ML, Chen SW, Chen YH. Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion. Arch Biochem Biophys 1991; 290:265-271.
23. Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate/polyacrylamide gel electrophoresis for the separation of protein in the range from 1 to 100 kDa. Anal Biochem 1987; 116:368-379.
24. Schwert GW, Takenaka Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochem Biophys Acta 1955; 16:570-575.
25. Coronel CE, San Agustin J, Lardy HA. Identification and partial characterization of caltrin-like proteins in the reproductive tract of the guinea pig. Biol Reprod 1988; 38:713-722.
26. Ey PL, Prowse SJ, Jenkin CR. Isolation of pure IgG1, IgG2a, IgG2b immunoglobulins from mouse serum using protein A-Sepharose. Biochemistry 1978; 15:429-436.
27. Irwing M, Nicholson N, Haywood JT, Poirier GR. Immunofluorescence of a murine seminal vesicle proteinase inhibitor. Biol Reprod 1983; 28:1201-1206.
28. Laemmli UK. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 1970; 277:680-685.
29. Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 1979; 76:4350-4354.
30. Allen G. Sequencing of proteins and peptides. In: Burdon RH, van Knippenberg PH (eds.), Laboratory Techniques in Biochemistry and Molecular Biology, vol. 9. Amsterdam: Elsevier; 1989; 55-59.
31. Hewick RM, Hunkapiller MW, Hood LE, Dreyer WJ. A gas-liquid solid phase peptide and protein sequenator. J Biol Chem 1981; 256: 7990-7997.
32. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchoninic acid. Anal Biochem 1985; 150:76-85.
33. Coronel CE, Maldonado C, Aoki A, Lardy HA. Electron microscopic imrnunolocalization of caltrin proteins in guinea pig seminal vesicles. Arch Androl 1995; 35:233-246.
34. Uda K, Ogawa M, Shibata T, Murata A, Mori T, Kikuchi N, Yoshida N, Tsusanawa S, Sakayima F. Purification, characterization and amino acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice. Biol Chem Hoppe-Seyler 1988; 369(suppl):55-61.
35. Kido H, Yokogoshi Y, Katunuma R. A low-molecular-mass Kazaltype protease inhibitor isolated from rat hepatocytes is identical to rat pancreatic secretory trypsin inhibitor II. Eur J Biochem 1990; 188: 501-506.
36. Fink E, Hehlein-Fink C, Eulitz M. Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to β-subunits of glycoprotein hormones. FEBS Lett 1990; 270:222-224.
37. Guy O, Shapanka R, Greene LJ. The structure of bovine pancreatic secretory trypsin inhibitor-Kazal's inhibitor. J Biol Chem 1971; 246: 7740-7747.
38. Adham IM, Nayernia K, Engel W. Spermatozoa lacking acrosin protein show delayed fertilization. Mol Reprod Dev 1997; 46:370-376.
39. Jansen S, Jones R, Jenneckens I, Marschall B, Kreigesmann B, Coadwell J, Brenig B. Site-directed mutagenesis of boar proacrosin reveals residues involved in binding of zona pellucida glycoproteins. Mol Reprod Dev 1998; 51:184-192.
40. Fraser LR. p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction. J Reprod Fertil 1982; 65:185-194.
41. Ponce RH, Dematteis MA, Novella ML, Winnica DE, Coronel CE. Rat caltrin inhibits acrosin activity and induces sperm-oocyte recognition. In: Bat-Sheva Seminar on Physiological and Molecular Processes Leading to Fertilization in Mammals; 1997; Zichron-Ya'cov, Israel. Page 55.
42. Dematteis A, Cohen DJ, Novella ML, Coronel CE, Cuasnicu PS. Effect of caltrin (calcium transport inhibitor) protein on rat fertilization. In: Program of the 8th International Symposium on Spermalology; 1998; Montreal, Canada. Abstract P3-18.
43. De Ioannes AE, Becker MI, Pérez C, Capote C, Barros C. Role of acrosin and antibodies to acrosin in gamete interactions. In: Alexander N, Griffin D, Spieler J, Waites G (eds.), Gamete Interactions: Prospect for Immuno Contraception. New York: Wiley-Liss; 1990; 185-195.
44. Crosby JA, Jones R, Barros C, Carvallo P. Characterization of the functional domains of boar acrosin involved in nonenzymatic binding to homologous zona pellucida glycoproteins. Mol Reprod Dev 1998; 49:426-434.
45. Coronel CE, Novella ML, Winnica DE, Lardy HA. Trypsin inhibitor activity of caltrin, the calcium transport inhibitor protein from seminal vesicle secretion. Biol Reprod 1995; 52 (suppl 1):16.
46. Novella ML, Maldonado C, Aoki A, Coronel CE. Androgen-dependent synthesis/secretion of caltrin, calcium transport inhibitor protein of mammalian seminal vesicle. Arch Androl 1999; 43:1-12.