Induction of the acrosome reaction in black tiger shrimp (Penaeus monodon) requires sperm trypsin-like enzyme activity

Biology of Reproduction

Volumn 79, Issue 1, 2008, Pages 134-141

  Kruevaisayawan, Hathairat ^a   Vanichviriyakit, Rapeepun ^a   Weerachatyanukul, Wattana ^a   Lamsaard, Sitthichai ^a   Withyachumnarnkul, Boonsirm ^a   Basak, Ajoy ^b,c   Tanphaichitr, Nongnuj ^b,c   Sobhon, Prasert ^a  

^a Mahidol University   (Thailand)

^b OTTAWA HOSPITAL RESEARCH INSTITUTE   (Canada)

^c UNIVERSITY OF OTTAWA   (Canada)

Author keywords

Acrosome reaction; Egg water; Fertilization; Gamete biology; P. monodon; Sperm; Trypsin

Indexed keywords

CHYMOTRYPSIN; SOYBEAN TRYPSIN INHIBITOR; TRYPSIN INHIBITOR; TRYPTASE;

ACROSOME REACTION; ANIMAL CELL; ARTICLE; CELL SURFACE; CONTROLLED STUDY; DEPOLYMERIZATION; ENZYME ACTIVITY; EXOCYTOSIS; FERTILIZATION; NONHUMAN; PRIORITY JOURNAL; SHRIMP; SPERMATOZOON;

ACROSOME REACTION; ANIMALS; FEMALE; MALE; MODELS, BIOLOGICAL; OVUM; PENAEIDAE; PEPTIDE HYDROLASES; PROTEASE INHIBITORS; TRYPSIN;

DECAPODA (CRUSTACEA); GLYCINE MAX; PENAEUS MONODON;

EID: 46449133212     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.107.066316     Document Type: Article

References (40)

1. Clark WH Jr, Yudin AI, Griffin FJ, Shigekawa K. The control of gamete activation and fertilization in the marine penaeidae, Sicyonia ingentis. In: Engels W (ed.). Advances in Invertebrate Reproduction, 3rd ed. Amsterdam: Elsevier Science Publishers; 1984:459-472.
2. Alfaro J, Munoz N, Vargas M, Komen J. Induction of sperm activation in open and closed thelycum penaeoid shrimps. Aquaculture 2003; 216:371-381.
3. Vanichviriyakit R, Kruevaisayawan H, Weerachatyanukul W, Tawipreeda P, Withyachumnarnkul B, Pratoomchat B, Chavadej J, Sobhon P. Molecular modification of Penaeus monodon sperm in female thelyeum and its consequent responses. Mol Reprod Dev 2004; 69:356-363.
4. Kleve MG, Yudin AI, Clark WH Jr. Fine structure of the unistellate sperm of the shrimp, Sicyonia ingentis (Natantia). Tissue Cell 1980; 12:29-45.
5. Clark WH Jr, Kleve MG, Yudin AI. An acrosome reaction in natantian sperm. J Exp Zool 1981; 218:279-291.
6. Griffin FJ, Shigekawa K, Clark WH Jr. Formation and structure of the acrosomal filament in the sperm of Sicyonia ingentis. J Exp Zool 1988; 246:94-102.
7. Griffin FJ. Clark WH Jr. Induction of acrosomal filament formation in the sperm of Sicyonia ingentis. J Exp Zool 1990; 254:296-304.
8. Clark WH Jr, Griffin FJ. Acquisition and manipulation of penaeoidean gametes. In: McVew J (ed.), Handbook of Techniques for Crustacean Aquaculture, vol. 1, 2nd ed. Boca Raton: CRC Press; 1993:133-152.
9. Pongtippatee-Taweepreda P, Chavadaj J, Plodpai P, Pratoomchart B, Sobhon P, Weerachatyanukul W, Withyachumnarnkul B. Egg activation in the black tiger shrimp Penaeus monodon. Aquaculture 2004; 234:183-198.
10. Griffin FJ, Clark WH Jr, Crowe JH, Crowe LM. Intracellular pH decreases during the in vitro induction of the acrosome reaction in the sperm of Sicyonia ingentis. Biol Bull 1987; 173:311-323.
11. Dan JC. Studies on the acrosome. I. Reaction to egg-water and other stimuli. Biol Bull 1952; 103:54-66.
12. Afzelius BA, Murray A. The acrosomal reaction of spermatozoa during fertilization or treatment with egg water. Exp Cell Res 1957; 12:325-337.
13. Cherr GN, Clark WH Jr. An egg envelope component induces the acrosome reaction in sturgeon sperm. J Exp Zool 1985; 234:75-85.
14. Lindsay LL, Clark WH Jr. Protease-induced formation of the sperm acrosomal filament. Develop Growth Differ 1992; 34:189-197.
15. Levine AE, Walsh KA. Involvement of an acrosin-like enzyme in the acrosome reaction of sea urchin sperm. Dev Biol 1979; 72:126-137.
16. Sawada H. Ascidian sperm lysin system. Zoolog Sci 2002; 19:139-151.
17. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-254.
18. Lynn JW, Clark WH Jr. Physiological and biochemical investigations of the egg jelly release in Penaeus aztecus. Biol Bull 1987; 173:451-460.
19. Zimmerman M, Ashe B, Yurewicz EC, Patel G. Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates. Anal Biochem 1977; 78:47-51.
20. Yasothornsrikul S, Hook VY. Detection of proteolytic activity by fluorescent zymogram in-gel assays. Biotechniques 2000; 28:1166-1168,1170,1172- 1163.
21. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
22. Clark WH Jr, Griffin FJ. The morphology and physiology of the acrosome reaction in the sperm of the decapod, Sicyonia ingentis. Develop Growth Differ 1988; 30:451-462.
23. Morales P, Socias T, Cortez J, Llanos MN. Evidences for the presence of chymotrypsin-like activity in human spermatozoa with a role in the acrosome reaction. Mol Reprod Dev 1994; 38:222-230.
24. Collins F, Epel D. The role of calcium ions in the acrosome reaction of sea urchin sperm: regulation of exocytosis. Exp Cell Res 1977; 106:211-222.
25. Lewis CA, Talbot CF, Vacquier VD. A protein from abalone sperm dissolves the egg vitelline layer by a nonenzymatic mechanism. Dev Biol 1982; 92:227-239.
26. Yamagata K, Murayama K. Okabe M, Toshimori K, Nakanishi T, Kashiwabara S, Baba T. Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J Biol Chem 1998; 273: 10470-10474.
27. Honda A, Yamagata K, Sugiura S, Watanabe K, Baba T. A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J Biol Chem 2002; 277:16976-16984.
28. Matsumura K, Aketa K. Proteasome (multicatalytic proteinase) of sea urchin sperm and its possible participation in the acrosome reaction. Mol Reprod Dev 1991; 29:189-199.
29. Yokota Y, Sawada H. Sperm proteasomes are responsible for the acrosome reaction and sperm penetration of the vitelline envelope during fertilization of the sea urchin Pseudocentrotus depressus. Dev Biol 2007; 308:222-231.
30. Pasten C, Morale P, Kong M. Role of sperm proteasome during fertilization and gamete interaction in the mouse. Mol Reprod Dev 2005; 71:209-219.
31. Sutovsky P, Manandhar G, McCauley TC, Caamaño JN, Sutovsky M, Thompson WE, Day BN. Proteasomal interference prevents zona pellucida penetration and fertilization in mammals. Biol Reprod 2004; 71:1625-1637.
32. Carrard G, Bulteau AL, Petropoulos I, Friguet B. Impairment of proteasome structure and function in aging. Int J Biochem Cell Biol 2002; 34:1461-1474.
33. Heinemeyer W, Fischer M, Krimmer T, Stachon U, Wolf DH. The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing. J Biol Chem 1997: 272:25200-25209.
34. Bradfield JY, Berlin RL, Rankin SM, Keeley LL. Cloned cDNA and antibody for an ovarian cortical granule polypeptide of the shrimp Penaeus vannamei. Biol Bull 19S9; 177:344-349.
35. Clark WH Jr, Yudin AI, Lynn JW, Griffin FJ, Pillai MC. Jelly layer formation in Penaeoidean shrimp eggs. Biol Bull 1990; 178:295-299.
36. Alves AP, Mulloy B, Diniz JA, Mourao PA. Sulfated polysaccharides from the egg jelly layer are species-specific inducers of acrosomal reaction in sperm of sea urchins. J Biol Chem 1997; 272:6965-6971.
37. Alves AP, Mulloy B, Moy GW, Vacquier VD, Mourao PA. Females of the sea urchin Strongyiocentrotus purpuratus differ in the structures of their egg jelly sulfated fucans. Glycobiology 1998; 8:939-946.
38. Vilela-Silva AC, Castro MO, Valente AP, Biermann CH, Mourao PA. Sulfated fucans from the egg jellies of the closely related sea urchins Strongyiocentrotus droebachiensis and Strongyiocentrotus pallidus ensure species-specific fertilization. J Biol Chem 2002; 277:379-387.
39. Clark WH Jr, Griffin FJ, Wikramanayake AH. Prefusion events of sperm-oocyte interaction in the marine shrimp. Sicyonia ingentis. Semin Dev Biol 1994; 5:225-231.
40. Wikramanayake AH, Clark WH Jr. Two extracellular matrices from oocytes of the marine shrimp Sicyonia ingentis that independently mediate only primary or secondary sperm binding. Dev Growth Differ 1994; 36:89-101.