Importance of the porcine ADAM3 disintegrin domain in sperm-egg interaction

Journal of Reproduction and Development

Volumn 55, Issue 2, 2009, Pages 156-162

  Kim, Ekyune ^a   Park, Ki Eun ^b   Kim, Ji Su ^a   Baek, Dong Chul ^a,c   Lee, Jae Woong ^a   Lee, Sang Rae ^a   Kim, Myeong Su ^a   Kim, Sang Hyun ^a   Kim, Chan Shick ^c   Koo, Deog Bon ^d   Kang, Han Seok ^e   Ryoo, Zae Young ^f   Chang, Kyu Tae ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b PURDUE UNIVERSITY   (United States)

^c Jeju National University   (South Korea)

^d Daegu University   (South Korea)

^e Pusan National University   (South Korea)

^f Kyungpook National University   (South Korea)

Author keywords

A disintegrin and metalloprotease (ADAM); Disintegrin domain; Porcine; Sperm egg interaction

Indexed keywords

ADAM PROTEIN; DNA; ISOPROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ANIMAL DISEASE; ARTICLE; CHEMISTRY; FEMALE; FERTILITY; FERTILIZATION IN VITRO; GENE DOSAGE; GENETICS; MALE; MOLECULAR GENETICS; PHYSIOLOGY; POLYMERASE CHAIN REACTION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SOUTHERN BLOTTING; SWINE; WESTERN BLOTTING;

ADAM PROTEINS; AMINO ACID SEQUENCE; ANIMALS; BLOTTING, SOUTHERN; BLOTTING, WESTERN; DNA; FEMALE; FERTILIZATION IN VITRO; GENE DOSAGE; MALE; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SPERM-OVUM INTERACTIONS; SWINE;

SUIDAE; SUS; SUS SCROFA DOMESTICA;

EID: 66949137135     PISSN: 09168818     EISSN: 13484400     Source Type: Journal    
DOI: 10.1262/jrd.20134     Document Type: Article

References (24)

1. Primakoff P, Myles DG. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet 2000; 16: 83-87.
2. Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Gene Dev 2003; 17: 7-30.
3. Hooper NM, Karran EH, Turner AJ. Membrane protein secretases. Biochem J 1997; 321: 265-279.
4. Suzuki A, Kadota N, Hara T, Nakagami Y, Izumi T, Takenawa T, Sabe H, Endo T. Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src. Oncogene 2000; 19: 5842-5850.
5. Waters SI, White JM. Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol Reprod 1997; 56: 1245-1254.
6. 1 integrin is the receptor for sperm fertilin β. Chem Biol 1999; 6: 1-10.
7. Cho C, Bunch DO, Faure JE, Goulding EH, Eddy EM, Primakoff P, Myles DG. Fertilization defects in sperm from mice lacking fertilin β. Science 1998; 281: 1857-1859.
8. Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin β. Dev Biol 2001; 233: 204-213.
9. Nishimura H, Kim E, Nakanishi T, Baba T. Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem 2004; 279: 34957-34962.
10. Kim E, Yamashita M, Nakanishi T, Park KE, Kimura M, Kashiwabara S, Baba T. Mouse sperm lacking ADAM1b/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization. J Biol Chem 2006; 281: 5634-5639.
11. Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 1992; 356: 248-252.
12. Lum L, Blobel CP. Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev Biol 1997; 191: 131-145.
13. Waters SI, White JM. Biochemical and molecular characterization of bovine fertilin α and β (ADAM 1 and ADAM 2): a candidate sperm-egg binding/fusion complex. Biol Reprod 1997; 56: 1245-1254.
14. Nishimura H, Kim E, Fujimori T, Kashiwabara S, Kuroiwa A, Matsuda Y, Baba T. The ADAM1a and ADAM1b genes, instead of the ADAM1 (fertilin α) gene, are localized on mouse chromosome 5. Gene 2002; 291: 67-76.
15. Kim E, Nishimura H, Baba T. Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm. Biochem Biophys Res Commun 2003; 304: 313-319.
16. Linder B, Heinlein UAO. Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides. Dev Growth Differ 1997; 39: 243-247.
17. Yuan R, Primakoff P, Myles DG. A role of the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J Cell Biol 1997; 137: 105-112.
18. Adham IM, Kim Y, Shamsadin R, Heinlein UA, vonBeust G, Mattei MG, Engel W. Molecular cloning, chromosomal localization, and expression analysis of CYRN1 and CYRN2, two human genes coding for cyritestin, a sperm protein involved in gamete interaction. DNA Cell Biol 1998; 17: 161-168.
19. Grzmil P, Kim Y, Shamsadin R, Neesen J, Adham IM, Heinlein UA, Schwarzer UJ, Engel W. Human cyritestin genes (CYRN1 and CYRN2) are non-functional. Biochem J 2001; 357: 551-556.
20. Kim E, Lee JW, Baek DC, Lee SR, Kim MS, Kim SH, Imakawa K, Chang KT. Identification of novel retromer complexes in the mouse testis. Biochem Biophys Res Commun 2008; 375: 16-21.
21. Funahashi H, Cantley T, Day BN. Different hormonal requirements of pig oocytecumulus complexes during maturation in vitro. J Reprod Fertil Suppl 1994; 101: 159-165.
22. Petters RM, Wells KD. Culture of pig embryos. J Reprod Fertil Suppl 1993; 48: 61-73.
23. Abeydeera LR, Day BN. Fertilization and subsequent development in vitro of pig oocytes inseminated in a modified tris-buffered medium with frozen-thawed ejaculated spermatozoa. Biol Reprod 1997; 57: 729-734.
24. Kim E, Baba D, Kimura M, Yamashita M, Kashiwabara S, Baba T. Identification of a hyaluronidase, Hyal5, involved in penetration of mouse sperm through cumulus mass. Proc Natl Acad Sci USA 2005; 102: 18028-18033.