Processing and subcellular localization of ADAM2 in the Macaca fascicularis testis and sperm.
Fertilin, a heterodimeric protein complex composed of ADAM1 and ADAM2 located on the sperm surface, is involved in sperm-egg interaction. In our study, we examined the physiological processing and subcellular localization of M. fascicularis ADAM2 during spermatogenesis in the testis and epididymal tract. M. fascicularis ADAM2 was initially synthesized as a 100 kDa precursor in testicular germ cells. After passing into 50 kDa intermediate form in the epididymal tracts, the precursor form was finally processed into a 47 kDa protein in sperm. We found that M. fascicularis ADAM2 is localized on the sperm surface and contributes to the formation of a candidate fertilin complex. In particular, Far-Western blot analysis revealed that M. fascicularis ADAM2 cystein-rich domain may be related to protein-protein interaction. Therefore, the cystein-rich domain of ADAM2 could provide a mechanism to form a fertilin complex.
Kim
Ekyune
E
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 685-1 Yangcheong-ri Ochang-eup, Chung-buk 363-883, Republic of Korea.
Lee
Jae-Woong
JW
Baek
Dong Chul
DC
Lee
Sang-Rae
SR
Kim
Myeong-Su
MS
Kim
Sang-Hyun
SH
Kim
Chan-Shick
CS
Ryoo
Zae-Young
ZY
Kang
Han-Seok
HS
Chang
Kyu-Tae
KT
D051722:ADAM Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry; D004822:Epididymis / Q000378:metabolism; D000072196:Fertilins; D005306:Fertilization / Q000502:physiology; D008252:Macaca fascicularis / Q000378:metabolism*; D008297:Male; D008562:Membrane Glycoproteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins; D013091:Spermatogenesis; D013094:Spermatozoa / Q000378:metabolism* / Q000648:ultrastructure; D013737:Testis / Q000378:metabolism* / Q000648:ultrastructure
D008562:Membrane Glycoproteins; D011994:Recombinant Proteins; D051722:ADAM Proteins; D000072196:Fertilins