The Change of Protein Patterns in Follicular Fluid on Ovarian Response Following Controlled Ovarian Hyperstimulation (COH) of Human

사람의 과배란 유도 후 난소 반응별 난포액 내 단백질 변화

  • 이채식 (세화병원 불임연구소) ;
  • 이상찬 (세화병원 불임연구소) ;
  • 노용호 (세화병원 불임연구소) ;
  • 오대식 (세화병원 불임연구소) ;
  • 이용승 (강원대학교 동물생명과학대학) ;
  • 송은지 (강원대학교 동물생명과학대학) ;
  • 정희태 (강원대학교 수의과대학) ;
  • 양부근 (강원대학교 동물생명과학대학) ;
  • 박춘근 (강원대학교 동물생명과학대학)
  • Received : 2011.08.17
  • Accepted : 2011.08.24
  • Published : 2011.09.30

Abstract

It was conducted the experiment, divided into three groups as normal, poor and polycystic ovary syndrome, to detect the change of protein patterns in follicular fluid on ovarian response following controlled ovarian hyperstimulation for human IVF outcome. In the normal group, it was confirmed reproducible 57 spots in the detected total 81 spots. Then 1 spot was not found in the other groups. In the poor responder group, it was found reproducible 53 spots in the detected total 98 spots. 6 spots were down-regulation and 7 spots were up-regulation comparable with normal group. There were not 5 spots in poor responder group comparable with other groups. In the polycystic ovary syndrome group, it was expressed reproducible 53 spots in the detected total 80 spots and 3 spots were just expressed in this group. However, 4 spots were not found in polycystic ovary syndrome. 9 spots were up-regulation comparable with normal group. Significant up and down-regulation spots among the each groups were identified. The results were a cytosolic carboxypeptidase, a signal-induced proliferation-associated protein 1, a ceruloplasmin, a keratin(type II cytoskeletal 1), a polypeptide N-acetylgalactosantinyltransferase 2, a serine/threonine-protein phosphatase 4 regulatory subunit 4. It was identified that 8 spots, 6 kinds of protein are corresponded with NCBInr database research, but 10 spots were failed in the identification. In conclusion, it has been confirmed change and expression of protein on the ovarian response following COH of human.

Keywords

References

  1. Aldred AR, Grimes A, Schreiber G, Mercer JF (1987): Rat ceruloplasmin. Molecular cloning and gene expression in liver, choroid plexus, yolk sac, placenta, and testis. J Biol Chem 262:2875-2878.
  2. Bowden PE, Haley JL, Kansky A, Rothnagel JA, Jones DO, Turner RJ (1995): Mutation of a type II keratin gene(K6a) in pachyonychia congenita. Nat Genet 10:363-365. https://doi.org/10.1038/ng0795-363
  3. Chung E, Fisher TS, Morgan RW, Robbins MD, Duerr JM, Vander Heiden MG, Gardner JP, Hambor JE, Neveu MJ, Thompson CB (2000): The CD28 and CTLA-4 receptors associate with the serine/ threonine phosphatase PP2A. Immunity 13:313-322. https://doi.org/10.1016/S1074-7613(00)00031-5
  4. Ehrenwald E, Chisolm GM, Fox PL (1994): Intact human ceruloplasmin oxidatively modifies low density lipoprotein. J Clin Invest 93:1493-1501. https://doi.org/10.1172/JCI117127
  5. Fasouliotis SJ, Simon A, Laufer N (2000): Evaluation and treatment of low responders assisted reproductive technology: a challenge to meet. J Assist Reprod Genet 17:357-373. https://doi.org/10.1023/A:1009465324197
  6. Fox PL, Mukhopadhyay C, Ehrenwald E (1995): Structure, oxidant activity, and cardiovascular mechanisms of human ceruloplasmin. Life Sci 56:1749- 1759. https://doi.org/10.1016/0024-3205(95)00146-W
  7. Frattarelli JL, Peterson E (2004): Effect of androgen levels on in vitro fertilization cycles. Fertil Steril 81: 1713-1714. https://doi.org/10.1016/j.fertnstert.2003.11.032
  8. Gallego M, Virshup DM (2005): Protein serine/ threonine phosphatases: life, death and sleeping. Curr Opin Cell Biol 17:197-202. https://doi.org/10.1016/j.ceb.2005.01.002
  9. Herzig S, Neumann J (2000): Effects of serine/threonine protein phosphastase on ion channels in exitable membranes. Physiol Rev 80:173-210.
  10. Hwang KR, Choi YM, Choi DS, Baek KH, Jeon HW, Bae KB, Son YS, Ku SY, Jee BC, Suh CH, Kim SH, Kim JG, Moon SY (2004): Effect of metformin treatment and insulin resistance in patients with polycystic ovary syndrome. Korean J Obstet Gynecol 47:1949-1953.
  11. Ishida D, Kometani K, Yang H, Kakugawa K, Masuda K, Iwai K, Suzuki M, Itohara S, Nakahata T, Hiai H, Kawamoto H, Hattori M, Minato N (2003): Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1 deficient mice. Cancer Cell 4:55-65. https://doi.org/10.1016/S1535-6108(03)00163-6
  12. Jeon GH, Kim CH, Kim EG, Kim SR, Kim SH, Chae HD, Kang BM (2009): The effect of body mass index of on the outcome of in vitro fertilization and embryo transfer in patients with polycystic ovary syndrome. Korean J Obstet Gynecol 52:75-82.
  13. Kawano Y, Fukuda J, Nasu K, Nishida M, Narahara H, Miyakawa I (2004): Production of macrophage inflammatory protein-3$\alpha$ in human follicular fluid and cultured granulosa cells. Fertil Steril supplement 3 82:1206-1211.
  14. Keay SD, Liversedge NH, Mathur RS, Jenkins JM (1997): Assisted conception following poor ovarian response to gonadotropin stimulation. British Journal of Obstetrics and Gynecology 104:521-527. https://doi.org/10.1111/j.1471-0528.1997.tb11525.x
  15. Kim YS, Perdomo J, Whitehead JS, Curtis KJ (1972): Glycosyltransferases in human blood. II. Study of serum galactosyltransferase and N-acetylgalactosaminyltransferase in patients with liver diseases. J Clin Invest 51:2033-2039. https://doi.org/10.1172/JCI107009
  16. Kimura Y, Kurabe N, Ikegami K, Tsutsumi K, Konishi Y, Kaplan OI, Kunitomo H, Iino Y, Blacque OE, Setou M (2010): Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases(CCPs). J Biol Chem 285:22936-22941. https://doi.org/10.1074/jbc.C110.128280
  17. Klumpp S, Krieglstein J.(2002): Serine/threonine protein phosphatases in apoptosis. Curr Opin Pharmacol 2:458-462. https://doi.org/10.1016/S1471-4892(02)00176-5
  18. Kometani K, Ishida D, Hattori M, Minato N (2004): Rap1 and SPA-1 in hematologic malignancy. Trends Mol Med 10:401-408. https://doi.org/10.1016/j.molmed.2004.06.004
  19. Loutradis D, Vomvolaki E, Drakakis P (2008): Poor responder protocols for in-vitro fertilization: options and results. Curr Opin Obstet Gynecol 20:374-378. https://doi.org/10.1097/GCO.0b013e328305b9b8
  20. Mendoza C, Ruiz-Requena, Ortega E, Cremades N, Martinez F, Bernabeu R, Greco E, Tesarik J (2002): Follicular fluid markers of oocyte development potential. Hum Reprod 17:1017-1022. https://doi.org/10.1093/humrep/17.4.1017
  21. Nayudu PL, Lopata A, Jones GM, Gook DA, Bourne HM, Sheather SJ, Brown TC, Johnston WI (1989): An analysis of human oocytes and follicles from stimulated cycles: oocyte morphology and associated follicular fluid characteristics. Hum Reprod 4: 558-567.
  22. Schweiger FJ, Gericke B, Wolfram W, Kaisers U, Dudenhausen JW (2006): Peptide and protein profiles in serum and follicular fluid of women undergoing IVF. Hum Reprod 21:2960-2968. https://doi.org/10.1093/humrep/del257
  23. Song L, Fricker LD (1996): Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J Biol Chem 271: 28884-28889. https://doi.org/10.1074/jbc.271.46.28884
  24. Tarlatzis BC, Zepiridis L, Grimbizis G, Bontis J (2003): Clinical management of low ovarian response to stimulation for IVF: a systemic review. Hum Reprod Update 9:61-76. https://doi.org/10.1093/humupd/dmg007
  25. Thomford PJ, Jelovsek FR, Mattison DR (1987): Effect of oocyte number and rate of atresia on the age of menopause. Reprod Toxicol 1:41-51. https://doi.org/10.1016/0890-6238(87)90070-0
  26. Toba S, Tenno M, Konishi M, Mikami T, Itoh N, Kurosaka A (2000): Brain-specific expression of a novel human UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase( GalNAc-T9). Biochim Biophys Acta 1493:264-268. https://doi.org/10.1016/S0167-4781(00)00180-9
  27. Tonear JP, Philput CB, Jones GS, Muasher SJ (1991): Basal follicle-stimulating hormone level is a better predictor of in vitro fertilization performance than age. Fertil Steril 55:784-791.
  28. Varlamov O, Fricker LD (1998): Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface. J Cell Sci 111:887-885.
  29. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H (1997): Substrate specificities of three members of the human UDP-N-acetyl-D-galactosamine: Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem 272: 23503-235014. https://doi.org/10.1074/jbc.272.38.23503
  30. Webster DR, Modesti NM, Bulinski JC (1992): Regulation of cytoplasmic tubuin carboxypeptidase activity during neural and muscle differentiation: characterization using a microtubule-based assay. Biochemistry 31:5849-5856. https://doi.org/10.1021/bi00140a021
  31. Zhang X, Ozawa Y, Lee H, Wen YD, Tan TH, Wadzinski BE, Seto E (2005): Histone deacetylase 3(HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes 19:827- 839. https://doi.org/10.1101/gad.1286005