Protein oligomerization is the biochemical process highly up-regulated in porcine oocytes before in vitro maturation (IVM)

1. Watson AJ. Oocyte cytoplasmic maturation: a key mediator of oocyte and embryo developmental competence. J Anim Sci 2007;85:E1-3; DOI:10.2527/jas.2006-432.10.2527/jas.2006-43217322120Search in Google Scholar

2. Agung B, Otoi T, Fuchimoto D, Senbon S, Onishi A, Nagai T. In vitro fertilization and development of porcine oocytes matured in follicular fluid. J Reprod Dev. 2013;59:103–6.10.1262/jrd.2011-050393419223428620Search in Google Scholar

3. Chang CL, Wang H-S, Soong Y-K, Huang SY, Pai SY, Hsu SYT. Regulation of oocyte and cumulus cell interactions by intermedin/adrenomedullin 2. J Biol Chem. 2011;286:43193–203; DOI:10.1074/jbc.M111.297358.10.1074/jbc.M111.297358323484922009752Search in Google Scholar

4. Palma GA, Argañaraz ME, Barrera AD, Rodler D, Mutto AÁ, Sinowatz F. Biology and biotechnology of follicle development. ScientificWorldJournal. 2012;2012:938138; DOI:10.1100/2012/938138.10.1100/2012/938138336621922666170Search in Google Scholar

5. Liu S. A review on protein oligomerization process. Int J Precis Eng Manuf. 2015;16:2731–60; DOI:10.1007/s12541-015-0349-x.10.1007/s12541-015-0349-xSearch in Google Scholar

6. Celichowski P, Nawrocki MJ, Dyszkiewicz-Konwińska M, Jankowski M, Budna J, Bryja A, Kranc W, Borys S, Knap S, Ciesiółka S, Jeseta M, Piasecka- Stryczyńska K, Khozmi R, Bukowska D, Antosik P, Brüssow KP, Bruska M, Nowicki M, Zabel M, Kempisty B. “Positive Regulation of RNA Metabolic Process” Ontology Group Highly Regulated in Porcine Oocytes Matured In Vitro: A Microarray Approach. BioMed Res Int. 2018;2018:2863068; DOI:10.1155/2018/2863068.10.1155/2018/2863068581892229546053Search in Google Scholar

7. Marques E, Nkrumah JD, Sherman EL, Moore SS. Polymorphisms in positional candidate genes on BTA14 and BTA26 affect carcass quality in beef cattle. J Anim Sci. 2009;87:2475–84; DOI:10.2527/jas.2008-1456.10.2527/jas.2008-145619395506Search in Google Scholar

8. Davoli R, Fontanesi L, Braglia S, Russo V. A missense mutation in the porcine mitochondrial 2,4-dienoyl CoA reductase 1 (DECR1) gene and linkage mapping of this locus to chromosome 4; Anim Genet. 2002;33:73–5.10.1046/j.1365-2052.2002.0742b.xSearch in Google Scholar

9. Wathes DC, Clempson AM, Pollott GE. Associations between lipid metabolism and fertility in the dairy cow. Reprod Fertil Dev. 2012;25:48–61; DOI:10.1071/RD12272.10.1071/RD1227223244828Search in Google Scholar

10. Biterova E, Esmaeeli M, Alanen HI, Saaranen M, Ruddock LW. Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease. Sci Rep. 2018;8:6752; DOI:10.1038/s41598-018-25237-7.10.1038/s41598-018-25237-7592806129713054Search in Google Scholar

11. Al-Edani T, Assou S, Ferrières A, Bringer Deutsch S, Gala A, Lecellier C-H, Aït-Ahmed O, Hamamah S. Female aging alters expression of human cumulus cells genes that are essential for oocyte quality. BioMed Res Int. 2014;2014:964614; DOI:10.1155/2014/964614.10.1155/2014/964614416802825276836Search in Google Scholar

12. Groh KJ, Schönenberger R, Eggen RIL, Segner H, Suter MJ-F. Analysis of protein expression in zebrafish during gonad differentiation by targeted proteomics. Gen Comp Endocrinol. 2013;193:210–20; DOI:10.1016/j.ygcen.2013.07.020.10.1016/j.ygcen.2013.07.020Search in Google Scholar

13. Cooke G, Armstrong ME, Donnelly SC. Macrophage migration inhibitory factor (MIF), enzymatic activity and the inflammatory response. BioFactors Oxf Engl. 2009;35:165–8; DOI:10.1002/biof.27.10.1002/biof.27Search in Google Scholar

14. Lopes F, Vannoni A, Sestini S, Casciaro A, Carducci A, Bartolommei S, Toschi P, Ptak G, Cintorino M, Arcuri F. Sheep (Ovis aries) Macrophage Migration Inhibitory Factor: molecular cloning, characterization, tissue distribution and expression in the ewe reproductive tract and in the placenta. Cytokine. 2011;54:315–23; DOI:10.1016/j.cyto.2011.02.013.10.1016/j.cyto.2011.02.013Search in Google Scholar

15. Franz A, Ackermann L, Hoppe T. Create and preserve: Proteostasis in development and aging is governed by Cdc48/p97/VCP. Biochim Biophys Acta BBA - Mol Cell Res. 2014;1843:205–15; DOI:10.1016/j.bbamcr.2013.03.031.10.1016/j.bbamcr.2013.03.031Search in Google Scholar

16. Capkova J, Kubatova A, Ded L, Tepla O, Peknicova J. Evaluation of the expression of sperm proteins in normozoospermic and asthenozoospermic men using monoclonal antibodies. Asian J Androl 2016;18:108–13; DOI:10.4103/1008-682X.151400.10.4103/1008-682X.151400Search in Google Scholar

17. Müller JMM, Deinhardt K, Rosewell I, Warren G, Shima DT. Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality. Biochem Biophys Res Commun. 2007;354:459–65; DOI:10.1016/j.bbrc.2006.12.206.10.1016/j.bbrc.2006.12.206Search in Google Scholar

18. Shi Y, Vattem KM, Sood R, An J, Liang J, Stramm L, Wek RC. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol Cell Biol. 1998;18:7499–509.10.1128/MCB.18.12.7499Search in Google Scholar

19. Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell. 2000;5:897–904.10.1016/S1097-2765(00)80330-5Search in Google Scholar

20. Lin JH, Li H, Yasumura D, Cohen HR, Zhang C, Panning B, Shokat KM, Lavail MM, Walter P. IRE1 signaling affects cell fate during the unfolded protein response. Science. 2007;318:944–9; DOI:10.1126/science.1146361.10.1126/science.1146361367058817991856Search in Google Scholar

21. Basheer WA, Fu Y, Shimura D, Xiao S, Agvanian S, Hernandez DM, Hitzeman TC, Hong T, Shaw RM. Stress response protein GJA1-20k promotes mitochondrial biogenesis, metabolic quiescence, and cardioprotection against ischemia/reperfusion injury. JCI Insight. 2018;3; DOI:10.1172/jci.insight.121900.10.1172/jci.insight.121900623744230333316Search in Google Scholar

22. Kempisty B, Ziółkowska A, Ciesiółka S, Piotrowska H, Antosik P, Bukowska D, Nowicki M, Brüssow KP, Zabel M. Study on connexin gene and protein expression and cellular distribution in relation to real-time proliferation of porcine granulosa cells. J Biol Regul Homeost Agents. 2014;28:625–35.Search in Google Scholar

23. Wang H-X, Tong D, El-Gehani F, Tekpetey FR, Kidder GM. Connexin expression and gap junctional coupling in human cumulus cells: contribution to embryo quality. J Cell Mol Med. 2009;13:972–84; DOI:10.1111/j.1582-4934.2008.00373.x.10.1111/j.1582-4934.2008.00373.x382341218505471Search in Google Scholar

24. Richard S, Baltz JM. Prophase I arrest of mouse oocytes mediated by natriuretic peptide precursor C requires GJA1 (connexin-43) and GJA4 (connexin-37) gap junctions in the antral follicle and cumulus- oocyte complex. Biol Reprod. 2014;90:137; DOI:10.1095/biolreprod.114.118505.10.1095/biolreprod.114.11850524804968Search in Google Scholar

25. Moller DE, Cohen O, Yamaguchi Y, Assiz R, Grigorescu F, Eberle A, Morrow LA, Moses AC, Flier JS. Prevalence of mutations in the insulin receptor gene in subjects with features of the type A syndrome of insulin resistance. Diabetes. 1994;43:247–55.10.2337/diab.43.2.2478288049Search in Google Scholar

26. Chaves RN, Duarte ABG, Rodrigues GQ, Celestino JJH, Silva GM, Lopes CAP, Almeida AP, Donato MAM, Peixoto CA, Moura AAA, Lobo CH, Locatelli Y, Mermillod P, Campello CC, Figueiredo JR. The effects of insulin and follicle-simulating hormone (FSH) during in vitro development of ovarian goat preantral follicles and the relative mRNA expression for insulin and FSH receptors and cytochrome P450 aromatase in cultured follicles. Biol Reprod. 2012;87:69; DOI:10.1095/biolreprod.112.099010.10.1095/biolreprod.112.09901022811569Search in Google Scholar

27. Borys S, Brązert M, Jankowski M, Kocherova I, Ożegowska K, Celichowski P, Nawrocki MJ, Kranc W, Bryja A, Kulus M, Jeseta M, Pieńkowski W, Bręborowicz A, Bukowska D, Antosik P, Pawelczyk L, Skowroński MT, Brüssow KP, Bruska M, Zabel M, Nowicki M, Kempisty B. Enzyme linked receptor protein signaling pathway is one of the ontology groups that are highly up-regulated in porcine oocytes before in vitro maturation. J Biol Regul Homeost Agents. 2018;32:1089–103.Search in Google Scholar

28. Procházková J, Kabátková M, Šmerdová L, Pacherník J, Sykorová D, Kohoutek J, Šimečková P, Hrubá E, Kozubík A, Machala M, Vondráček J. Aryl hydrocarbon receptor negatively regulates expression of the plakoglobin gene (jup). Toxicol Sci Off J Soc Toxicol. 2013;134:258–70; DOI:10.1093/toxsci/kft110.10.1093/toxsci/kft11023690540Search in Google Scholar

29. Swope D, Li J, Muller EJ, Radice GL. Analysis of a Jup hypomorphic allele reveals a critical threshold for postnatal viability. Genes N Y N 2000. 2012;50:717–27; DOI:10.1002/dvg.22034.10.1002/dvg.22034341004022522917Search in Google Scholar

30. Fan H-Y, Liu Z, Shimada M, Sterneck E, Johnson PF, Hedrick SM, Richards JS. MAPK3/1 (ERK1/2) in ovarian granulosa cells are essential for female fertility. Science. 2009;324:938–41; DOI:10.1126/science.1171396.10.1126/science.1171396284789019443782Search in Google Scholar

31. Ou X-H, Li S, Xu B-Z, Chen L-N, Jiang M-X, Chen S-Q, Chen N-Q. Mitogen-activated protein kinase-activated protein kinase 2 is a critical regulator of pig oocyte meiotic maturation. Reprod Fertil Dev. 2017;29:223–33; DOI:10.1071/RD15150.10.1071/RD1515026193799Search in Google Scholar

32. Cao R, Wu W, Zhou X, Liu K, Li B, Huang X, Zhang Y, Liu H. Let-7g induces granulosa cell apoptosis by targeting MAP3K1 in the porcine ovary. Int J Biochem Cell Biol. 2015;68:148–57; DOI:10.1016/j.biocel.2015.08.011.10.1016/j.biocel.2015.08.01126299328Search in Google Scholar

33. Xia Y, Karin M. The control of cell motility and epithelial morphogenesis by Jun kinases. Trends Cell Biol. 2004;14:94–101; DOI:10.1016/j.tcb.2003.12.005.10.1016/j.tcb.2003.12.00515102441Search in Google Scholar