Year 2019,
, 74 - 83, 27.08.2019
Bahar Kartal
,
Mehmet Tahir Hatipoğlu
Ümit Ali Kayışlı
Sevtap Hamdemir Kılıç
Evrim Ünsal
Candan Özoğul
Project Number
This research received no specific grant from any funding agency in the public, commercial or not-for-profit sectors
References
- [1]Ma, Y., Hendershot, L.M., “ER chaperone functions during normal and stress conditions ”, Journal of Chemical Neuroanatomy, 28, 51–65, 2004.
- [2] Anelli, T., Sitia, R., “Protein quality control in the early secretory pathway”, EMBO Journal, 27, 315–327, 2008.
- [3] Ron, D., Walter, P., “Signal integration in the endoplasmic reticulum unfolded protein response”, Nature Reviews Molecular Cell Biology, 8, 519–529, 2007.
- [4] Malhotra, J.D., Kaufman, R.J.,“The endoplasmic reticulum and the unfolded protein response”, Cell and Developmental Biology, 18, 716–731, 2007.
- [5] Schroder, M., Kaufman, R.J., “The mammalian unfolded protein response”, Annual Review Of Biochemistry, 74, 739-89, 2005.
- [6] Bernales, S., Papa, F.R., et al., “Intracellular signaling by the unfolded protein response”, Annual Review of Cell and Developmental Biology, 22, 487–508, 2006.
- [7] Bertolotti, A., Zhang, Y., et al., “Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response”, Nature Cell Biology, 2, 326-32,2000.
- [8] Liu, C.Y., Xu, Z., et al., “Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha”, Journal of Biological Chemistry, 278, 17680-7,2003.
- [9] Harding, H.P., Zhang, Y., Bertolotti, A., et al., “Perk is essential for translational regulation and cell survival during the unfolded protein response”, Molacular Cell ,5, 897–90, 2005.
- [10] Scheuner, D., Song, B., et al., “Translational control is required for the unfolded protein response and in vivo glucose homeostasis”, Molecular Cell ,7, 1165-76, 2001.
- [11] Patil, C., Walter, P., “Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals”, Current Opinion in Cell Biology , 13, 349–355, 2001 .
- [12] Yoshida, H., Matsui, T., et al., “XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor”, Cell ,107, 881– 891,2011.
- [13] Kaufman, R.J., “Regulation of mRNA translation by protein folding in the endoplasmic reticulum”, Trends in Biochemical Sciences ,29,152–158, 2004.
- [14] Lee, A.H., Chu, G.C., Iwakoshi, N.N., Glimcher, L.H., “XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands”, EMBO Journal, 24, 4368–80, 2005.
- [15] Ye, J., Rawson, R.B., et al., “ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs ”, Molecular Cell, 6,1355–1364, 2000.
- [16] Liang, G., Audas, T.E., Li, Y., et al., “Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element”, Molecular and Cellular Biology,26,7999–8010, 2006.
- [17] Kimura, K., Bugg, T.D.H., “Recent advances in antimicrobial nucleoside antibiotics targeting cell wall biosynthesis”, Natural Product Reports , 20, 252-273,2003.
- [18] Boatright, J.H., Nickerson, J.M., et al., “Bile acids in treatment of ocular disease”, Journal of Ocular Biology, Diseases, and Informatics, 2, 149–159, 2009.
- [19] Xuan, W.J., Zhang, F.K., et al., “The clinical profiles of primary biliary cirrhosis with a suboptimal biochemical response toursodeoxycholic acid”, Zhonghua Gan Zang Bing Za Zhi, 19, 118-120, 2011.
- [20] Shen, J., Chen, X., et al., “ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals”, Developmental Cell, 3, 99-111, 2002.
- [21] Wang, Y., Puscheck, E.E., et al., “Increases in phosphorylation of SAPK/JNK and p38MAPK correlate negatively with mouse embryo development after culture in different media”, Fertil Steril, 83,1144-54, 2005.
- [22] Gupta, M.K., Uhm, S.J., et al., “Embryo quality and production efficiency of porcine parthenotes is improved by phytohemagglutinin”, Molecular Reproduction and Development,74, 435-44, 2007.
- [23] Hao, L., Vassena, R., et al., “The unfolded protein response contributes to preimplantation mouse embryo death in the DDK syndrome”, Biology of Reproduction,80 ,944- 53, 2009.
- [24] Wu, L.L., Russell, D.L., et al., “Endoplasmic reticulum (ER) stress in cumulus-oocyte complexes impairs pentraxin-3 secretion, mitochondrial membrane potential (DeltaPsi m), and embryo development”, Molecular Endocrinology, 26,562-73, 2012.
- [25] Takahashi, N., Harada, M., et al., “A potential role of endoplasmic reticulum stress in development of ovarian hyperstimulation syndrome”, Molecular and Cellular Endocrinology, 428, 161-9, 2016.
- [26] Zhang, J.Y., Lee, K.S., et al., “Functional characterization of the ER stress induced X-box-binding protein-1 (Xbp-1) in the porcine system”, BMC Molecular Biology, 12, 1471-219, 2011.
- [27] Harada, M., Nose, E., et al., “Evidence of the activation of unfolded protein response in granulosa and cumulus cells during follicular growth and maturation”, Gynecol Endocrinol, 31, 783-7, 2015.
INVESTIGATION OF ENDOPLASMIC RETICULUM SIGNAL PROTEINS IN CUMULUS CELLS WITH NORMAL, HYPERRESPONSIVE, HYPORESPONSIVE AND POLYCYSTIC OVARY SYNDROMES
Year 2019,
, 74 - 83, 27.08.2019
Bahar Kartal
,
Mehmet Tahir Hatipoğlu
Ümit Ali Kayışlı
Sevtap Hamdemir Kılıç
Evrim Ünsal
Candan Özoğul
Abstract
The aim of the study
was to
investigate Endoplasmic reticulum dependent Unfolded Protein Response signal molecules in cumulus cells of the patients
presenting normal, hyperresponsive, hyporesponsive, and polycystic ovary
syndrome . Cumulus
cells were
provided during oocyte retrieval.
Of the patients applying for in vitro fertilization treatment, three
subtypes of patient groups were distinguished
according to their response to follicle stimulations. The first group composed
of normoresponsive (n=8) was considered as retrieval of 10-20 oocytes. The
second group composed of hyporesponsive (n=8) as retrieval of 6 or less
oocytes. Retrieval of 30 or more oocytes as a response to the same stimulus was
considered hyperrespponsive (n=8), which included polycyctıc ovary sydromes. (n=8). We analyzed
the protein expressions of glucose
regulated protein 78 and mRNAs levels of
the X-box binding protein-1 and splicing
X-box binding protein-1 by Western blot and Reverse Transcriptase PCR,
respectively ,in the CCs from different patient groups. All data were loaded to
the software Sigma Stat 3. Differences between groups were evaluated with
one-way ANOVA post hoc TURKEY test. We found that the protein expression of glucose regulated protein 78 was two fold
higher in cumulus cells from hyporesponsive group than the other
groups. Reverse
Transcriptase PCR results
showed us, the mRNA expression of splicing X-box / X-box binding protein-1 level was 1,5
fold higher in the cumulus
cells from the hyporesponsive group compared to
others. Furthermore, we have shown that
when the cumulus cells were
exposed to signal pathway molecules that
related with ER stress; a decrease in the cell proliferation and/or increase in
apoptosis can occured. We have shown that an increased ER stress in the cumulus cells of the ovarian follicle from the
patients forming the hyporesponsive group. We can concluded that increased ER stress or impaired protein folding mechanism in
cumulus cells may affect oocyte
maturation therefore the agents may
be used to decrease
pathological ER stress in the hyporesponsive patients.
Supporting Institution
This research received no specific grant from any funding agency in the public, commercial or not-for-profit sectors
Project Number
This research received no specific grant from any funding agency in the public, commercial or not-for-profit sectors
Thanks
We gratefully acknowledge Gen Art IVF Center for supplying cumulus cells.
References
- [1]Ma, Y., Hendershot, L.M., “ER chaperone functions during normal and stress conditions ”, Journal of Chemical Neuroanatomy, 28, 51–65, 2004.
- [2] Anelli, T., Sitia, R., “Protein quality control in the early secretory pathway”, EMBO Journal, 27, 315–327, 2008.
- [3] Ron, D., Walter, P., “Signal integration in the endoplasmic reticulum unfolded protein response”, Nature Reviews Molecular Cell Biology, 8, 519–529, 2007.
- [4] Malhotra, J.D., Kaufman, R.J.,“The endoplasmic reticulum and the unfolded protein response”, Cell and Developmental Biology, 18, 716–731, 2007.
- [5] Schroder, M., Kaufman, R.J., “The mammalian unfolded protein response”, Annual Review Of Biochemistry, 74, 739-89, 2005.
- [6] Bernales, S., Papa, F.R., et al., “Intracellular signaling by the unfolded protein response”, Annual Review of Cell and Developmental Biology, 22, 487–508, 2006.
- [7] Bertolotti, A., Zhang, Y., et al., “Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response”, Nature Cell Biology, 2, 326-32,2000.
- [8] Liu, C.Y., Xu, Z., et al., “Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha”, Journal of Biological Chemistry, 278, 17680-7,2003.
- [9] Harding, H.P., Zhang, Y., Bertolotti, A., et al., “Perk is essential for translational regulation and cell survival during the unfolded protein response”, Molacular Cell ,5, 897–90, 2005.
- [10] Scheuner, D., Song, B., et al., “Translational control is required for the unfolded protein response and in vivo glucose homeostasis”, Molecular Cell ,7, 1165-76, 2001.
- [11] Patil, C., Walter, P., “Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals”, Current Opinion in Cell Biology , 13, 349–355, 2001 .
- [12] Yoshida, H., Matsui, T., et al., “XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor”, Cell ,107, 881– 891,2011.
- [13] Kaufman, R.J., “Regulation of mRNA translation by protein folding in the endoplasmic reticulum”, Trends in Biochemical Sciences ,29,152–158, 2004.
- [14] Lee, A.H., Chu, G.C., Iwakoshi, N.N., Glimcher, L.H., “XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands”, EMBO Journal, 24, 4368–80, 2005.
- [15] Ye, J., Rawson, R.B., et al., “ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs ”, Molecular Cell, 6,1355–1364, 2000.
- [16] Liang, G., Audas, T.E., Li, Y., et al., “Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element”, Molecular and Cellular Biology,26,7999–8010, 2006.
- [17] Kimura, K., Bugg, T.D.H., “Recent advances in antimicrobial nucleoside antibiotics targeting cell wall biosynthesis”, Natural Product Reports , 20, 252-273,2003.
- [18] Boatright, J.H., Nickerson, J.M., et al., “Bile acids in treatment of ocular disease”, Journal of Ocular Biology, Diseases, and Informatics, 2, 149–159, 2009.
- [19] Xuan, W.J., Zhang, F.K., et al., “The clinical profiles of primary biliary cirrhosis with a suboptimal biochemical response toursodeoxycholic acid”, Zhonghua Gan Zang Bing Za Zhi, 19, 118-120, 2011.
- [20] Shen, J., Chen, X., et al., “ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals”, Developmental Cell, 3, 99-111, 2002.
- [21] Wang, Y., Puscheck, E.E., et al., “Increases in phosphorylation of SAPK/JNK and p38MAPK correlate negatively with mouse embryo development after culture in different media”, Fertil Steril, 83,1144-54, 2005.
- [22] Gupta, M.K., Uhm, S.J., et al., “Embryo quality and production efficiency of porcine parthenotes is improved by phytohemagglutinin”, Molecular Reproduction and Development,74, 435-44, 2007.
- [23] Hao, L., Vassena, R., et al., “The unfolded protein response contributes to preimplantation mouse embryo death in the DDK syndrome”, Biology of Reproduction,80 ,944- 53, 2009.
- [24] Wu, L.L., Russell, D.L., et al., “Endoplasmic reticulum (ER) stress in cumulus-oocyte complexes impairs pentraxin-3 secretion, mitochondrial membrane potential (DeltaPsi m), and embryo development”, Molecular Endocrinology, 26,562-73, 2012.
- [25] Takahashi, N., Harada, M., et al., “A potential role of endoplasmic reticulum stress in development of ovarian hyperstimulation syndrome”, Molecular and Cellular Endocrinology, 428, 161-9, 2016.
- [26] Zhang, J.Y., Lee, K.S., et al., “Functional characterization of the ER stress induced X-box-binding protein-1 (Xbp-1) in the porcine system”, BMC Molecular Biology, 12, 1471-219, 2011.
- [27] Harada, M., Nose, E., et al., “Evidence of the activation of unfolded protein response in granulosa and cumulus cells during follicular growth and maturation”, Gynecol Endocrinol, 31, 783-7, 2015.