A stress paradox: the dual role of the unfolded protein response in the placenta

被引:0
作者
Chowdhury, Diba [1 ]
Jang, Chloe E. [1 ,2 ,3 ]
Lajoie, Patrick [1 ,3 ]
Renaud, Stephen J. [1 ,3 ]
机构
[1] Western Univ, Schulich Sch Med & Dent, Dept Anat & Cell Biol, London, ON, Canada
[2] Western Univ, Schulich Sch Med & Dent, Dept Biochem, London, ON, Canada
[3] Childrens Hlth Res Inst, Lawson Hlth Res Inst, London, ON, Canada
来源
FRONTIERS IN ENDOCRINOLOGY | 2024年 / 15卷
基金
加拿大健康研究院;
关键词
ER stress; UPR; placenta; trophoblast; decidua; ENDOPLASMIC-RETICULUM STRESS; GROWTH-FACTOR-I; ER STRESS; CELL-DIFFERENTIATION; GENE-EXPRESSION; TRANSCRIPTIONAL INDUCTION; TRANSMEMBRANE PROTEIN; TRANSLATIONAL CONTROL; CHEMICAL CHAPERONE; INDUCED APOPTOSIS;
D O I
10.3389/fendo.2024.1525189
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The placenta is a temporary organ that forms during pregnancy and is essential for fetal development and maternal health. As an endocrine organ, proper placental function requires continual production, folding, and transport of proteins and lipids. Central to these processes is the endoplasmic reticulum (ER), a dynamic organelle responsible for maintaining cellular protein and lipid synthesis and processing. ER stress occurs when there is an accumulation of unfolded or misfolded proteins, which triggers the activation of cellular pathways collectively called the unfolded protein response. Unfolded protein response pathways act to alleviate the misfolded protein burden and restore ER homeostasis, or if unresolved, initiate cell death. While prolonged ER stress has been linked to deficient placental function and adverse pregnancy outcomes, basal activation of unfolded protein response pathways is required for placental development and function. This review explores the importance of ER homeostasis in placental development and function, examining how disruptions in ER stress responses may contribute to adverse pregnancy outcomes.
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页数:14
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共 156 条
[1]   The endocannabinoid 2-arachidonoylglycerol promotes endoplasmic reticulum stress in placental cells [J].
Almada, Marta ;
Costa, Lia ;
Fonseca, Bruno ;
Alves, Patricia ;
Braga, Jorge ;
Goncalves, Daniela ;
Teixeira, Natercia ;
Correia-da-Silva, Georgina .
REPRODUCTION, 2020, 160 (02) :171-180
[2]   Endoplasmic reticulum stress signalling - from basic mechanisms to clinical applications [J].
Almanza, Aitor ;
Carlesso, Antonio ;
Chintha, Chetan ;
Creedican, Stuart ;
Doultsinos, Dimitrios ;
Leuzzi, Brian ;
Luis, Andreia ;
McCarthy, Nicole ;
Montibeller, Luigi ;
More, Sanket ;
Papaioannou, Alexandra ;
Pueschel, Franziska ;
Sassano, Maria Livia ;
Skoko, Josip ;
Agostinis, Patrizia ;
de Belleroche, Jackie ;
Eriksson, Leif A. ;
Fulda, Simone ;
Gorman, Adrienne M. ;
Healy, Sandra ;
Kozlov, Andrey ;
Munoz-Pinedo, Cristina ;
Rehm, Markus ;
Chevet, Eric ;
Samali, Afshin .
FEBS JOURNAL, 2019, 286 (02) :241-278
[3]   The c-Jun N-terminal protein kinase family of mitogen-activated protein kinases (JNK MAPKs) [J].
Barr, RK ;
Bogoyevitch, MA .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2001, 33 (11) :1047-1063
[4]   The fine-tuning of endoplasmic reticulum stress response and autophagy activation during trophoblast syncytialization [J].
Bastida-Ruiz, Daniel ;
Yart, Lucile ;
Wuillemin, Christine ;
Ribaux, Pascale ;
Morris, Nolwenn ;
Epiney, Manuella ;
de Tejada, Begona Martinez ;
Cohen, Marie .
CELL DEATH & DISEASE, 2019, 10 (9)
[5]   Histone deacetylase 1 and 2 drive differentiation and fusion of progenitor cells in human placental trophoblasts [J].
Bhattad, Gargi Jaju ;
Jeyarajah, Mariyan J. ;
McGill, Megan G. ;
Dumeaux, Vanessa ;
Okae, Hiroaki ;
Arima, Takahiro ;
Lajoie, Patrick ;
Berube, Nathalie G. ;
Renaud, Stephen J. .
CELL DEATH & DISEASE, 2020, 11 (05)
[6]   Uterine Selection of Human Embryos at Implantation [J].
Brosens, Jan J. ;
Salker, Madhuri S. ;
Teklenburg, Gijs ;
Nautiyal, Jaya ;
Salter, Scarlett ;
Lucas, Emma S. ;
Steel, Jennifer H. ;
Christian, Mark ;
Chan, Yi-Wah ;
Boomsma, Carolien M. ;
Moore, Jonathan D. ;
Hartshorne, Geraldine M. ;
Sucurovic, Sandra ;
Mulac-Jericevic, Biserka ;
Heijnen, Cobi J. ;
Quenby, Siobhan ;
Koerkamp, Marian J. Groot ;
Holstege, Frank C. P. ;
Shmygol, Anatoly ;
Macklon, Nick S. .
SCIENTIFIC REPORTS, 2014, 4
[7]   Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia [J].
Buhimschi, Irina A. ;
Nayeri, Unzila A. ;
Zhao, Guomao ;
Shook, Lydia L. ;
Pensalfini, Anna ;
Funai, Edmund F. ;
Bernstein, Ira M. ;
Glabe, Charles G. ;
Buhimschi, Catalin S. .
SCIENCE TRANSLATIONAL MEDICINE, 2014, 6 (245)
[8]   Pre-eclampsia: pathophysiology and clinical implications [J].
Burton, Graham J. ;
Redman, Christopher W. ;
Roberts, James M. ;
Moffett, Ashley .
BMJ-BRITISH MEDICAL JOURNAL, 2019, 366
[9]   Endoplasmic reticulum stress in the pathogenesis of early-onset pre-eclampsia [J].
Burton, Graham J. ;
Yung, Hong-Wa .
PREGNANCY HYPERTENSION-AN INTERNATIONAL JOURNAL OF WOMENS CARDIOVASCULAR HEALTH, 2011, 1 (01) :72-78
[10]   IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA [J].
Calfon, M ;
Zeng, HQ ;
Urano, F ;
Till, JH ;
Hubbard, SR ;
Harding, HP ;
Clark, SG ;
Ron, D .
NATURE, 2002, 415 (6867) :92-96