Comparative Analysis of AGE and RAGE Levels in Human Somatic and Embryonic Stem Cells Under HO-Induced Noncytotoxic Oxidative Stress Conditions

Overview

Journal Oxid Med Cell Longev

Publisher Wiley

Specialties Cell Biology
Endocrinology

Date 2017 Nov 7

PMID 29104727

Citations 8

Authors

Maria Barandalla

Elisa Haucke

Bernd Fischer

Alexander Navarrete Santos

Silvia Colleoni

Cesare Galli

Anne Navarrete Santos

Giovanna Lazzari

Affiliations

Soon will be listed here.

Abstract

The accumulation of advanced glycation end products (AGEs) occurs in ageing and in many degenerative diseases as a final outcome of persistent oxidative stress on cells and organs. Environmental alterations taking place during early embryonic development can also lead to oxidative damage, reactive oxygen species (ROS) production, and AGE accumulation. Whether similar mechanisms act on somatic and embryonic stem cells (ESC) exposed to oxidative stress is not known; and therefore, the modelling of oxidative stress in vitro on human ESC has been the focus of this study. We compared changes in N -carboxymethyl-lysine (CML) advanced glycation end products and RAGE levels in hESC versus differentiated somatic cells exposed to HO within the noncytotoxic range. Our data revealed that hESC accumulates CML and RAGE under oxidative stress conditions in different ways than somatic cells, being the accumulation of CML statistically significant only in somatic cells and, conversely, the RAGE increase exclusively appreciated in hESC. Then, following cardiac and neural differentiation, we observed a progressive removal of AGEs and at the same time an elevated activity of the 20S proteasome. We conclude that human ESCs constitute a unique model to study the consequence of an oxidative environment in the pluripotent cells of the embryo during the human preimplantation period.

Citing Articles

Slot Blot- and Electrospray Ionization-Mass Spectrometry/Matrix-Assisted Laser Desorption/Ionization-Mass Spectrometry-Based Novel Analysis Methods for the Identification and Quantification of Advanced Glycation End-Products in the Urine.

Takata T, Inoue S, Kunii K, Masauji T, Miyazawa K Int J Mol Sci. 2024; 25(17).

PMID: 39273579 PMC: 11395049. DOI: 10.3390/ijms25179632.

Role of NF-κB signaling pathway in HO-induced oxidative stress of hiPSCs.

Qin J, Yang J, Li J, Zhao D, An J, Zhai Z In Vitro Cell Dev Biol Anim. 2024; 60(9):1021-1033.

PMID: 39134871 DOI: 10.1007/s11626-024-00943-x.

Slot Blot Analysis of Intracellular Glyceraldehyde-Derived Advanced Glycation End Products Using a Novel Lysis Buffer and Polyvinylidene Difluoride Membrane.

Takata T, Murayama H, Masauji T Bio Protoc. 2024; 14(14):e5038.

PMID: 39100597 PMC: 11292133. DOI: 10.21769/BioProtoc.5038.

Potential of the Novel Slot Blot Method with a PVDF Membrane for Protein Identification and Quantification in Kampo Medicines.

Takata T, Masauji T, Motoo Y Membranes (Basel). 2023; 13(12).

PMID: 38132900 PMC: 10745123. DOI: 10.3390/membranes13120896.

Is the Novel Slot Blot a Useful Method for Quantification of Intracellular Advanced Glycation End-Products?.

Takata T Metabolites. 2023; 13(4).

PMID: 37110222 PMC: 10144988. DOI: 10.3390/metabo13040564.

References

Piperi C, Goumenos A, Adamopoulos C, Papavassiliou A . AGE/RAGE signalling regulation by miRNAs: associations with diabetic complications and therapeutic potential. Int J Biochem Cell Biol. 2015; 60:197-201. DOI: 10.1016/j.biocel.2015.01.009. View

Oya T, Hattori N, Mizuno Y, Miyata S, Maeda S, Osawa T . Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J Biol Chem. 1999; 274(26):18492-502. DOI: 10.1074/jbc.274.26.18492. View

Hohn T, Grune T . The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system. Redox Biol. 2014; 2:388-94. PMC: 3926120. DOI: 10.1016/j.redox.2013.12.029. View

Ahmed K, Muniandy S, Ismail I . N(epsilon)-(Carboxymethyl)lysine and Coronary Atherosclerosis-Associated Low Density Lipoprotein Abnormalities in Type 2 Diabetes: Current Status. J Clin Biochem Nutr. 2009; 44(1):14-27. PMC: 2613495. DOI: 10.3164/jcbn.08-190. View

Ben-Nissan G, Sharon M . Regulating the 20S proteasome ubiquitin-independent degradation pathway. Biomolecules. 2014; 4(3):862-84. PMC: 4192676. DOI: 10.3390/biom4030862. View

Nielsen J, Kristiansen S, Norregaard R, Andersen C, Denner L, Nielsen T . Blockage of receptor for advanced glycation end products prevents development of cardiac dysfunction in db/db type 2 diabetic mice. Eur J Heart Fail. 2009; 11(7):638-47. DOI: 10.1093/eurjhf/hfp070. View

Grune T, Jung T, Merker K, Davies K . Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol. 2004; 36(12):2519-30. DOI: 10.1016/j.biocel.2004.04.020. View

Bucciarelli L, Wendt T, Qu W, Lu Y, Lalla E, Rong L . RAGE blockade stabilizes established atherosclerosis in diabetic apolipoprotein E-null mice. Circulation. 2002; 106(22):2827-35. DOI: 10.1161/01.cir.0000039325.03698.36. View

Younessi P, Yoonessi A . Advanced glycation end-products and their receptor-mediated roles: inflammation and oxidative stress. Iran J Med Sci. 2013; 36(3):154-66. PMC: 3556769. View

10.

Park H, Ku S, Park H, Hong J, Kim D, Choi B . RAGE siRNA-mediated gene silencing provides cardioprotection against ventricular arrhythmias in acute ischemia and reperfusion. J Control Release. 2015; 217:315-26. DOI: 10.1016/j.jconrel.2015.09.006. View

11.

George S, Heng B, Vinoth K, Kishen A, Cao T . Comparison of the response of human embryonic stem cells and their differentiated progenies to oxidative stress. Photomed Laser Surg. 2009; 27(4):669-74. DOI: 10.1089/pho.2008.2354. View

12.

Saretzki G, Walter T, Atkinson S, Passos J, Bareth B, Keith W . Downregulation of multiple stress defense mechanisms during differentiation of human embryonic stem cells. Stem Cells. 2007; 26(2):455-64. DOI: 10.1634/stemcells.2007-0628. View

13.

Lizotte P, Hanford L, Enghild J, Nozik-Grayck E, Giles B, Oury T . Developmental expression of the receptor for advanced glycation end-products (RAGE) and its response to hyperoxia in the neonatal rat lung. BMC Dev Biol. 2007; 7:15. PMC: 1828052. DOI: 10.1186/1471-213X-7-15. View

14.

Machahua C, Montes-Worboys A, Llatjos R, Escobar I, Dorca J, Molina-Molina M . Increased AGE-RAGE ratio in idiopathic pulmonary fibrosis. Respir Res. 2016; 17(1):144. PMC: 5097848. DOI: 10.1186/s12931-016-0460-2. View

15.

Gkogkolou P, Bohm M . Advanced glycation end products: Key players in skin aging?. Dermatoendocrinol. 2013; 4(3):259-70. PMC: 3583887. DOI: 10.4161/derm.22028. View

16.

Ott C, Jacobs K, Haucke E, Navarrete Santos A, Grune T, Simm A . Role of advanced glycation end products in cellular signaling. Redox Biol. 2014; 2:411-29. PMC: 3949097. DOI: 10.1016/j.redox.2013.12.016. View

17.

Pamplona R, Costantini D . Molecular and structural antioxidant defenses against oxidative stress in animals. Am J Physiol Regul Integr Comp Physiol. 2011; 301(4):R843-63. DOI: 10.1152/ajpregu.00034.2011. View

18.

Goldin A, Beckman J, Schmidt A, Creager M . Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation. 2006; 114(6):597-605. DOI: 10.1161/CIRCULATIONAHA.106.621854. View

19.

Di Pasquale E, Song B, Condorelli G . Generation of human cardiomyocytes: a differentiation protocol from feeder-free human induced pluripotent stem cells. J Vis Exp. 2013; (76). PMC: 3729284. DOI: 10.3791/50429. View

20.

Barandalla M, Colleoni S, Lazzari G . Differential Response of Human Embryonic Stem and Somatic Cells to Non-Cytotoxic Hydrogen Peroxide Exposure: An Attempt to Model the Effects of Oxidative Stress on the Early Embryo. Cell Dev Biol. 2016; 5(2). PMC: 5074058. DOI: 10.4172/2168-9296.1000177. View