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Article

Intracellular Protein S-Nitrosylation—A Cells Response to Extracellular S100B and RAGE Receptor

1
Mass Spectrometry Laboratory, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
2
Laboratory of Cell Biophysics, Nencki Institute of Experimental Biology, Polish Academy of Science, Pasteura 3, 02-093 Warsaw, Poland
3
Clinical Research Centre, Medical University of Białystok, Kilińskiego 1, 15-369 Białystok, Poland
*
Author to whom correspondence should be addressed.
Academic Editors: Marcus O. W. Grimm and Lukasz Kurgan
Biomolecules 2022, 12(5), 613; https://doi.org/10.3390/biom12050613
Received: 22 November 2021 / Revised: 18 February 2022 / Accepted: 9 March 2022 / Published: 20 April 2022
(This article belongs to the Section Bioinformatics and Systems Biology)
Human S100B is a small, multifunctional protein. Its activity, inside and outside cells, contributes to the biology of the brain, muscle, skin, and adipocyte tissues. Overexpression of S100B occurs in Down Syndrome, Alzheimer’s disease, Creutzfeldt–Jakob disease, schizophrenia, multiple sclerosis, brain tumors, epilepsy, melanoma, myocardial infarction, muscle disorders, and sarcopenia. Modulating the activities of S100B, related to human diseases, without disturbing its physiological functions, is vital for drug and therapy design. This work focuses on the extracellular activity of S100B and one of its receptors, the Receptor for Advanced Glycation End products (RAGE). The functional outcome of extracellular S100B, partially, depends on the activation of intracellular signaling pathways. Here, we used Biotin Switch Technique enrichment and mass-spectrometry-based proteomics to show that the appearance of the S100B protein in the extracellular milieu of the mammalian Chinese Hamster Ovary (CHO) cells, and expression of the membrane-bound RAGE receptor, lead to changes in the intracellular S-nitrosylation of, at least, more than a hundred proteins. Treatment of the wild-type CHO cells with nanomolar or micromolar concentrations of extracellular S100B modulates the sets of S-nitrosylation targets inside cells. The cellular S-nitrosome is tuned differently, depending on the presence or absence of stable RAGE receptor expression. The presented results are a proof-of-concept study, suggesting that S-nitrosylation, like other post-translational modifications, should be considered in future research, and in developing tailored therapies for S100B and RAGE receptor-related diseases. View Full-Text
Keywords: extracellular S100B; receptor RAGE; S-nitrosome; SNOSID; mass spectrometry extracellular S100B; receptor RAGE; S-nitrosome; SNOSID; mass spectrometry
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MDPI and ACS Style

Zaręba-Kozioł, M.; Burdukiewicz, M.; Wysłouch-Cieszyńska, A. Intracellular Protein S-Nitrosylation—A Cells Response to Extracellular S100B and RAGE Receptor. Biomolecules 2022, 12, 613. https://doi.org/10.3390/biom12050613

AMA Style

Zaręba-Kozioł M, Burdukiewicz M, Wysłouch-Cieszyńska A. Intracellular Protein S-Nitrosylation—A Cells Response to Extracellular S100B and RAGE Receptor. Biomolecules. 2022; 12(5):613. https://doi.org/10.3390/biom12050613

Chicago/Turabian Style

Zaręba-Kozioł, Monika, Michał Burdukiewicz, and Aleksandra Wysłouch-Cieszyńska. 2022. "Intracellular Protein S-Nitrosylation—A Cells Response to Extracellular S100B and RAGE Receptor" Biomolecules 12, no. 5: 613. https://doi.org/10.3390/biom12050613

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