GSNOR regulates cardiomyocyte differentiation and maturation through protein S-nitrosylation.

J Cardiovasc Aging

Institute for Transformative Molecular Medicine, Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.

Published: October 2021

S-nitrosoglutathione reductase (GSNOR) is a denitrosylase enzyme responsible for reverting protein S-nitrosylation (SNO). In this issue, Salerno provide evidence that GSNOR deficiency - and thus elevated protein S-nitrosylation - accelerates cardiomyocyte differentiation and maturation of induced pluripotent stem cells (iPSCs). GSNOR inhibition (GSNOR iPSCs) expedites the epithelial-mesenchymal transition (EMT) and promotes cardiomyocyte progenitor cell proliferation, differentiation, and migration. These findings are consistent with emerging roles for protein S-nitrosylation in developmental biology (including cardiomyocyte development), aging/longevity, and cancer.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8594876PMC
http://dx.doi.org/10.20517/jca.2021.25DOI Listing

Publication Analysis

Top Keywords

protein s-nitrosylation
16
cardiomyocyte differentiation
8
differentiation maturation
8
gsnor
5
gsnor regulates
4
cardiomyocyte
4
regulates cardiomyocyte
4
protein
4
maturation protein
4
s-nitrosylation
4

Similar Publications

Metaplastic breast cancer (MpBC) is a highly chemoresistant subtype of breast cancer with no standardized therapy options. A clinical study in anthracycline-refractory MpBC patients suggested that nitric oxide synthase (NOS) inhibitor NG-monomethyl-l-arginine (L-NMMA) may augment anti-tumor efficacy of taxane. We report that NOS blockade potentiated response of human MpBC cell lines and tumors to phosphoinositide 3-kinase (PI3K) inhibitor alpelisib and taxane.

View Article and Find Full Text PDF

S-nitrosylation (SNO) modification, a nitric oxide (NO)-mediated post-translational modification (PTM) of proteins, plays an important role in protein microstructure, degradation, activity, and stability. Due to the presence of reducing agents, the SNO modification process mediated by NO derivatives is often reversible and unstable. This reversible transformation between SNO modification and denitrification often influences the structure, activity, and function of proteins.

View Article and Find Full Text PDF

Introduction: Cerebrovascular dysfunction occurs in Alzheimer's disease (AD), impairing hemodynamic regulation. Large conductance Ca-activated K channels (BK) regulate cerebrovascular reactivity and are impaired in AD. BK activity depends on intracellular Ca (Ca sparks) and nitro-oxidative post-translational modifications.

View Article and Find Full Text PDF

Hypoxia Microenvironment Preconditioning Attenuated Myocardial Ischemia-Reperfusion Injury via Stc1-Mediating Cardiomyocyte Self-Protection and Neutrophil Polarization.

Adv Sci (Weinh)

December 2024

Department of Cardiology, State Key Laboratory of Organ Failure Research, Nanfang Hospital, Southern Medical University, 1838 North Guangzhou Avenue, Guangzhou, 510515, China.

Ischemic preconditioning (IPC) therapy application to attenuate myocardial ischemia-reperfusion (MI/R) injury in clinical practice remains challenging. The secretome, derived from hypoxia-preconditioned cardiomyocytes (SHPC), potentially mimics the IPC microenvironment and facilitates IPC clinical translation. This study aims to determine whether SHPC can be a feasible alternative to IPC for attenuating MI/R injury, and to identify the functional factor of SHPC.

View Article and Find Full Text PDF

Dual BACH1 regulation by complementary SCF-type E3 ligases.

Cell

December 2024

Discovery Sciences, Novartis Biomedical Research, Basel, Switzerland. Electronic address:

Broad-complex, tramtrack, and bric-à-brac domain (BTB) and CNC homolog 1 (BACH1) is a key regulator of the cellular oxidative stress response and an oncogene that undergoes tight post-translational control by two distinct F-box ubiquitin ligases, SCF and SCF. However, how both ligases recognize BACH1 under oxidative stress is unclear. In our study, we elucidate the mechanism by which FBXO22 recognizes a quaternary degron in a domain-swapped β-sheet of the BACH1 BTB dimer.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!