ArticleJournal of molecular and cellular cardiology2010
Activation of the cardiac Na(+)-Ca(2+) exchanger by sorcin via the interaction of the respective Ca(2+)-binding domains.
Article in Journal of molecular and cellular cardiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 50 citations in OpenAlex.
- First-in-human controlled inhalation of thin graphene oxide nanosheets to study acute cardiorespiratory responses.Nature nanotechnology · 2024Trial
- Kinetic investigation of calcium-induced Sorcin aggregation by stopped-flow light scattering.The Biochemical journal · 2025Article
- Sorcin regulates alveolarization and airway tissue remodeling during lung morphogenesis.Cellular and molecular life sciences : CMLS · 2025Article
- Disruption of the sorcin‒PAX5 protein‒protein interaction induces ferroptosis by promoting the FBXL12-mediated ubiquitination of ALDH1A1 in pancreatic cancer.Journal of hematology & oncology · 2025Article
- Sorcin: mechanisms of action in cancer hallmarks, drug resistance and opportunities in therapeutics.Medical oncology (Northwood, London, England) · 2024Review
- Review
- Sorcin promotes migration in cancer and regulates the EGF-dependent EGFR signaling pathways.Cellular and molecular life sciences : CMLS · 2023Article
- AnnexinA7 promotes epithelial-mesenchymal transition by interacting with Sorcin and contributes to aggressiveness in hepatocellular carcinoma.Cell death & disease · 2021Article
- Sorcin Activates the Brain PMCA and Blocks the Inhibitory Effects of Molecular Markers of Alzheimer's Disease on the Pump Activity.International journal of molecular sciences · 2021Article
- Mitochondria: Insights into Crucial Features to Overcome Cancer Chemoresistance.International journal of molecular sciences · 2021Review
- Sorcin is an early marker of neurodegeneration, CaCell death & disease · 2020Article
- Roles of Sorcin in Drug Resistance in Cancer: One Protein, Many Mechanisms, for a Novel Potential Anticancer Drug Target.Cancers · 2020Review
- Unbalance Between Sarcoplasmic Reticulum CaFrontiers in physiology · 2019Review
- Sorcin a Potential Molecular Target for Cancer Therapy.Translational oncology · 2018Review
- Sorcin ablation plus β-adrenergic stimulation generate an arrhythmogenic substrate in mouse ventricular myocytes.Journal of molecular and cellular cardiology · 2018Article
- Binding of doxorubicin to Sorcin impairs cell death and increases drug resistance in cancer cells.Cell death & disease · 2017Article
- Negative Regulation of Hepatic Inflammation by the Soluble Resistance-Related Calcium-Binding ProteinFrontiers in immunology · 2017Article
- Sequestration of sorcin by aberrant forms of tau results in the defective calcium homeostasis.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2016Article
- Colchicine modulates calcium homeostasis and electrical property of HL-1 cells.Journal of cellular and molecular medicine · 2016Article
- Nonstructural 5A Protein of Hepatitis C Virus Regulates Soluble Resistance-Related Calcium-Binding Protein Activity for Viral Propagation.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Sorcin is a penta-EF-hand protein that interacts with intracellular target proteins after Ca(2+) binding. The sarcolemmal Na(+)/Ca(2+) exchanger (NCX1) may be an important sorcin target in cardiac muscle. In this study, RNAi knockdown of sorcin, purified sorcin or sorcin variants was employed in parallel measurements of: (i) NCX activity in isolated rabbit cardiomyocytes using electrophysiological techniques and (ii) sorcin binding to the NCX1 calcium binding domains (CBD1 and (iii) using surface plasmon resonance and gel overlay techniques. Sorcin is activated by Ca(2+) binding to the EF3 and EF2 regions, which are connected by the D helix. To investigate the importance of this region in the interaction with NCX1, three variants were examined: W105G and W99G, mutated respectively near EF3 and EF2, and E124A that does not bind Ca(2+) due to a mutation at EF3. Downregulation of sorcin decreased and supplementation with wt sorcin (3muM) increased NCX activity in isolated cardiomyocytes. The relative stimulatory effects of the sorcin variants were: W105G>wt sorcin>Sorcin Calcium Binding Domain (SCBD)>W99G>E124A. Sorcin binding to both CBD1 and 2 was observed. In the presence of 50microM Ca(2+), the interaction with CBD1 followed the order W105G>SCBD>wt sorcin>W99G>E124A. In sorcin, the interacting surface can be mapped on the C-terminal Ca(2+)-binding domain in the D helix region comprising W99. The fast association/dissociation rates that characterize the interaction of sorcin with CBD1 and 2 may permit complex formation/dissociation during an excitation/contraction cycle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.