ArticleThe Journal of biological chemistry2009
Characterization of calumenin-SERCA2 interaction in mouse cardiac sarcoplasmic reticulum.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 58 citations in OpenAlex.
- Calumenin, A Calcium-Binding Modulatory Protein, Effective in Pathological Calcifications and Cancers, With Therapeutic Application Promise.FASEB bioAdvances · 2025Review
- Environment-induced heat stress causes ventricular-dependent biochemical changes in the heart in female pigs.Physiological reports · 2025Article
- Mechanism of myocardial damage induced by doxorubicinWorld journal of cardiology · 2025Article
- Characterize direct protein interactions with enrichable, cleavable and latent bioreactive unnatural amino acids.Nature communications · 2024Article
- Pan-Cancer Screening and Validation of CALU's Role in EMT Regulation and Tumor Microenvironment in Triple-Negative Breast Cancer.Journal of inflammation research · 2024Article
- Physiology of intracellular calcium buffering.Physiological reviews · 2023Review
- Spatial and Functional Crosstalk between the Mitochondrial NaInternational journal of molecular sciences · 2022Article
- Review
- Upregulation of miR-335-5p Contributes to Right Ventricular Remodeling via Calumenin in Pulmonary Arterial Hypertension.BioMed research international · 2022Article
- CaFaculty reviews · 2022Review
- Update on Calcium Signaling in Cystic Fibrosis Lung Disease.Frontiers in pharmacology · 2021Review
- Calumenin-1 Interacts with Climp63 to Cooperatively Determine the Luminal Width and Distribution of Endoplasmic Reticulum Sheets.iScience · 2019Article
- Structures of the heart specific SERCA2a CaThe EMBO journal · 2019Article
- Creatine phosphate disodium salt protects against Dox-induced cardiotoxicity by increasing calumenin.Medical molecular morphology · 2018Article
- Calumenin relieves cardiac injury by inhibiting ERS-initiated apoptosis during viral myocarditis.International journal of clinical and experimental pathology · 2017Review
- Ca-Dependent Folding of Human Calumenin.PloS one · 2016Article
- Total Flavonoids of Astragalus Plays a Cardioprotective Role in Viral Myocarditis.Acta Cardiologica Sinica · 2016Article
- The Golgi apparatus is a functionally distinct Ca2+ store regulated by the PKA and Epac branches of the β1-adrenergic signaling pathway.Science signaling · 2015Article
- Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.Fish physiology and biochemistry · 2015Article
- Circulating Pneumolysin Is a Potent Inducer of Cardiac Injury during Pneumococcal Infection.PLoS pathogens · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calumenin is a multiple EF-hand Ca(2+)-binding protein localized in the sarcoplasmic reticulum (SR) with C-terminal SR retention signal HDEF. Recently, we showed evidence that calumenin interacts with SERCA2 in rat cardiac SR (Sahoo, S. K., and Kim, D. H. (2008) Mol. Cells 26, 265-269). The present study was undertaken to further characterize the association of calumenin with SERCA2 in mouse heart by various gene manipulation approaches. Immunocytochemical analysis showed that calumenin and SERCA2 were partially co-localized in HL-1 cells. Knockdown (KD) of calumenin was conducted in HL-1 cells and 80% reduction of calumenin did not induce any expressional changes of other Ca(2+)-cycling proteins. But it enhanced Ca(2+) transient amplitude and showed shortened time to reach peak and decreased time to reach 50% of baseline. Oxalate-supported Ca(2+) uptake showed increased Ca(2+) sensitivity of SERCA2 in calumenin KD HL-1 cells. Calumenin and SERCA2 interaction was significantly lower in the presence of thapsigargin, vanadate, or ATP, as compared with 1.3 mum Ca(2+), suggesting that the interaction is favored in the E1 state of SERCA2. A glutathione S-transferase-pulldown assay of calumenin deletion fragments and SERCA2 luminal domains suggested that regions of 132-222 amino acids of calumenin and 853-892 amino acids of SERCA2-L4 are the major binding partners. On the basis of our in vitro binding data and available information on three-dimensional structure of Ca(2+)-ATPases, a molecular model was proposed for the interaction between calumenin and SERCA2. Taken together, the present results suggest that calumenin is a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca(2+)-cycling of cardiomyocytes.
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