ArticleThe Journal of biological chemistry2011
Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 62 citations in OpenAlex.
- Calpain-2 facilitates infection of the intracellular bacteria Listeria monocytogenes and invasion intestinal immune barrier by impairing nitric oxide homeostasis.Journal of advanced research · 2026Article
- Review
- Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025Review
- Comprehensive Analysis of Selenium Metabolism and Selenoproteins-Associated Gene Signatures in Ulcerative Colitis.Journal of inflammation research · 2025Article
- Selenoprotein K enhances STING oligomerization to facilitate antiviral response.PLoS pathogens · 2023Article
- Selenoprotein K Is Essential for the Migration and Phagocytosis of Immature Dendritic Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Functional genome-wide short hairpin RNA library screening identifies key molecules for extracellular vesicle secretion from microglia.Cell reports · 2022Article
- Prominent Effects of Berbamine Hydrochloride on Alzheimer's Disease Model Mice.Frontiers in pharmacology · 2022Article
- Effect of Selenium and Peroxynitrite on Immune Function of Immature Dendritic Cells in Humans.Medical science monitor : international medical journal of experimental and clinical research · 2021Article
- Molecular Mechanisms by Which Selenoprotein K Regulates Immunity and Cancer.Biological trace element research · 2019Review
- Use of a Mouse Model and Human Umbilical Vein Endothelial Cells to Investigate the Effect of Arsenic Exposure on Vascular Endothelial Function and the Associated Role of Calpains.Environmental health perspectives · 2019Article
- Selenoprotein K deficiency inhibits melanoma by reducing calcium flux required for tumor growth and metastasis.Oncotarget · 2018Article
- Calpain-2 inhibitor treatment preferentially reduces tumor progression for human colon cancer cells expressing highest levels of this enzyme.Cancer medicine · 2018Article
- Calpain Inhibition Attenuates Adipose Tissue Inflammation and Fibrosis in Diet-induced Obese Mice.Scientific reports · 2017Article
- Comparison of the protein expression of calpain-1, calpain-2, calpastatin and calmodulin between gastric cancer and normal gastric mucosa.Oncology letters · 2017Article
- Selenium nanoparticles decorated with Ulva lactuca polysaccharide potentially attenuate colitis by inhibiting NF-κB mediated hyper inflammation.Journal of nanobiotechnology · 2017Article
- Selenoprotein K regulation of palmitoylation and calpain cleavage of ASAP2 is required for efficient FcγR-mediated phagocytosis.Journal of leukocyte biology · 2017Article
- Critical role of calpain in inflammation.Biomedical reports · 2016Article
- Adiposity-Dependent Regulatory Effects on Multi-tissue Transcriptomes.American journal of human genetics · 2016Article
- Leukocyte Calpain Deficiency Reduces Angiotensin II-Induced Inflammation and Atherosclerosis But Not Abdominal Aortic Aneurysms in Mice.Arteriosclerosis, thrombosis, and vascular biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Calpains are proteolytic enzymes that modulate cellular function through cleavage of targets, thereby modifying their actions. An important role is emerging for calpains in regulating inflammation and immune responses, although specific mechanisms by which this occurs have not been clearly defined. In this study, we identify a novel target of calpain, selenoprotein K (SelK), which is an endoplasmic reticulum transmembrane protein important for Ca(2+) flux in immune cells. Calpain-mediated cleavage of SelK was detected in myeloid cells (macrophages, neutrophils, and dendritic cells) but not in lymphoid cells (B and T cells). Both m- and μ-calpain were capable of cleaving immunoprecipitated SelK, but m-calpain was the predominant isoform expressed in mouse immune cells. Consistent with these results, specific inhibitors were used to show that only m-calpain cleaved SelK in macrophages. The cleavage site in SelK was identified between Arg(81) and Gly(82) and the resulting truncated SelK was shown to lack selenocysteine, the amino acid that defines selenoproteins. Resting macrophages predominantly expressed cleaved SelK and, when activated through different Toll-like receptors (TLRs), SelK cleavage was inhibited. We found that decreased calpain cleavage was due to TLR-induced up-regulation of the endogenous inhibitor, calpastatin. TLR-induced calpastatin expression not only inhibited SelK cleavage, but cleavage of another calpain target, talin. Moreover, the expression of the calpain isoforms and calpastatin in macrophages were different from T and B cells. Overall, our findings identify SelK as a novel calpain target and reveal dynamic changes in the calpain/calpastatin system during TLR-induced activation of macrophages.
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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.