ArticleMolecular and cellular biology2007
Double knockouts reveal that protein tyrosine phosphatase 1B is a physiological target of calpain-1 in platelets.
Article in Molecular and cellular biology, 2007. 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, 70 citations in OpenAlex.
- Activating pyruvate kinase improves red blood cell integrity by reducing band 3 tyrosine phosphorylation.Blood advances · 2024Article
- Protein tyrosine phosphatase 1B in metabolic diseases and drug development.Nature reviews. Endocrinology · 2024Review
- Human Protein Tyrosine Phosphatase 1B (PTP1B): From Structure to Clinical Inhibitor Perspectives.International journal of molecular sciences · 2022Review
- Rapid degradation of protein tyrosine phosphatase 1B in sickle cells: Possible contribution to sickle cell membrane weakening.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Mechanisms of reduced leptin-mediated satiety signaling during obesity.International journal of obesity (2005) · 2022Article
- Calpain-1 inhibition attenuates in vivo thrombosis in a humanized model of sickle cell disease.Thrombosis research · 2022Article
- CAPN1 promotes malignant behavior and erlotinib resistance mediated by phosphorylation of c-Met and PIK3R2 via degrading PTPN1 in lung adenocarcinoma.Thoracic cancer · 2020Article
- Impaired Glycoprotein VI-Mediated Signaling and Platelet Functional Responses in CD45 Knockout Mice.Thrombosis and haemostasis · 2019Article
- Targeting Tyrosine Phosphatases by 3-Bromopyruvate Overcomes Hyperactivation of Platelets from Gastrointestinal Cancer Patients.Journal of clinical medicine · 2019Article
- Comparative Analysis of Microfluidics Thrombus Formation in Multiple Genetically Modified Mice: Link to Thrombosis and Hemostasis.Frontiers in cardiovascular medicine · 2019Article
- CALPA-IN NF1.Oncotarget · 2018Article
- Calpain-1 regulates platelet function in a humanized mouse model of sickle cell disease.Thrombosis research · 2017Article
- Protein Phosphotyrosine Phosphatase 1B (PTP1B) in Calpain-dependent Feedback Regulation of Vascular Endothelial Growth Factor Receptor (VEGFR2) in Endothelial Cells: IMPLICATIONS IN VEGF-DEPENDENT ANGIOGENESIS AND DIABETIC WOUND HEALING.The Journal of biological chemistry · 2017Article
- Regulation of platelet-activating factor-mediated protein tyrosine phosphatase 1B activation by a Janus kinase 2/calpain pathway.PloS one · 2017Article
- Roles of integrin β3 cytoplasmic tail in bidirectional signal transduction in a trans-dominant inhibition model.Frontiers of medicine · 2016Article
- Receptor-Interacting Protein 140 Orchestrates the Dynamics of Macrophage M1/M2 Polarization.Journal of innate immunity · 2016Article
- Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors.Acta pharmaceutica Sinica. B · 2015Review
- Role of sodium tungstate as a potential antiplatelet agent.Drug design, development and therapy · 2015Article
- Calpain-1 contributes to IgE-mediated mast cell activation.Journal of immunology (Baltimore, Md. : 1950) · 2014Article
- Reactive oxygen species play a critical role in collagen-induced platelet activation via SHP-2 oxidation.Antioxidants & redox signaling · 2014Article
Corrections and comments
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Authors and funding
5 authors at 5 institutions in 1 country.
Funding
Abstract
Calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal organization, cell proliferation, apoptosis, cell motility, and hemostasis. Gene targeting was used to evaluate the physiological function of mouse calpain-1 and establish that its inactivation results in reduced platelet aggregation and clot retraction potentially by causing dephosphorylation of platelet proteins. Here, we report that calpain-1 null (Capn1-/-) platelets accumulate protein tyrosine phosphatase 1B (PTP1B), which correlates with enhanced tyrosine phosphatase activity and dephosphorylation of multiple substrates. Treatment of Capn1-/- platelets with bis(N,N-dimethylhydroxamido)hydroxooxovanadate, an inhibitor of tyrosine phosphatases, corrected the aggregation defect and recovered impaired clot retraction. More importantly, platelet aggregation, clot retraction, and tyrosine dephosphorylation defects were rescued in the double knockout mice lacking both calpain-1 and PTP1B. Further evaluation of mutant mice by the ferric chloride-induced arterial injury model suggests that the Capn1-/- mice are relatively resistant to thrombosis in vivo. Together, our results demonstrate that PTP1B is a physiological target of calpain-1 and suggest that a similar mechanism may regulate calpain-1-mediated tyrosine dephosphorylation in other cells.
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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.