ArticleThe Journal of biological chemistry2011
The novel plasminogen receptor, plasminogen receptor(KT) (Plg-R(KT)), regulates catecholamine release.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Liver-derived plasminogen mediates muscle stem cell expansion during caloric restriction through the plasminogen receptor Plg-RCell reports · 2024Article
- Plg-RBiomolecules · 2022Article
- The plasminogen receptor Plg-RJournal of thrombosis and haemostasis : JTH · 2022Article
- Assessing Plasmin Generation in Health and Disease.International journal of molecular sciences · 2021Review
- Polycystic Ovary Syndrome and Risk of Five Common Psychiatric Disorders Among European Women: A Two-Sample Mendelian Randomization Study.Frontiers in genetics · 2021Article
- The plasminogen receptor, Plg-RCell death & disease · 2020Article
- The multifaceted role of plasminogen in inflammation.Cellular signalling · 2020Review
- Functions of the plasminogen receptor Plg-RJournal of thrombosis and haemostasis : JTH · 2020Review
- Neuroendocrine Targeting of Tissue Plasminogen Activator (t-PA).Journal of neurological disorders & stroke · 2020Article
- Plasminogen and the Plasminogen Receptor, Plg-RFrontiers in immunology · 2019Article
- The plasminogen receptorJournal of thrombosis and haemostasis : JTH · 2018Article
- Genetic risk variants for metabolic traits in Arab populations.Scientific reports · 2017Article
- Deficiency of plasminogen receptor, Plg-RJournal of thrombosis and haemostasis : JTH · 2017Article
- Fibrinolysis and the control of blood coagulation.Blood reviews · 2015Review
- New insights into the role of Plg-RKT in macrophage recruitment.International review of cell and molecular biology · 2014Review
- Plasminogen receptors: the first quarter century.Seminars in thrombosis and hemostasis · 2013Review
- Characterization of plasminogen binding to NB4 promyelocytic cells using monoclonal antibodies against receptor-induced binding sites in cell-bound plasminogen.Journal of biomedicine & biotechnology · 2012Article
- Cell surface remodeling by plasmin: a new function for an old enzyme.Journal of biomedicine & biotechnology · 2012Review
- The plasminogen activation system and the regulation of catecholaminergic function.Journal of biomedicine & biotechnology · 2012Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Neurotransmitter release by catecholaminergic cells is negatively regulated by prohormone cleavage products formed from plasmin-mediated proteolysis. Here, we investigated the expression and subcellular localization of Plg-R(KT), a novel plasminogen receptor, and its role in catecholaminergic cell plasminogen activation and regulation of catecholamine release. Prominent staining with anti-Plg-R(KT) mAb was observed in adrenal medullary chromaffin cells in murine and human tissue. In Western blotting, Plg-R(KT) was highly expressed in bovine adrenomedullary chromaffin cells, human pheochromocytoma tissue, PC12 pheochromocytoma cells, and murine hippocampus. Expression of Plg-R(KT) fused in-frame to GFP resulted in targeting of the GFP signal to the cell membrane. Phase partitioning, co-immunoprecipitation with urokinase-type plasminogen activator receptor (uPAR), and FACS analysis with antibody directed against the C terminus of Plg-R(KT) were consistent with Plg-R(KT) being an integral plasma membrane protein on the surface of catecholaminergic cells. Cells stably overexpressing Plg-R(KT) exhibited substantial enhancement of plasminogen activation, and antibody blockade of non-transfected PC12 cells suppressed plasminogen activation. In functional secretion assays, nicotine-evoked [(3)H]norepinephrine release from cells overexpressing Plg-R(KT) was markedly decreased (by 51 ± 2%, p < 0.001) when compared with control transfected cells, and antibody blockade increased [(3)H]norepinephrine release from non-transfected PC12 cells. In summary, Plg-R(KT) is present on the surface of catecholaminergic cells and functions to stimulate plasminogen activation and modulate catecholamine release. Plg-R(KT) thus represents a new mechanism and novel control point for regulating the interface between plasminogen activation and neurosecretory cell function.
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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.