ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Cell-surface actin binds plasminogen and modulates neurotransmitter release from catecholaminergic cells.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Rather a versatile multi-tool than a sword: an integral role of the plasminogen system in health and disease.Frontiers in immunology · 2026Review
- Neuronal conversion of single-chain tissue-type plasminogen activator into its two-chain form: implications in neurodevelopment, learning, and memory.Cell death & disease · 2025Article
- Oral bacteria induce IgA autoantibodies against a mesangial protein in IgA nephropathy model mice.Life science alliance · 2024Article
- The CDR3 region as the major driver of TREM-1 interaction with its ligands, anComputational and structural biotechnology journal · 2023Article
- Blood-Borne Microparticles Are an Inflammatory Stimulus in Type 2 Diabetes Mellitus.ImmunoHorizons · 2023Article
- Heparin binding proteins on monocyte cell surfaces regulates pre-inflammatory responses in diabetes.Journal of allergy and infectious diseases · 2023Article
- The ANXA2/S100A10 Complex-Regulation of the Oncogenic Plasminogen Receptor.Biomolecules · 2021Review
- Plasma gelsolin modulates the production and fate of IL-1β-containing microparticles following high-pressure exposure and decompression.Journal of applied physiology (Bethesda, Md. : 1985) · 2021Article
- Response of Leucine-Rich Repeat Domain-Containing Protein in Haemaphysalis longicornis to Babesia microti Infection and Its Ligand Identification.Infection and immunity · 2021Article
- Plasminogen Receptors and Fibrinolysis.International journal of molecular sciences · 2021Review
- Functions of the plasminogen receptor Plg-RJournal of thrombosis and haemostasis : JTH · 2020Review
- Extracellular Actin Is a Receptor forFrontiers in cellular and infection microbiology · 2018Article
- Astrocytes regulate the balance between plasminogen activation and plasmin clearance via cell-surface actin.Cell discovery · 2017Article
- New Insight on the Role of Plasminogen Receptor in Cancer Progression.Cancer growth and metastasis · 2015Review
- From plasminogen to plasmin: role of plasminogen receptors in human cancer.International journal of molecular sciences · 2014Review
- Inhibition of plasminogen activation by apo(a): role of carboxyl-terminal lysines and identification of inhibitory domains in apo(a).Journal of lipid research · 2014Article
- New insights into the role of Plg-RKT in macrophage recruitment.International review of cell and molecular biology · 2014Review
- Peptidergic regulation of plasminogen activator inhibitor-1 gene expression in vivo.Journal of thrombosis and haemostasis : JTH · 2013Article
- Plasminogen receptors: the first quarter century.Seminars in thrombosis and hemostasis · 2013Review
- β-Actin-binding complementarity-determining region 2 of variable heavy chain from monoclonal antibody C7 induces apoptosis in several human tumor cells and is protective against metastatic melanoma.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
An emerging area of research has documented a novel role for the plasminogen activation system in the regulation of neurotransmitter release. Prohormones, secreted by cells within the sympathoadrenal system, are processed by plasmin to bioactive peptides that feed back to inhibit secretagogue-stimulated release. Catecholaminergic cells of the sympathoadrenal system are prototypic prohormone-secreting cells. Processing of prohormones by plasmin is enhanced in the presence of catecholaminergic cells, and the enhancement requires binding of plasmin(ogen) to cellular receptors. Consequently, modulation of the local cellular fibrinolytic system of catecholaminergic cells results in substantial changes in catecholamine release. However, mechanisms for enhancing prohormone processing and cell-surface molecules mediating the enhancement on catecholaminergic cells have not been investigated. Here we show that plasminogen activation was enhanced >6.5-fold on catecholaminergic cells. Carboxypeptidase B treatment decreased cell-dependent plasminogen activation by approximately 90%, suggesting that the binding of plasminogen to proteins exposing C-terminal lysines on the cell surface is required to promote plasminogen activation. We identified catecholaminergic plasminogen receptors required for enhancing plasminogen activation, using a novel strategy combining targeted specific proteolysis using carboxypeptidase B with a proteomics approach using two-dimensional gel electrophoresis, radioligand blotting, and tandem mass spectrometry. Two major plasminogen-binding proteins that exposed C-terminal lysines on the cell surface contained amino acid sequences corresponding to beta/gamma-actin. An anti-actin monoclonal antibody inhibited cell-dependent plasminogen activation and also enhanced nicotine-dependent catecholamine release. Our results suggest that cell-surface-expressed forms of actin bind plasminogen, thereby promoting plasminogen activation and increased prohormone processing leading to inhibition of neurotransmitter release.
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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.