ArticleThe Journal of cell biology1996
Ligand-induced protease receptor translocation into caveolae: a mechanism for regulating cell surface proteolysis of the tissue factor-dependent coagulation pathway.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed, 207 citations in OpenAlex.
- Manipulation of tissue factor-mediated basal PAR-2 signalling on macrophages determines sensitivity for IFNγ responsiveness and significantly modifies the phenotype of murine DTH.Frontiers in immunology · 2022Article
- Extracellular Vesicles and Thrombosis: Update on the Clinical and Experimental Evidence.International journal of molecular sciences · 2021Review
- De-Palmitoylation of Tissue Factor Regulates Its Activity, Phosphorylation and Cellular Functions.Cancers · 2021Article
- Activation of β1 integrins and caveolin-1 by TF/FVIIa promotes IGF-1R signaling and cell survival.Apoptosis : an international journal on programmed cell death · 2020Article
- Article
- Role of Cell Surface Lipids and Thiol-Disulphide Exchange Pathways in Regulating the Encryption and Decryption of Tissue Factor.Thrombosis and haemostasis · 2019Review
- Article
- Sphingomyelin encrypts tissue factor: ATP-induced activation of A-SMase leads to tissue factor decryption and microvesicle shedding.Blood advances · 2017Article
- Extracellular Thiol Isomerases and Their Role in Thrombus Formation.Antioxidants & redox signaling · 2016Review
- Extracellular vesicles, tissue factor, cancer and thrombosis - discussion themes of the ISEV 2014 Educational Day.Journal of extracellular vesicles · 2015Article
- How it all starts: Initiation of the clotting cascade.Critical reviews in biochemistry and molecular biology · 2015Review
- Biology of tissue factor pathway inhibitor.Blood · 2014Review
- Cellular expression and biological activities of alternatively spliced forms of tissue factor pathway inhibitor.Current opinion in hematology · 2013Review
- Comparison of the inhibitory activities of human tissue factor pathway inhibitor (TFPI)α and TFPIβ.Journal of thrombosis and haemostasis : JTH · 2013Article
- Article
- Regulation of tissue factor coagulant activity on cell surfaces.Journal of thrombosis and haemostasis : JTH · 2012Review
- Caveolae optimize tissue factor-Factor VIIa inhibitory activity of cell-surface-associated tissue factor pathway inhibitor.The Biochemical journal · 2012Article
- TFPIβ is the GPI-anchored TFPI isoform on human endothelial cells and placental microsomes.Blood · 2012Article
- Tissue factor: mechanisms of decryption.Frontiers in bioscience (Elite edition) · 2012Review
- Posttranslational modifications of tissue factor.Frontiers in bioscience (Elite edition) · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The ability to regulate proteolytic functions is critical to cell biology. We describe events that regulate the initiation of the coagulation cascade on endothelial cell surfaces. The transmembrane protease receptor tissue factor (TF) triggers coagulation by forming an enzymatic complex with the serine protease factor VIIa (VIIa) that activates substrate factor X to the protease factor Xa (Xa). Feedback inhibition of the TF-VIIa enzymatic complex is achieved by the formation of a quaternary complex of TF-VIIa, Xa, and the Kunitz-type inhibitor tissue factor pathway inhibitor (TFPI). Concomitant with the downregulation of TF-VIIa function on endothelial cells, we demonstrate by immunogold EM that TF redistributes to caveolae. Consistently, TF translocates from the Triton X-100-soluble membrane fractions to low-density, detergent-insoluble microdomains that inefficiently support TF-VIIa proteolytic function. Downregulation of TF-VIIa function is dependent on quaternary complex formation with TFPI that is detected predominantly in detergent-insoluble microdomains. Partitioning of TFPI into low-density fractions results from the association of the inhibitor with glycosyl phosphatidylinositol anchored binding sites on external membranes. Free Xa is not efficiently bound by cell-associated TFPI; hence, we propose that the transient ternary complex of TF-VIIa with Xa supports translocation and assembly with TFPI in glycosphingolipid-rich microdomains. The redistribution of TF provides evidence for an assembly-dependent translocation of the inhibited TF initiation complex into caveolae, thus implicating caveolae in the regulation of cell surface proteolytic activity.
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What OpenQuestion holds
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.