Evidence map›Paper›PMID 7535337›Full record

ArticleThe Journal of experimental medicine1995

Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes.

J Bohuslav, V Horejsí, C Hansmann, J Stöckl, U H Weidle, O Majdic, I Bartke, W Knapp, H Stockinger

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
8.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

74 citing papers in PubMed, 350 citations in OpenAlex.

  1. Review
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  5. Article
  6. Article
  7. βFrontiers in immunology · 2017
    Review
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  9. Article
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  12. Article
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  14. Article
  15. Review
  16. Role of integrins in regulating proteases to mediate extracellular matrix remodeling.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2012
    Article
  17. Article
  18. Article
  19. Review
  20. Review

14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

J BohuslavInstitute of Immunology, Vienna International Research Cooperation Center, SFI University of Vienna, Austria.
V Horejsí
C Hansmann
J Stöckl
U H Weidle
O Majdic
I Bartke
W Knapp
H Stockinger
Austrian Institute for International Affairs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycosylphosphatidylinositol (GPI)-anchored membrane protein urokinase plasminogen activator-receptor (uPA-R; CD87) is one of the key molecules involved in migration of leukocytes and tumor cells. uPA bound to uPA-R provides the cell proteolytic potential used for degradation of extracellular matrix. uPA-R is also involved in induction of cell adhesion and chemotaxis. Here, we provide a molecular explanation for these uPA-R-related cellular events. By size fractionation of monocyte lysate and affinity isolation on its natural ligand uPA, we demonstrate uPA-R as a component of a receptor complex of relatively large size. Reprecipitation and immunoblotting techniques allowed us to detect the protein tyrosine kinases (PTKs) p60fyn, p53/56lyn, p58/64hck, and p59fgr as components of this "uPA-R complex". Activation of monocytes even with enzymatically inactivated uPA resulted in induction of tyrosine phosphorylation, suggesting modulation of uPA-R-associated PTKs upon ligand binding. In spite of their presence in large complexes, we did not find the GPI-linked proteins CD14, CD58, and CD59 in the uPA-R complex, which indicates the presence of different receptor domains containing GPI-linked proteins in monocytes. However, we identified the leukocyte integrins LFA-1 and CR3 as components of the uPA-R complex as indicated by coisolation of these molecules, as well as by cocapping and comodulation of uPA-R and leukocyte integrins on the monocyte surface. The assemblage of uPA-R, PTKs and membrane spanning beta 2-integrins in one receptor complex indicates functional cooperation. In regard to the involvement of these molecules in pericellular proteolysis, signal transduction, as well as adhesion and chemotactic movement, we suggest uPA-R complex as a potential cellular device for cell migration.

Indexed as

Signal Transductionsrc-Family KinasesAntigens, CDCD18 AntigensCell AdhesionCell MovementHumansIntegrinsLymphocyte Function-Associated Antigen-1Macromolecular SubstancesMacrophage-1 AntigenMonocytesMultienzyme ComplexesPhosphorylationProtein Processing, Post-TranslationalProtein-Tyrosine KinasesAntigens, CDCD18 AntigensFYN protein, humanHCK protein, humanIntegrinsLymphocyte Function-Associated Antigen-1lyn protein-tyrosine kinaseMacromolecular SubstancesMacrophage-1 AntigenMultienzyme ComplexesPLAUR protein, humanProtein-Tyrosine KinasesProto-Oncogene Proteinsproto-oncogene proteins c-fgrProto-Oncogene Proteins c-fynProto-Oncogene Proteins c-hckReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceReceptors, Urokinase Plasminogen Activatorsrc-Family Kinases

Identifiers

PMID7535337
PMCPMC2191946
OpenAlexW2042155824

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.