Evidence map›Paper›PMID 23997214›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2013

Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking.

Jaganathan Subramani, Mallika Ghosh, M Mamunur Rahman, Leslie A Caromile, Claire Gerber, Karim Rezaul, David K Han, Linda H Shapiro

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

37 citing papers in PubMed, 55 citations in OpenAlex.

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  16. Coronavirus Receptors as Immune Modulators.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Review
  17. Review
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  19. Review
  20. Article
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

8 authors at 1 institution in 1 country.

Jaganathan SubramaniCenter for Vascular Biology, University of Connecticut Health Center, Farmington, CT 06030.
Mallika Ghosh
M Mamunur Rahman
Leslie A Caromile
Claire Gerber
Karim Rezaul
David K Han
Linda H Shapiro
UConn Health · US

Funding

Vascular Pathophysiology and History Core (VPHC)P01HL070694 · NHLBI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI COWAN, ANN E. · 2002 to 2013
$17.5M
CD13 as a Biomarker for NSAIDS Chemoprevention of Breast CancerR01CA106345 · NCI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SHAPIRO, LINDA H · 2005 to 2009
$1.4M
NCI NIH HHS CA-106345NCI NIH HHS R01 CA106345NHLBI NIH HHS HL-70694NHLBI NIH HHS P01 HL070694
6 · The paper itself

Abstract

CD13 is a large cell surface peptidase expressed on the monocytes and activated endothelial cells that is important for homing to and resolving the damaged tissue at sites of injury. We showed previously that cross-linking of human monocytic CD13 with activating Abs induces strong adhesion to endothelial cells in a tyrosine kinase- and microtubule-dependent manner. In the current study, we examined the molecular mechanisms underlying these observations in vitro and in vivo. We found that cross-linking of CD13 on U937 monocytic cells induced phosphorylation of a number of proteins, including Src, FAK, and ERK, and inhibition of these abrogated CD13-dependent adhesion. We found that CD13 itself was phosphorylated in a Src-dependent manner, which was an unexpected finding because its 7-aa cytoplasmic tail was assumed to be inert. Furthermore, CD13 was constitutively associated with the scaffolding protein IQGAP1, and CD13 cross-linking induced complex formation with the actin-binding protein α-actinin, linking membrane-bound CD13 to the cytoskeleton, further supporting CD13 as an inflammatory adhesion molecule. Mechanistically, mutation of the conserved CD13 cytoplasmic tyrosine to phenylalanine abrogated adhesion; Src, FAK, and ERK phosphorylation; and cytoskeletal alterations upon Ab cross-linking. Finally, CD13 was phosphorylated in isolated murine inflammatory peritoneal exudate cells, and adoptive transfer of monocytic cell lines engineered to express the mutant CD13 were severely impaired in their ability to migrate into the inflamed peritoneum, confirming that CD13 phosphorylation is relevant to inflammatory cell trafficking in vivo. Therefore, this study identifies CD13 as a novel, direct activator of intracellular signaling pathways in pathophysiological conditions.

Indexed as

AnimalsCD13 AntigensCell AdhesionCell LineCell MovementExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesInflammationMiceMice, KnockoutMonocytesPhosphorylationPlakinsProtein BindingSignal Transductionsrc-Family KinasesCD13 AntigensExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesPlakinssrc-Family Kinases

Identifiers

PMID23997214
PMCPMC3810388
OpenAlexW1567059590

What OpenQuestion holds

Textmetadata
LicenceTDM
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.