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Coordinated expression of DNAM-1 and LFA-1 in educated NK cells
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2015 (English)In: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 194, no 9, 4518-4527 p.Article in journal (Refereed) Published
Abstract [en]

The functional capacity of NK cells is dynamically tuned by integrated signals from inhibitory and activating cell surface receptors in a process termed NK cell education. However, the understanding of the cellular and molecular mechanisms behind this functional tuning is limited. In this study, we show that the expression of the adhesion molecule and activation receptor DNAX accessory molecule 1 (DNAM-1) correlates with the quantity and quality of the inhibitory input by HLA class I-specific killer cell Ig-like receptors and CD94/NKG2A as well as with the magnitude of functional responses. Upon target cell recognition, the conformational state of LFA-1 changed in educated NK cells, associated with rapid colocalization of both active LFA-1 and DNAM-1 at the immune synapse. Thus, the coordinated expression of LFA-1 and DNAM-1 is a central component of NK cell education and provides a potential mechanism for controlling cytotoxicity by functionally mature NK cells.

Place, publisher, year, edition, pages
2015. Vol. 194, no 9, 4518-4527 p.
Keyword [en]
alpha interferon, CD94 antigen, cell adhesion molecule, cell adhesion molecule LFA 1, DNAX accessory molecule 1, HLA E antigen, interleukin 12, interleukin 15, interleukin 18, interleukin 2, interleukin 21, killer cell immunoglobulin like receptor, natural killer cell receptor, natural killer cell receptor NKG2A, natural killer cell receptor NKG2D, unclassified drug, antigen expression, antigen presentation, antigen presenting cell, antigen recognition, Article, cell maturation, cellular distribution, conformational transition, controlled study, cytokine production, cytokine release, cytolysis, effector cell, human, human cell, immunological memory, immunological synapse, immunoregulation, lymphocyte differentiation, natural killer cell, priority journal, protein determination, protein expression, protein function, protein localization, protein protein interaction, protein targeting, receptor intrinsic activity, signal transduction
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URN: urn:nbn:se:kth:diva-167771DOI: 10.4049/jimmunol.1401972ISI: 000353727400050PubMedID: 25825444ScopusID: 2-s2.0-84928474098OAI: diva2:814282
Swedish Research CouncilSwedish Childhood Cancer FoundationSwedish Cancer SocietyThe Karolinska Institutet's Research FoundationWenner-Gren FoundationsEU, European Research CouncilScience for Life Laboratory - a national resource center for high-throughput molecular bioscience

QC 20150526

Available from: 2015-05-26 Created: 2015-05-22 Last updated: 2015-06-12Bibliographically approved

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Önfelt, Björn
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Cell PhysicsScience for Life Laboratory, SciLifeLab
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