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Differential inside...
Differential inside-out activation of β2 integrins by leukotriene B4 and fMLP in human neutrophils
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- Patcha Brodin, Veronika (author)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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- Wigren, Jane (author)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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Winberg, Martin E. (author)
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- Rasmusson, Birgitta (author)
- Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet
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- Li, Jianxun (author)
- Department of Oral Biology, College of Dentistry, University of Illinois, Chicago, USA
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- Särndahl, Eva (author)
- Linköpings universitet,Cellbiologi,Hälsouniversitetet
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(creator_code:org_t)
- Elsevier BV, 2004
- 2004
- English.
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In: Experimental Cell Research. - : Elsevier BV. - 0014-4827 .- 1090-2422. ; 300:2, s. 308-319
- Related links:
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http://urn.kb.se/res...
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http://urn.kb.se/res...
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https://doi.org/10.1...
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Abstract
Subject headings
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- We have investigated how LTB4, an endogenous chemoattractant encountered early in the inflammatory process, and fMLP, a bacteria-derived chemotactic peptide emanating from the site of infection, mediate inside-out regulation of the β2-integrin. The role of the two chemoattractants on β2-integrin avidity was investigated by measuring their effect on β2-integrin clustering and surface mobility, whereas their effect on β2-integrin affinity was measured by the expression of a high affinity epitope, a ligand-binding domain on β2-integrins, and by integrin binding to s-ICAM. We find that the two chemoattractants modulate the β2-integrin differently. LTB4 induces an increase in integrin clustering and surface mobility, but only a modest increase in integrin affinity. fMLP evokes a large increase in β2-integrin affinity as well as in clustering and mobility. Lipoxin, which acts as a stop signal for the functions mediated by pro-inflammatory agents, was used as a tool for further examining the inside-out mechanisms. While LTB4-induced integrin clustering and mobility were inhibited by lipoxin, only a minor inhibition of fMLP-induced β2-integrin avidity and no inhibition of integrin affinity were detected. The different modes of the inside-out regulation of β2-integrins suggest that distinct mechanisms are involved in the β2-integrin modulation induced by various chemoattractants.
Keyword
- β2-Integrins
- Cell adhesion
- Chemotactic factors
- Eicosanoids
- Inflammation
- Leukotriene B4
- Lipoxins
- Human Neutrophils
- Signal transduction
- MEDICINE
- MEDICIN
Publication and Content Type
- ref (subject category)
- art (subject category)
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