Differential inside-out activation of β2 integrins by leukotriene B4 and fMLP in human neutrophils

Patcha Brodin, Veronika (author): Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet

Wigren, Jane (author): Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet

Winberg, Martin E. (author)

Rasmusson, Birgitta (author): Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet

Li, Jianxun (author): Department of Oral Biology, College of Dentistry, University of Illinois, Chicago, USA

Särndahl, Eva (author): Linköpings universitet,Cellbiologi,Hälsouniversitetet

(creator_code:org_t)

Elsevier BV, 2004
2004
English.
In: Experimental Cell Research. - : Elsevier BV. - 0014-4827 .- 1090-2422. ; 300:2, s. 308-319

Related links:: http://urn.kb.se/res...; show more...; http://urn.kb.se/res...; https://urn.kb.se/re...; https://doi.org/10.1...; show less...

Abstract Subject headings

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.

By the author/editor: Patcha Brodin, V ...; Wigren, Jane; Winberg, Martin ...; Rasmusson, Birgi ...; Li, Jianxun; Särndahl, Eva

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