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

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Fältnamn	Indikatorer	Metadata
000		03584naa a2200469 4500
001		oai:DiVA.org:liu-14629
003		SwePub
008		070913s2004 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-146292 URI
024	7	a https://doi.org/10.1016/j.yexcr.2004.07.0152 DOI
040		a (SwePub)liu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Patcha Brodin, Veronikau Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet4 aut0 (Swepub:liu)verpa92
245	1 0	a Differential inside-out activation of β2 integrins by leukotriene B4 and fMLP in human neutrophils
264	1	b Elsevier BV,c 2004
338		a print2 rdacarrier
520		a 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.
653		a β2-Integrins
653		a Cell adhesion
653		a Chemotactic factors
653		a Eicosanoids
653		a Inflammation
653		a Leukotriene B4
653		a Lipoxins
653		a Human Neutrophils
653		a Signal transduction
653		a MEDICINE
653		a MEDICIN
700	1	a Wigren, Janeu Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet4 aut0 (Swepub:liu)janwi24
700	1	a Winberg, Martin E.4 aut
700	1	a Rasmusson, Birgittau Linköpings universitet,Medicinsk mikrobiologi,Hälsouniversitetet4 aut0 (Swepub:liu)birra51
700	1	a Li, Jianxunu Department of Oral Biology, College of Dentistry, University of Illinois, Chicago, USA4 aut
700	1	a Särndahl, Evau Linköpings universitet,Cellbiologi,Hälsouniversitetet4 aut0 (Swepub:liu)evasa98
710	2	a Linköpings universitetb Medicinsk mikrobiologi4 org
773	0	t Experimental Cell Researchd : Elsevier BVg 300:2, s. 308-319q 300:2<308-319x 0014-4827x 1090-2422
856	4	u http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-9661y Link to Ph.D. Thesis (Veronika Brodin Patcha)
856	4	u http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-43383y Link to Ph.D. Thesis (Martin Tinnerfelt Winberg)
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-14629
856	4 8	u https://doi.org/10.1016/j.yexcr.2004.07.015

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Av författaren/redakt...: Patcha Brodin, V ...; Wigren, Jane; Winberg, Martin ...; Rasmusson, Birgi ...; Li, Jianxun; Särndahl, Eva

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Av lärosätet: Linköpings universitet

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