ArticleAnnals of surgery1997
Integrin stimulation regulates polymorphonuclear leukocytes inflammatory cytokine expression.
Article in Annals of surgery, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 12 citations in OpenAlex.
- The effects of substrate stiffness on the in vitro activation of macrophages and in vivo host response to poly(ethylene glycol)-based hydrogels.Journal of biomedical materials research. Part A · 2012Article
- Tumor necrosis factor-alpha binding in porcine primary stromal-vascular cell cultures.In vitro cellular & developmental biology. Animal · 2001Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
objectiveThe purpose of these studies is to investigate the role of integrin binding on the regulation of polymorphonuclear leukocyte (PMN) cytokine receptor expression. SUMMARY BACKGROUND DATA: Current knowledge in this area revolves around the ability of beta 2 integrins to mediate PMN adherence and chemotaxis. The role of alpha 1-6/beta 1 integrins in regulating cytokine receptor expression has not been probed.
methodsPurified human PMN were adhered on plastic, fibronectin, or laminin-coated surfaces followed by the addition of iodine 125 (125I) monoclonal antibodies (mAbs) directed against tumor necrosis factor-alpha R (TNF-alpha R) p60, p80, or interleukin-1 beta R (IL-1 beta R) types I, II. Receptor expression was calculated based on the counts per minute (cpm) bound. The role of individual beta 1 integrins was assessed using mAbs directed against the alpha 1-6 subunit of the beta 1 complex, and integrin cross-linkage was achieved using secondary goat antimouse F(ab')2 antibodies. Polymorphonuclear leukocytes were pretreated with herbimycin A to determine the role of protein tyrosine kinase in mediating the effect of the beta 1 integrins.
resultsAdherence of PMN to Ln decreased IL-1 beta types I, II receptor expression, whereas adherence to Fn increased TNF-alpha R p60 and p80 expression. Anti-VLA-5 (CD49e) but not anti-VLA-1 through VLA-4 and VLA-6, blocked the effect of Fn on TNF-alpha receptors, whereas anti-VLA-6 but not anti-VLA-1 through VLA-5 blocked the effect of Ln on IL-1 beta receptors. Modulation of IL-1 beta and TNF-alpha receptors by VLA-5 and VLA-6 required protein tyrosine kinase activation as herbimycin A (10 micrograms/mL) blocked the affect of Fn and Ln. Changes in PMN cytokine receptor expression led to parallel changes in functional activity as assessed by the binding of 125I IL-1 beta and TNF-alpha.
conclusionsIntegrin stimulation regulates the cell surface expression of PMN cytokine receptors. Ligation of CD49e upregulates TNF-alpha receptor expression, whereas binding of CD49f downregulates IL-1 beta receptor expression. Both processes are protein tyrosine kinase dependent. Changes in PMN cytokine receptor expression led to corresponding changes in functional activity. These results provide the first demonstration that chemotaxis of PMN into the interstitium provides a mechanism for ongoing participation in the local inflammatory response and is regulated by matrix protein integrin receptors.
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