PMID: 9544581Apr 17, 1998Paper

Modulation of neutrophil adherence to endothelial cells by platelet-derived adherence-inhibiting factor through interactions with selectin molecules

Journal of Leukocyte Biology
K IwabuchiT Yamashita

Abstract

Platelet-derived adherence-inhibiting factor (AIF) has been demonstrated to regulate the neutrophil binding to type IV collagen. In this study, we have examined the effect of AIF on neutrophil adherence to confluently cultured human umbilical vein endothelial cells (EC). AIF inhibited neutrophil adherence to thrombin- or tumor necrosis factor alpha (TNF-alpha)-stimulated EC by 75 or 43%, respectively, but hardly affected neutrophil adherence to resting EC. It is interesting to note that the inhibitory activity of AIF was reduced by N-formyl-methionyl-leucyl-phenylalanine (fMLP) stimulation of neutrophils. Pretreatment of neutrophils or EC with AIF inhibited neutrophil adherence to thrombin- or TNF-alpha-stimulated EC, suggesting that neutrophils and EC have AIF-binding proteins. Using AIF-Sepharose affinity chromatography, AIF-binding proteins containing L-selectin were isolated from 125I-labeled resting neutrophils. However, L-selectin was markedly decreased in the AIF-binding fraction from fMLP-stimulated neutrophils. With the use of AIF-affinity chromatography, P- and E-selectins were obtained in the AIF-binding fractions from resting, thrombin-, and TNF-alpha-stimulated EC. It is important to note that P- and E-selectin wer...Continue Reading

Citations

Apr 27, 1999·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·S S YadavP A Clavien
Aug 28, 2003·Liver Transplantation : Official Publication of the American Association for the Study of Liver Diseases and the International Liver Transplantation Society·Nobuaki SakamotoAndrew S Klein

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