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A novel beta 1-dependent adhesion pathway on neutrophils: a mechanism invoked by dihydrocytochalasin B or endothelial transmigration.
FASEB J. 1995 Aug; 9(11):1103-11.FJ

Abstract

It is generally accepted that the beta 2-integrin is restricted to mononuclear leukocytes. The objective of this study was to determine whether neutrophils can also express beta 1-integrin (specifically alpha 4 beta 1) and whether this can support neutrophil adhesion to endothelial cells and to extracellular matrix. We stimulated neutrophils with dihydrocytochalasin B (DHCB) and various chemotactic stimuli and observed that chemotactic stimuli induced neutrophil adhesion via beta 2-integrin (CD18), whereas DHCB and either fMLP, PAF, or IL-8 induced adhesion to endothelium or protein-coated plastic that was not inhibitable by anti-CD18 antibody. beta 2-integrin-deficient cells, which did not respond to chemotactic stimuli alone, also adhered avidly in the presence of chemotactic stimuli and DHCB. The induced neutrophil adhesion was inhibited by antibody to beta 1- or alpha 4-integrin chains, but only if an anti-beta 2-integrin antibody was also present. Flow cytometry revealed increased expression of both beta 1 and alpha 4 in the presence of fMLP plus DHCB. Transendothelial migration of neutrophils induced by chemotactic stimuli alone also increased expression of beta 1 and alpha 4. Transmigration across deendothelialized membranes induced a similar beta 1 expression on neutrophils suggesting that events other than an endothelial signal elicited beta 1-integrin expression. Transmigration-induced beta 1-dependent expression translated into only modest adhesion to protein-coated plastic. These data suggest that both a pharmacological (DHCB) and a physiological (transmigration) stimulus can invoke expression of alpha 4 and beta 1 on human neutrophils to mediate adhesion.

Authors+Show Affiliations

Immunology Research Group, University of Calgary, Alberta, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7544310

Citation

Kubes, P, et al. "A Novel Beta 1-dependent Adhesion Pathway On Neutrophils: a Mechanism Invoked By Dihydrocytochalasin B or Endothelial Transmigration." FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, vol. 9, no. 11, 1995, pp. 1103-11.
Kubes P, Niu XF, Smith CW, et al. A novel beta 1-dependent adhesion pathway on neutrophils: a mechanism invoked by dihydrocytochalasin B or endothelial transmigration. FASEB J. 1995;9(11):1103-11.
Kubes, P., Niu, X. F., Smith, C. W., Kehrli, M. E., Reinhardt, P. H., & Woodman, R. C. (1995). A novel beta 1-dependent adhesion pathway on neutrophils: a mechanism invoked by dihydrocytochalasin B or endothelial transmigration. FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, 9(11), 1103-11.
Kubes P, et al. A Novel Beta 1-dependent Adhesion Pathway On Neutrophils: a Mechanism Invoked By Dihydrocytochalasin B or Endothelial Transmigration. FASEB J. 1995;9(11):1103-11. PubMed PMID: 7544310.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel beta 1-dependent adhesion pathway on neutrophils: a mechanism invoked by dihydrocytochalasin B or endothelial transmigration. AU - Kubes,P, AU - Niu,X F, AU - Smith,C W, AU - Kehrli,M E,Jr AU - Reinhardt,P H, AU - Woodman,R C, PY - 1995/8/1/pubmed PY - 2001/3/28/medline PY - 1995/8/1/entrez SP - 1103 EP - 11 JF - FASEB journal : official publication of the Federation of American Societies for Experimental Biology JO - FASEB J VL - 9 IS - 11 N2 - It is generally accepted that the beta 2-integrin is restricted to mononuclear leukocytes. The objective of this study was to determine whether neutrophils can also express beta 1-integrin (specifically alpha 4 beta 1) and whether this can support neutrophil adhesion to endothelial cells and to extracellular matrix. We stimulated neutrophils with dihydrocytochalasin B (DHCB) and various chemotactic stimuli and observed that chemotactic stimuli induced neutrophil adhesion via beta 2-integrin (CD18), whereas DHCB and either fMLP, PAF, or IL-8 induced adhesion to endothelium or protein-coated plastic that was not inhibitable by anti-CD18 antibody. beta 2-integrin-deficient cells, which did not respond to chemotactic stimuli alone, also adhered avidly in the presence of chemotactic stimuli and DHCB. The induced neutrophil adhesion was inhibited by antibody to beta 1- or alpha 4-integrin chains, but only if an anti-beta 2-integrin antibody was also present. Flow cytometry revealed increased expression of both beta 1 and alpha 4 in the presence of fMLP plus DHCB. Transendothelial migration of neutrophils induced by chemotactic stimuli alone also increased expression of beta 1 and alpha 4. Transmigration across deendothelialized membranes induced a similar beta 1 expression on neutrophils suggesting that events other than an endothelial signal elicited beta 1-integrin expression. Transmigration-induced beta 1-dependent expression translated into only modest adhesion to protein-coated plastic. These data suggest that both a pharmacological (DHCB) and a physiological (transmigration) stimulus can invoke expression of alpha 4 and beta 1 on human neutrophils to mediate adhesion. SN - 0892-6638 UR - https://www.unboundmedicine.com/medline/citation/7544310/A_novel_beta_1_dependent_adhesion_pathway_on_neutrophils:_a_mechanism_invoked_by_dihydrocytochalasin_B_or_endothelial_transmigration_ DB - PRIME DP - Unbound Medicine ER -