PMID- 10201950
OWN - NLM
STAT- MEDLINE
DCOM- 19990513
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 162
IP  - 7
DP  - 1999 Apr 1
TI  - Lipopolysaccharide-coated erythrocytes activate human neutrophils via CD14 while 
      subsequent binding is through CD11b/CD18.
PG  - 4220-5
AB  - Interaction of LPS with monocytes and neutrophils is known to occur via CD14 and 
      is strongly enhanced by LPS-binding protein (LBP). Integrins as well as CD14 play
      a role in the interaction of erythrocytes (E) coated with LPS or whole
      Gram-negative bacteria with phagocytes. We reasoned that the density of LPS on a 
      particle is an important determinant in these interactions. Therefore, E were
      coated with different concentrations of LPS (ELPS). The binding of these ELPS to 
      neutrophils was evaluated by flow cytometry. Simultaneously, we measured fMLP
      receptor expression to evaluate neutrophil activation. ELPS only bound to
      neutrophils in the presence of LBP. Blocking CD14 inhibited both activation and
      binding, whereas blocking complement (C) receptor 3 (CR3) inhibited binding but
      not activation. TNF activation restored ELPS binding in CD14-blocked cells but
      not in cells in which CR3 was blocked. Salmonella minnesota did bind to
      neutrophils independent of CR3 or CD14. The addition of LBP enhanced binding
      twofold, and this surplus was dependent upon CD14 but not on CR3. We conclude
      that ELPS interact with neutrophils via CD14, initially giving rise to cell
      activation; subsequently, binding is solely mediated by activated CR3.
FAU - Troelstra, A
AU  - Troelstra A
AD  - Eijkman-Winkler Institute for Medical Microbiology, Utrecht University, The
      Netherlands. a.troelstra@lab.azu.nl
FAU - de Graaf-Miltenburg, L A
AU  - de Graaf-Miltenburg LA
FAU - van Bommel, T
AU  - van Bommel T
FAU - Verhoef, J
AU  - Verhoef J
FAU - Van Kessel, K P
AU  - Van Kessel KP
FAU - Van Strijp, J A
AU  - Van Strijp JA
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Acute-Phase Proteins)
RN  - 0 (CD18 Antigens)
RN  - 0 (Carrier Proteins)
RN  - 0 (Lipopolysaccharide Receptors)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Macrophage-1 Antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Formyl Peptide)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Peptide)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (lipopolysaccharide-binding protein)
RN  - I223NX31W9 (Fluorescein-5-isothiocyanate)
SB  - AIM
SB  - IM
MH  - *Acute-Phase Proteins
MH  - CD18 Antigens/*metabolism
MH  - Carrier Proteins/physiology
MH  - Cell Adhesion/immunology
MH  - Erythrocytes/*immunology/metabolism
MH  - Fluorescein-5-isothiocyanate/metabolism
MH  - Humans
MH  - Lipopolysaccharide Receptors/*physiology
MH  - Lipopolysaccharides/*immunology/metabolism
MH  - Macrophage-1 Antigen/*metabolism
MH  - *Membrane Glycoproteins
MH  - Neutrophil Activation/*immunology
MH  - Neutrophils/*immunology
MH  - Protein Binding/immunology
MH  - Receptors, Formyl Peptide
MH  - Receptors, Immunologic/metabolism
MH  - Receptors, Peptide/metabolism
MH  - Salmonella/immunology/metabolism
MH  - Tumor Necrosis Factor-alpha/physiology
EDAT- 1999/04/14 00:00
MHDA- 1999/04/14 00:01
CRDT- 1999/04/14 00:00
PHST- 1999/04/14 00:00 [pubmed]
PHST- 1999/04/14 00:01 [medline]
PHST- 1999/04/14 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1999 Apr 1;162(7):4220-5.