TY - JOUR
T1 - Adherence of human monocytes to haemodialysis membranes
T2 - LFA 1 (CDlla/CD18) CR1 (CD35) and CR3 (CDllb/CD18) triggering promotes the biosynthesis of platelet-activating factor and adherence
AU - Tetta, C.
AU - Tropea, F.
AU - Camussi, G.
AU - Neri, R.
AU - Wratten, L.
AU - Sereni, L.
AU - Silvestro, L.
AU - Franceschi, C.
AU - Haeffner-Cavaillon, N.
PY - 1995
Y1 - 1995
N2 - Background Platelet-activating factor is a mediator of inflammation involved in the blood-membrane interaction.We report that selective stimulation of complement receptors (CR1 and CR3) triggers PAF synthesis and monocyte adherenceto complement-activating membranes. Methods The synthesis of PAF was studied after stimulation of normal human adherent monocytes with F(ab)2 and Fab fragments of monoclonal antibodies specific to CR1 and CR3. CD11a, CD11b, CD18, and CD35 was studied by flow cytometry on neutrophils and monocytes. The molecular species of PAF from stimulated monocytes were identified by reverse-phase high-performance liquid chromatography coupled with mass spectrometry. Results Anti-CR1 and anti-CR3 monoclonal antibodies induced a dose-dependent C-16 but not C-18 PAF production. The latter occurred also with mono-valent Fab fragments of both anti-CRl and anti-CR3 monoclonal antibodies, that were not internalized as seen by immunofluorescence. Adherence of monocytes to Cuprophan membranes was markedly higher (P>0.01) in membranes pretreated with fresh than with heat-inactivated normal plasma. However, the high adherence to fresh plasma-treated membranes wascompletely abrogated by coincubating the cells with Web 2170, a specific PAF receptor antagonist. This was not due to downregulation of adhesion molecules expression on leukocytes. Conclusions These studies implicate a crucial role of PAF in blood interaction with haemodialysis membranes that fix complement activated products.
AB - Background Platelet-activating factor is a mediator of inflammation involved in the blood-membrane interaction.We report that selective stimulation of complement receptors (CR1 and CR3) triggers PAF synthesis and monocyte adherenceto complement-activating membranes. Methods The synthesis of PAF was studied after stimulation of normal human adherent monocytes with F(ab)2 and Fab fragments of monoclonal antibodies specific to CR1 and CR3. CD11a, CD11b, CD18, and CD35 was studied by flow cytometry on neutrophils and monocytes. The molecular species of PAF from stimulated monocytes were identified by reverse-phase high-performance liquid chromatography coupled with mass spectrometry. Results Anti-CR1 and anti-CR3 monoclonal antibodies induced a dose-dependent C-16 but not C-18 PAF production. The latter occurred also with mono-valent Fab fragments of both anti-CRl and anti-CR3 monoclonal antibodies, that were not internalized as seen by immunofluorescence. Adherence of monocytes to Cuprophan membranes was markedly higher (P>0.01) in membranes pretreated with fresh than with heat-inactivated normal plasma. However, the high adherence to fresh plasma-treated membranes wascompletely abrogated by coincubating the cells with Web 2170, a specific PAF receptor antagonist. This was not due to downregulation of adhesion molecules expression on leukocytes. Conclusions These studies implicate a crucial role of PAF in blood interaction with haemodialysis membranes that fix complement activated products.
KW - Biocompatibility
KW - Monocyte
KW - Paf
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U2 - 10.1093/oxfordjournals.ndt.a091406
DO - 10.1093/oxfordjournals.ndt.a091406
M3 - Article
C2 - 8559489
AN - SCOPUS:0029080855
SN - 0931-0509
VL - 10
SP - 1679
EP - 1688
JO - Nephrology Dialysis Transplantation
JF - Nephrology Dialysis Transplantation
IS - 9
ER -