PMID- 9482700
OWN - NLM
STAT- MEDLINE
DCOM- 19980227
LR  - 20180213
IS  - 1018-2438 (Print)
IS  - 1018-2438 (Linking)
VI  - 115
IP  - 2
DP  - 1998 Feb
TI  - Eosinophil granulocyte interaction with serum-opsonized particles: binding and 
      degranulation are enhanced by tumor necrosis factor alpha.
PG  - 121-8
AB  - Eosinophils participate in the inflammatory response seen in allergy and 
      helminthic infestation. Their release of granule-bound cationic proteins may play 
      a role in these diseases. Therefore, we investigated mechanisms involved in the 
      release of eosinophil cationic protein (ECP). Serum-opsonized zymosan was 
      phagocytosed by eosinophils, and ECP was released into the phagosomes as judged 
      by immunoelectron microscopy. Degranulation to the external milieu was induced by 
      serum-opsonized, non-phagocytosable Sephadex beads (SOS), and ECP release was 
      determined by use of an enzyme-linked immunosorbent assay. CD11b, CD18, and CD32 
      monoclonal antibodies inhibited degranulation, demonstrating dependence on 
      complement receptor type 3 (CR3), and the low-affinity Fc receptor for IgG. Tumor 
      necrosis factor-alpha (TNF-alpha) and interleukin (IL)-5 both rapidly enhanced 
      the binding of eosinophils to serum-opsonized zymosan, and also the release of 
      ECP upon interaction with SOS. The cytokine-induced increase in ECP release was 
      inhibited by the phospholipase A2 (PLA2) inhibitor mepacrine, indicating an 
      involvement of PLA2 in the enhanced response but not in baseline degranulation. 
      Autocrine stimulation by the platelet-activating factor (PAF) is unlikely since 
      the PAF receptor antagonist WEB 2086 did not inhibit the enhanced response. In 
      conclusion, the main signals for eosinophil degranulation on serum-opsonized 
      particles are mediated by CR3 and receptors for immunoglobulins. As for IL-5, 
      TNF-alpha changes eosinophil phenotype from a resting to an activated state.
FAU - Egesten, A
AU  - Egesten A
AD  - Department of Medicine, University Hospitals of Lund, Sweden. 
      Arne.Egesten@medforsk.mas.lu.se
FAU - Blom, M
AU  - Blom M
FAU - Calafat, J
AU  - Calafat J
FAU - Janssen, H
AU  - Janssen H
FAU - Knol, E F
AU  - Knol EF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Int Arch Allergy Immunol
JT  - International archives of allergy and immunology
JID - 9211652
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (Blood Proteins)
RN  - 0 (Dextrans)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Eosinophil Granule Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Opsonin Proteins)
RN  - 0 (Receptors, Complement)
RN  - 0 (Receptors, Fc)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (complement C3a receptor)
RN  - 9010-72-4 (Zymosan)
RN  - 9014-76-0 (sephadex)
RN  - EC 3.1.- (Ribonucleases)
RN  - EC 3.1.1.32 (Phospholipases A)
RN  - EC 3.1.1.4 (Phospholipases A2)
RN  - H0C805XYDE (Quinacrine)
SB  - IM
MH  - Antibodies, Monoclonal/pharmacology
MH  - Antigens, CD/immunology
MH  - Blood Proteins/metabolism
MH  - Cell Degranulation/*drug effects
MH  - Dextrans
MH  - Enzyme Inhibitors/pharmacology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Eosinophil Granule Proteins
MH  - Eosinophils/*physiology
MH  - Humans
MH  - *Membrane Proteins
MH  - Microspheres
MH  - Opsonin Proteins/*metabolism
MH  - Phagosomes/metabolism
MH  - Phospholipases A/antagonists & inhibitors
MH  - Phospholipases A2
MH  - Quinacrine/pharmacology
MH  - Receptors, Complement/physiology
MH  - Receptors, Fc/physiology
MH  - *Ribonucleases
MH  - Tumor Necrosis Factor-alpha/antagonists & inhibitors/*pharmacology
MH  - Zymosan/metabolism
EDAT- 1998/03/03 03:05
MHDA- 2000/10/06 11:01
CRDT- 1998/03/03 03:05
PHST- 1998/03/03 03:05 [pubmed]
PHST- 2000/10/06 11:01 [medline]
PHST- 1998/03/03 03:05 [entrez]
AID - iaa15121 [pii]
AID - 10.1159/000023891 [doi]
PST - ppublish
SO  - Int Arch Allergy Immunol. 1998 Feb;115(2):121-8. doi: 10.1159/000023891.