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Senescent human neutrophil binding to thrombospondin (TSP): evidence for a TSP‐independent pathway of phagocytosis by macrophages by Joseph F. Murphy; John L. Mcgregor; Lawrence L. K. Leung is a Medicine article available to read on EtoBox.

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This study investigated the interaction of apoptotic polymorphonuclear neutrophils (PMN) with thrombospondin (TSP), an important event mediating the clearance of apoptotic neutrophils by macrophages. We developed an __in vitro__ assay to examine this interaction. Based on this assay, we found that apoptotic but not fresh PMN bound specifically to surface‐immobilized TSP (33 ± 0.03 × 10^3^ cells/well) compared to fibrinogen, fibronectin or laminin (8.0 ± 0.3 × 10^3^ cells/well). Moreover, the binding was specific for surface bound but not soluble TSP and appeared to be divalent cation dependent, was not significantly inhibited by heparin and was sensitive to cycloheximide (CHX) treatment of senescent PMN (>90% inhibition at 10 μM CHX). In contrast to the binding studies, phagocytosis of senescent PMN by macrophages was not affected by EDTA or cycloheximide. Phosphatidyl‐ L‐serine liposomes, phospho‐ L‐serine, glucosamine, galactosamine, and the acetylated sugars had no effect on phagocytosis. We conclude that: (i) there was specific binding of senescent human PMN to immobilized TSP, which is divalent cation dependent and requires new protein synthesis in the PMN during senescence; (

Who reads Senescent human neutrophil binding to thrombospondin (TSP): evidence for a TSP‐independent pathway of phagocytosis by macrophages?

Author

Joseph F. Murphy; John L. Mcgregor; Lawrence L. K. Leung

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0007-1048)

Published

1998

Language

EN

Field

Medicine (Health Sciences)