In:
Journal of Leukocyte Biology, Oxford University Press (OUP), Vol. 60, No. 6 ( 1996-12-01), p. 784-792
Abstract:
The Interaction of altered lipids or proteins with the several scavenger receptors (SR) on macrophages can lead to disparate results in both gene expression and cell function. However, the molecular bases of signaling induced by SR ligation have remained obscure. Here we report that maleylated-bovine serum albumin (maleyl-BSA) binds a low-affinity SR, initiating POP2 hydrolysis, [Ca2+J spikes, phospholipase A2 (PLA2) activation, nuclear factor-κB (NF-κB) binding to its cognate nucleotide and tumor necrosis factor α (TNF-α) gene transcription. We recently reported that oxidized low-density lipoprotein (ox-LDL), which binds another macrophage SR, induced pertussis-toxin-sensitive hydrolysis of PIP2 and elevations in [Ca2+]i [J. Biol. Chem. 270, 3475–3478, 1995] . By contrast, maleyl-BSA-initiated events were not pertussis toxin-sensitive and produced less [Ca2+]i spiking than ox-LDL. Furthermore, maleyl-BSA led to binding of NF-κB to its cognate nucleotide and TNF-α gene transcription, whereas ox-LDL suppressed these events. Collectively, this data suggests that maleyl-BSA and ox-LDL bind to distinct SR on murine macrophages, initiate distinct signal transduction pathways, and produce different functional effects.
Type of Medium:
Online Resource
ISSN:
0741-5400
,
1938-3673
DOI:
10.1002/jlb.60.6.784
Language:
English
Publisher:
Oxford University Press (OUP)
Publication Date:
1996
detail.hit.zdb_id:
2026833-6
SSG:
12
Permalink