Apolipoprotein E and mimetic peptide initiate a calcium-dependent signaling response in macrophages.
Apolipoprotein E (ApoE) is a 34-kDa cholesterol transport protein that also possesses immunomodulatory properties. In this study, we demonstrate that ApoE initiates a signaling cascade in murine peritoneal macrophages that leads to increased production of inositol triphosphate with mobilization of intracellular Ca(2+) stores. This cascade is inhibited by pretreatment with receptor-associated protein and Ni(2+), and it is mediated by a pertussis toxin-sensitive G protein. These properties are characteristic of signal transduction induced via ligand binding to the cellular receptor, lipoprotein receptor-related protein. A peptide derived from the receptor-binding region of ApoE also initiates signal transduction in a manner similar to that of the intact protein, suggesting that this isolated region is sufficient for signal transduction. The ApoE-mimetic peptide competed for binding with the intact protein, confirming that they both interact with the same site. ApoE-dependent signal transduction might play a role in mediating the functional properties of this lipoprotein.[1]References
- Apolipoprotein E and mimetic peptide initiate a calcium-dependent signaling response in macrophages. Misra, U.K., Adlakha, C.L., Gawdi, G., McMillian, M.K., Pizzo, S.V., Laskowitz, D.T. J. Leukoc. Biol. (2001) [Pubmed]
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