RGD Reference Report - Functional and physical interactions between formyl-peptide-receptors and scavenger receptor MARCO and their involvement in amyloid beta 1-42-induced signal transduction in glial cells.

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Functional and physical interactions between formyl-peptide-receptors and scavenger receptor MARCO and their involvement in amyloid beta 1-42-induced signal transduction in glial cells.
Authors:	Brandenburg, Lars-Ove Konrad, Maximilian Wruck, Christoph J Koch, Thomas Lucius, Ralph Pufe, Thomas
Citation:	Brandenburg LO, etal., J Neurochem. 2010 May;113(3):749-60. doi: 10.1111/j.1471-4159.2010.06637.x. Epub 2010 Feb 5.
RGD ID:	12907556
Pubmed:	PMID:20141570 (View Abstract at PubMed)
DOI:	DOI:10.1111/j.1471-4159.2010.06637.x (Journal Full-text)
Recent studies suggest that the chemotactic G protein-coupled receptor formyl-peptide-receptor-like-1 (FPRL1) or the scavenger receptor MARCO (macrophage receptor with collagenous structure) plays an essential role in the inflammatory response of host defense mechanisms and neurodegenerative disorders such as Alzheimer's disease. We therefore analyzed the involvement of FPRL1 and MARCO in amyloid beta1-42 (Abeta1-42)-induced signalling by extracellular-signal regulated kinases 1/2 (ERK1/2) phosphorylation and cAMP level measurement in glial cells (astrocytes and microglia) and in transfected HEK293 cells. Receptors were inhibited by small interference RNA and the consequences in Abeta1-42- and MARCO agonist fucoidan-induced signal transduction were determined. Receptor deactivation by antagonists or small interference RNA verified the importance of FPRL1 for Abeta1-42-mediated signal transduction by ERK1/2 phosphorylation and cAMP level measurement in glial cells. Furthermore, for the first time, we have demonstrated a functional interaction between FPRL1 and scavenger receptors in fucoidan-mediated signalling by ERK1/2 phosphorylation and cAMP level measurement. In addition, co-immunoprecipitation data and fluorescence microscopy measurements revealed a physical interaction between FPR, FPRL1 and MARCO. These results suggest that FPRL1 plays a pivotal role for Abeta1-42-induced signal transduction in glial cells and the interaction with MARCO could explain the broad ligand spectrum of formyl peptide receptors.

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Biological Process

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Object Symbol	Species	Term	Qualifier	Evidence	With	Notes	Source	Original Reference(s)
Marco	Rat	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway	involved_in	IDA		PMID:20141570	ARUK-UCL
Marco	Rat	positive regulation of ERK1 and ERK2 cascade	involved_in	IDA		PMID:20141570	ARUK-UCL

Cellular Component

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Object Symbol	Species	Term	Qualifier	Evidence	With	Notes	Source	Original Reference(s)
Fpr1	Rat	cytoplasm	located_in	IDA		PMID:20141570	ARUK-UCL
Marco	Rat	cytoplasm	located_in	IDA		PMID:20141570	ARUK-UCL
Fpr1	Rat	plasma membrane	located_in	IDA		PMID:20141570	ARUK-UCL
Marco	Rat	plasma membrane	located_in	IDA		PMID:20141570	ARUK-UCL

Molecular Function

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Object Symbol	Species	Term	Qualifier	Evidence	With	Notes	Source	Original Reference(s)
Marco	Rat	G protein-coupled receptor binding	enables	IPI	UniProtKB:D4A7Q2	PMID:20141570	ARUK-UCL
Fpr1	Rat	scavenger receptor binding	enables	IPI	UniProtKB:M0R9F7	PMID:20141570	ARUK-UCL

Objects Annotated

Genes (Rattus norvegicus)

Fpr1 (formyl peptide receptor 1)

Marco (macrophage receptor with collagenous structure)

Objects referenced in this article

Gene	Fpr2	formyl peptide receptor 2	Rattus norvegicus

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Functional and physical interactions between formyl-peptide-receptors and scavenger receptor MARCO and their involvement in amyloid beta 1-42-induced signal transduction in glial cells.