ORBi: Vollmer J-Y - Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors

Reference : Subcellular compartmentalization of activation and desensitization of responses mediated...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/126231

Title :	Subcellular compartmentalization of activation and desensitization of responses mediated by NK2 neurokinin receptors
Language :	English
Author, co-author :	Vollmer, J-Y []
	Alix, Philippe [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Pharmacologie >]
	Chollet, A []
	Takeda, K []
	Galzi, J-L []
Publication date :	1999
Journal title :	Journal of Biological Chemistry
Publisher :	American Society for Biochemistry and Molecular Biology
Volume :	274
Pages :	37915-37922
Audience :	International
ISSN :	0021-9258
e-ISSN :	1083-351X
City :	Baltimore
Country :	MD
Keywords :	[en] Receptors ; NK2 neurokinin ; Protein
Abstract :	[en] A functional fluorescent neurokinin NK2 receptor was constructed by joining enhanced green fluorescent protein to the amino-terminal end of the rat NK2 receptor and was expressed in human embryonic kidney cells. On cell suspensions, the binding of fluorescent Bodipy-labeled neurokinin A results in a saturatable and reversible decrease of NK2 receptor fluorescence via fluorescence resonance energy transfer. This can be quantified for nM to mM agonist concentrations and monitored in parallel with intracellular calcium responses. On single cells, receptor site occupancy and local agonist concentration can be determined in real time from the decrease in receptor fluorescence. Simultaneous measurement of intracellular calcium responses and agonist binding reveals that partial receptor site occupancy is sufficient to desensitize cellular response to a second agonist application to the same membrane area. Subsequent stimulation of a distal membrane area leads to a second response to agonist, provided that it had not been exposed to agonist during the first application. Together with persistent translocation of fluorescent protein kinase C to the membrane area exposed to agonist, the present data support that not only homologous desensitization but also heterologous desensitization of NK2 receptors is compartmentalized to discrete membrane domains.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/126231

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