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Tytuł pozycji:

Caveolin-1 assembles type 1 inositol 1,4,5-trisphosphate receptors and canonical transient receptor potential 3 channels into a functional signaling complex in arterial smooth muscle cells.

Tytuł :
Caveolin-1 assembles type 1 inositol 1,4,5-trisphosphate receptors and canonical transient receptor potential 3 channels into a functional signaling complex in arterial smooth muscle cells.
Autorzy :
Adebiyi A; Department of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA.
Narayanan D
Jaggar JH
Pokaż więcej
Źródło :
The Journal of biological chemistry [J Biol Chem] 2011 Feb 11; Vol. 286 (6), pp. 4341-8. Date of Electronic Publication: 2010 Nov 23.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
Język :
English
Imprint Name(s) :
Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
MeSH Terms :
Caveolin 1/*metabolism
Cerebral Arteries/*metabolism
Inositol 1,4,5-Trisphosphate Receptors/*metabolism
Membrane Microdomains/*metabolism
Muscle, Smooth, Vascular/*metabolism
Myocytes, Smooth Muscle/*metabolism
TRPC Cation Channels/*metabolism
Animals ; Caveolin 1/genetics ; Cerebral Arteries/cytology ; Cholesterol/metabolism ; Cholesterol/pharmacology ; Gene Knockdown Techniques ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol 1,4,5-Trisphosphate/pharmacology ; Inositol 1,4,5-Trisphosphate Receptors/genetics ; Ion Transport/drug effects ; Ion Transport/physiology ; Male ; Membrane Microdomains/genetics ; Muscle, Smooth, Vascular/cytology ; Rats ; Rats, Sprague-Dawley ; TRPC Cation Channels/genetics ; Vasoconstriction/drug effects ; Vasoconstriction/physiology ; beta-Cyclodextrins/pharmacology
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Grant Information :
R01 HL094378 United States HL NHLBI NIH HHS; K01 HL096411 United States HL NHLBI NIH HHS; K01 HL096411-02 United States HL NHLBI NIH HHS; K01 HL096411-01 United States HL NHLBI NIH HHS; K01 HL096411-03 United States HL NHLBI NIH HHS; K01HL096411 United States HL NHLBI NIH HHS; R01 HL067061 United States HL NHLBI NIH HHS; R01 HL67061 United States HL NHLBI NIH HHS; HL094378 United States HL NHLBI NIH HHS
Substance Nomenclature :
0 (Cav1 protein, rat)
0 (Caveolin 1)
0 (Inositol 1,4,5-Trisphosphate Receptors)
0 (TRPC Cation Channels)
0 (TRPC3 cation channel)
0 (beta-Cyclodextrins)
0 (methyl-beta-cyclodextrin)
85166-31-0 (Inositol 1,4,5-Trisphosphate)
97C5T2UQ7J (Cholesterol)
Entry Date(s) :
Date Created: 20101125 Date Completed: 20110324 Latest Revision: 20210205
Update Code :
20210210
PubMed Central ID :
PMC3039319
DOI :
10.1074/jbc.M110.179747
PMID :
21098487
Czasopismo naukowe
Physical coupling of sarcoplasmic reticulum (SR) type 1 inositol 1,4,5-trisphosphate receptors (IP(3)R1) to plasma membrane canonical transient receptor potential 3 (TRPC3) channels activates a cation current (I(Cat)) in arterial smooth muscle cells that induces vasoconstriction. However, structural components that enable IP(3)R1 and TRPC3 channels to communicate locally are unclear. Caveolae are plasma membrane microdomains that can compartmentalize proteins. Here, we tested the hypothesis that caveolae and specifically caveolin-1 (cav-1), a caveolae scaffolding protein, facilitate functional IP(3)R1 to TRPC3 coupling in smooth muscle cells of resistance-size cerebral arteries. Methyl-β-cyclodextrin (MβCD), which disassembles caveolae, reduced IP(3)-induced I(Cat) activation in smooth muscle cells and vasoconstriction in pressurized arteries. Cholesterol replenishment reversed these effects. Cav-1 knockdown using shRNA attenuated IP(3)-induced vasoconstriction, but did not alter TRPC3 and IP(3)R1 expression. A synthetic peptide corresponding to the cav-1 scaffolding domain (CSD) sequence (amino acids 82-101) also attenuated IP(3)-induced I(Cat) activation and vasoconstriction. A cav-1 antibody co-immunoprecipitated cav-1, TRPC3, and IP(3)R1 from cerebral artery lysate. ImmunoFRET indicated that cav-1, TRPC3 channels and IP(3)R1 are spatially co-localized in arterial smooth muscle cells. IP(3)R1 and TRPC3 channel spatial localization was disrupted by MβCD and a CSD peptide. Cholesterol replenishment re-established IP(3)R1 and TRPC3 channel close spatial proximity. Taken together, these data indicate that in arterial smooth muscle cells, cav-1 co-localizes SR IP(3)R1 and plasma membrane TRPC3 channels in close spatial proximity thereby enabling IP(3)-induced physical coupling of these proteins, leading to I(Cat) generation and vasoconstriction.

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