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PMID: 10767434 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

ATP-induced activation of expressed RyR3 at low free calcium.

FEBS letters ·Vol. 471 ·No. 2-3 ·2000-04-14 ·Pages 256-60

Manunta M, Rossi D, Simeoni I, Butelli E, Romanin C, Sorrentino V, Schindler H

Abstract

Ca(2+) channel properties of the mink ryanodine receptor type 3 (RyR3), expressed in HEK293 cells, were studied in planar lipid bilayers to which RyR3 rich membrane fragments had been fused. RyR3 channels were not active at resting levels of Ca(2+)(free) but were gated by an additional 1 mM ATP, exhibiting long open times. The second major finding was the absence of channel inactivation at millimolar Ca(2+)(free). Insertion of a myc tag at the N-terminus of RyR3 did not affect the channel properties. As to skeletal muscle, the observed type 3 channel properties appear physiologically meaningful by assisting type 1 channels in calcium release.

MeSH Terms
Adenosine Triphosphate/metabolism,pharmacology Animals Calcium/metabolism,pharmacology Cell Line Electric Conductivity Humans Ion Channel Gating/drug effects Kinetics Lipid Bilayers/metabolism Microsomes/drug effects,metabolism Mink Protein Isoforms/chemistry,genetics,metabolism Recombinant Fusion Proteins/chemistry,genetics,metabolism Ryanodine Receptor Calcium Release Channel/chemistry,genetics,metabolism Sarcoplasmic Reticulum/drug effects,metabolism Transfection
Chemicals
Lipid Bilayers Protein Isoforms Recombinant Fusion Proteins Ryanodine Receptor Calcium Release Channel Adenosine Triphosphate Calcium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Manunta M
Institute for Biophysics, University of Linz, Altenberger Strasse 69, A-4040, Linz, Austria.
Rossi D
Simeoni I
Butelli E
Romanin C
Sorrentino V
Schindler H
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2000-04-14
Pages
256-60
Language
English
Region
England
NLM ID
0155157
Subset
IM
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