High-Throughput Ca2+ Flux Assay To Monitor Cyclic Nucleotide-Gated Channel Activity and Characterize Achromatopsia Mutant Channel Function

2019 ◽  
Vol 10 (8) ◽  
pp. 3662-3670
Author(s):  
Marlene A. Jacobson ◽  
Laura J. Jones ◽  
Dennis J. Colussi ◽  
Jacqueline C. Tanaka
Keyword(s):  
High Throughput ◽  
Cyclic Nucleotide ◽  
Channel Activity ◽  
Mutant Channel ◽  
Channel Function ◽  
Gated Channel

scholarly journals Development of a High-Throughput Ca2+ Flux Screening Assay to Monitor Cyclic Nucleotide-Gated Channel Activity and Evaluate Achromatopsia Disease Mutant Channel Function

2019 ◽  
Vol 116 (3) ◽  
pp. 107a-108a
Author(s):  
Jacqueline Tanaka ◽  
Cristy Almonte ◽  
Elizabeth McDuffie ◽  
Laura Jones ◽  
Dennis Colussi ◽  
...  
Keyword(s):  
High Throughput ◽  
Cyclic Nucleotide ◽  
Channel Activity ◽  
Screening Assay ◽  
Mutant Channel ◽  
Channel Function ◽  
Gated Channel

Expression of a single gene produces both forms of skeletal muscle cyclic nucleotide-gated channels

1997 ◽  
Vol 273 (6) ◽  
pp. E1140-E1148
Author(s):  
Lorraine C. Santy ◽  
Guido Guidotti
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Nucleotide ◽  
Single Gene ◽  
Rabbit Aorta ◽  
Rabbit Skeletal Muscle ◽  
Channel Activity ◽  
Cyclic Nucleotide Gated Channels ◽  
Gated Channel ◽  
Polymerase Chain ◽  
Two Populations

Cyclic nucleotide-gated cation channels in skeletal muscle are responsible for insulin-activated sodium entry into this tissue (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267: 832–841, 1992). These channels have previously been isolated from rabbit skeletal muscle by 8-bromoguanosine 3′,5′-cyclic monophosphate (8-BrcGMP) affinity chromatography, which separates them into two populations differing in nucleotide affinity [L. C. Santy and G. Guidotti. Am. J. Physiol. 271 ( Endocrinol. Metab. 34): E1051-E1060, 1996]. In this study, a polymerase chain reaction approach was used to identify skeletal muscle cyclic nucleotide-gated channel cDNAs. Rabbit skeletal muscle expresses the same cyclic nucleotide-gated channel as rabbit aorta (M. Biel, W. Altenhofen, R. Hullin, J. Ludwig, M. Freichel, V. Flockerzi, N. Dascal, U. B. Kaupp, and F. Hofmann. FEBS Lett. 329: 134–138, 1993). The entire cDNA for this gene was cloned from rabbit skeletal muscle and an antiserum to this protein produced. Expression of this cDNA produces a 63-kDa protein with cyclic nucleotide-gated channel activity. A similarly sized immunoreactive protein is present in sarcolemma. Purification of the expressed channels reveals that this single gene produces both native skeletal muscle channel populations.

scholarly journals Endoplasmic reticulum (ER) Ca2+-channel activity contributes to ER stress and cone death in cyclic nucleotide-gated channel deficiency

2017 ◽  
Vol 292 (27) ◽  
pp. 11189-11205 ◽  
Author(s):  
Michael R. Butler ◽  
Hongwei Ma ◽  
Fan Yang ◽  
Joshua Belcher ◽  
Yun-Zheng Le ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Er Stress ◽  
Cyclic Nucleotide ◽  
Channel Activity ◽  
Gated Channel

Impairment of Hyperpolarization-Activated, Cyclic Nucleotide-Gated Channel Function by the Intravenous General Anesthetic Propofol

2005 ◽  
Vol 315 (2) ◽  
pp. 517-525 ◽  
Author(s):  
Luisa P. Cacheaux ◽  
Norbert Topf ◽  
Gareth R. Tibbs ◽  
Ulrich R. Schaefer ◽  
Roberto Levi ◽  
...  
Keyword(s):  
Cyclic Nucleotide ◽  
General Anesthetic ◽  
Channel Function ◽  
Gated Channel

Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle

1996 ◽  
Vol 271 (6) ◽  
pp. E1051-E1060 ◽  
Author(s):  
L. C. Santy ◽  
G. Guidotti
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Nucleotide ◽  
Rod Outer Segments ◽  
Channel Activity ◽  
Cyclic Monophosphate ◽  
Cyclic Nucleotide Gated Channels ◽  
Muscle Plasma Membrane ◽  
Gated Channel ◽  
Two Peaks

A cyclic nucleotide-gated channel present in skeletal muscle plasma membrane has previously been identified as being responsible for insulin-activated sodium entry into muscle cells (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267:832-841, 1992). We have isolated this channel activity to further study and characterize it. The channel was solubilized from rabbit skeletal muscle sarcolemma and functionally reconstituted into phospholipid vesicles, as assayed by patch-clamp analysis of the reconstituted proteins. Channel activity was isolated by 8-bromo-guanosine 3',5'-cyclic monophosphate affinity chromatography, producing two distinct peaks of cyclic nucleotide-gated channel activity. These two types of channel activity differ in guanosine 3',5'-cyclic monophosphate affinity and in the ability to be opened by adenosine 3',5'-cyclic monophosphate. The cyclic nucleotide-gated channel from rod outer segments also forms two peaks of activity when purified in this manner. The presence of two forms of channel activity could have implications for the mechanism of insulin-activated sodium entry.

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