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286252 occurrences (No.88 in the rank) during 5 years in the PubMed. [cache]
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286252 occurrences (No.88 in the rank) during 5 years in the PubMed. [cache]
| 107) A screening of 77 compounds enabled the identification of effective chemical and pharmacological chaperones that result in a 1.5- to 4.8-fold increase of surface expression of mutant CNGA3. |
| PMID:33827965 DOI:10.1124/molpharm.120.000180 |
| 2021 Molecular pharmacology |
| * Identification of Chemical and Pharmacological Chaperones for Correction of Trafficking-Deficient Mutant Cyclic Nucleotide-Gated A3 Channels. |
| - Trafficking deficiency caused by missense mutations is a well known phenomenon that occurs for mutant, misfolded proteins. Typically, the misfolded protein is retained by the protein quality-control system and degraded by the endoplasmic reticulum-associated protein degradation pathway and thus does not reach its destination, although residual function of the protein may be preserved. Chemical and pharmacological chaperones can improve the targeting of trafficking-deficient proteins and thus may be promising candidates for therapeutic applications. Here, we report the application of a cellular bioassay based on the bioluminescent calcium reporter aequorin to quantify surface expression of mutant CNGA3 channels associated with the autosomal recessively inherited retinal disease achromatopsia. A screening of 77 compounds enabled the identification of effective chemical and pharmacological chaperones that result in a 1.5- to 4.8-fold increase of surface expression of mutant CNGA3. Using selected compounds, we confirmed that the rescue of the defective trafficking is not limited to a single mutation in CNGA3. Active compounds and our structure-activity correlated data for the dihydropyridine compound class may provide valuable information for developing a treatment of the trafficking defect in achromatopsia. SIGNIFICANCE STATEMENT: This study describes a novel luminescence-based assay to detect the surface expression of mutant trafficking-deficient CNGA3 channels based on the calcium-sensitive photoprotein aequorin. Using this assay for a compound screening, this study identifies novel chemical and pharmacological chaperones that restore the surface localization of mutant trafficking-deficient CNGA3 channels. The results from this work may serve as starting point for the development of potent compounds that rescue trafficking deficiencies in the autosomal recessively inherited retinal disease achromatopsia. |
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(24)2 KIF20B |
(36)2 heat |
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(14)4 specific |
(25)2 Ki-67 |
(37)2 miR-296 |
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(26)2 MMP-1 |
(38)2 miR-627 |
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(16)3 mitochondrial |
(27)2 NCS1 |
(39)2 miRNAs |
| (6)6 nuclear |
(17)3 multiple |
(29)2 SLCO2B1 |
(40)2 oncoproteins, |
| (7)5 Staphylococcus |
(18)3 several |
(30)2 VEGF |
(41)2 platelet-derived |
| (8)5 pro-inflammatory |
(19)3 vascular |
(31)2 asSuGR, |
(42)2 recombinant |
| (9)4 CYP3A4 |
(20)2 ACE-2 |
(32)2 cytokines/chemokines |
(43)2 tight |
| (10)4 both |
(21)2 ASIC1a, |
(33)2 farnesoid |
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(22)2 ATG5 |
(34)2 fibroblast |
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| (12)4 its |
(23)2 CCN1 |
(35)2 fibrogenic |
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