Introduction of BEST1
Bestrophin-1 (BEST1) is encoded by the BEST1 gene. The bestrophin protein family includes four evolutionarily related genes (BEST1, BEST2, BEST3, and BEST4) encoding integrated membrane proteins. The family was first discovered in humans by linking the BEST1 mutation to the best yolk-like macular dystrophy (BVMD). In humans, bestrophins function as calcium-activated anion channels, each channel having a unique tissue distribution throughout the body. Specifically, the BEST1 gene on chromosome 11q13 encodes a BEST1 protein in humans, which is most highly expressed in the retina. The mutation of the BEST1 gene has been identified as the leading cause of at least five different degenerative retinal diseases.
|Basic Information of BEST1|
|Aliases||VMD2, TU15B, VMDP2, BMD, RP50|
|Organism||Homo sapiens (Human)|
Function of BEST1 Membrane Protein
BEST1 acts primarily as an intracellular calcium-activated chloride channel on the cell membrane that is independent of voltage. Recently, BEST1 has been shown to act as a volume-regulating anion channel. BVMD is one of the most common BEST1 related diseases. Mutation of the BEST1 gene results in loss of channel function and ultimately leads to retinal degeneration. Loss of function of the BEST1 chloride channel may explain some of the most common problems associated with BVMD: the inability to modulate intracellular ion concentration and regulate overall cell volume. In addition, some studies have shown that BEST1 is also associated with diseases such as yolk-like macular dystrophy (AVMD) and autosomal recessive hereditary pterygium (ARB) in adults.
Fig.1 Structure of BEST1 membrane protein.
Application of BEST1 Membrane Protein in Literature
This article reports that mapping of transmembrane topography by insertion of N-linked glycosylation sites and tobacco etch virus protease cleavage sites provide evidence for cytosolic N and C termini and an unexpected transmembrane topography with at least three extracellular loops that include positions 60-63, 212-227, and 261-267. These experiments provide the first structural analysis of the bestrophin channel family.
Authors in this group apply their experiment results raise the possibility that disease-causing mutations in hBEST1 produce disease by altering HCO3(-) homeostasis as well as Cl(-) transport in the retina.
This article reveals that in a model system of a polarized epithelium, two of three mutations (p.L140V and p.D228N) caused mislocalization of BEST1 from the basolateral membrane to the cytoplasm. Mutations in BEST1 are increasingly recognized as an important cause of inherited retinal dystrophy.
This article identified possible mutation hotspots within the BEST gene, suggesting that particular regions of the protein have greater functional significance than others.
This article indicates a novel disease-causing mutation in the VMD2 gene (T990C) was found in Japanese patients with Best disease.
BEST1 Preparation Options
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-BEST1 antibody development services.
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