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Bestrophin 2

Best2, bestrophin-2, VMD2L1
This gene is a member of the bestrophin gene family of anion channels. Bestrophin genes share a similar gene structure with highly conserved exon-intron boundaries, but with distinct 3' ends. Bestrophins are transmembrane proteins that contain a homologous region rich in aromatic residues, including an invariant arg-phe-pro motif. Mutation in one of the family members (bestrophin 1) is associated with vitelliform macular dystrophy. The bestrophin 2 gene is mainly expressed in the retinal pigment epithelium and colon. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ARB, ACID, VMD2L2, V1a, VMD2L3
Papers on Best2
Lineage-specific expression of bestrophin-2 and bestrophin-4 in human intestinal epithelial cells.
Watanabe et al., Tokyo, Japan. In Plos One, 2012
Studies have suggested that, among the four human bestrophin-family genes, bestrophin-2 (BEST2) and bestrophin-4 (BEST4) might be expressed within the intestinal tissue.
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
Regulation of anterior chamber drainage by bicarbonate-sensitive soluble adenylyl cyclase in the ciliary body.
Marmorstein et al., Tucson, United States. In J Biol Chem, 2012
Mice deficient in the bicarbonate channel bestrophin-2 (Best2), however, exhibit a lower IOP despite an increase in AH production.
Bestrophin is important for the rhythmic but not the tonic contraction in rat mesenteric small arteries.
Matchkov et al., Århus, Denmark. In Cardiovasc Res, 2011
mRNA levels for bestrophin-1 and -2 were also significantly reduced by bestrophin-3 down-regulation
Bestrophin-2 mediates bicarbonate transport by goblet cells in mouse colon.
Hartzell et al., Atlanta, United States. In J Clin Invest, 2010
Bestrophin-2 mediates bicarbonate transport by goblet cells in mouse colon
Bestrophin 2 is expressed in human non-pigmented ciliary epithelium but not retinal pigment epithelium.
Marmorstein et al., Tucson, United States. In Mol Vis, 2009
These data suggest that Best2 may play a functional role in the regulation of aqueous flow and drainage in humans.
Calcium-activated chloride currents in olfactory sensory neurons from mice lacking bestrophin-2.
Menini et al., Trieste, Italy. In J Physiol, 2009
In the olfactory epithelium, bestrophin-2 (Best2) has been indicated as a candidate for being a molecular component of the olfactory Ca(2+)-activated Cl(-) channel.
Bestrophin 2: an anion channel associated with neurogenesis in chemosensory systems.
Möhrlen et al., Heidelberg, Germany. In J Comp Neurol, 2009
Results suggest that bestrophin 2 plays a critical role during differentiation and growth of axons and cilia.
Enhanced inflow and outflow rates despite lower IOP in bestrophin-2-deficient mice.
Marmorstein et al., Tucson, United States. In Invest Ophthalmol Vis Sci, 2009
PURPOSE: Bestrophin-2 (Best2), a putative Cl(-) channel is expressed in the nonpigmented epithelium (NPE).
Regulation of bestrophins by Ca2+: a theoretical and experimental study.
Anselmi et al., Trieste, Italy. In Plos One, 2008
Asp-rich domain has two defined binding sites and D301A and D304A mutations may impact the binding of the metal ions
Rescue of volume-regulated anion current by bestrophin mutants with altered charge selectivity.
Hartzell et al., Atlanta, United States. In J Gen Physiol, 2008
To test whether bestrophins are VRACs in mammalian cells, we compared VRACs in peritoneal macrophages from wild-type mice and mice with both bestrophin-1 and bestrophin-2 disrupted (best1(-/-)/best2(-/-)). VRACs were identical in wild-type and best1(-/-)/best2(-/-) mice, showing that bestrophins are unlikely to be the classical VRAC in mammalian cells.
Bestrophin 1 and 2 are components of the Ca(2+) activated Cl(-) conductance in mouse airways.
Kunzelmann et al., Regensburg, Germany. In Biochim Biophys Acta, 2008
suggest a role of bestrophin 1 and 2 for Ca(2+) dependent Cl(-) secretion in mouse airways
Molecular evolution and functional divergence of the bestrophin protein family.
Weber et al., Regensburg, Germany. In Bmc Evol Biol, 2007
Most notably, significant functional divergence was found between bestrophin 4 and the other family members, as well as between bestrophin 2 and bestrophin 3. Site-specific profiles were established by posterior probability analysis revealing significantly divergent clusters mainly in two hydrophilic loops and a region immediately adjacent to the last predicted transmembrane domain.
Activation of bestrophin Cl- channels is regulated by C-terminal domains.
Hartzell et al., Atlanta, United States. In J Biol Chem, 2007
Bestrophins (VMD2, VMD2L1, VMD2L2, and VMD2L3) are a new family of anion channels.
Functional and molecular characterization of the fluid secretion mechanism in human parotid acinar cells.
Melvin et al., Rochester, United States. In Am J Physiol Regul Integr Comp Physiol, 2007
Intracellular Ca2+ stimulated a niflumic acid-sensitive Cl- current with properties similar to the Ca2+ -gated Cl channel BEST2.
Bestrophin-2 is a candidate calcium-activated chloride channel involved in olfactory transduction.
Zucchelli et al., Trieste, Italy. In Proc Natl Acad Sci U S A, 2006
Here we have analyzed the expression of bestrophins in the mouse olfactory epithelium and demonstrated that only mouse bestrophin-2 (mBest2) was expressed.
The anion-selective pore of the bestrophins, a family of chloride channels associated with retinal degeneration.
Hartzell et al., Atlanta, United States. In J Neurosci, 2006
Here we systematically replaced every amino acid in mouse bestrophin-2 (mBest2) between positions 69 and 104 with cysteine.
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