gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Bestrophin 3

VMD2L3, bestrophin 3, Best-3, mBest4, Vitelliform Macular Dystrophy 2-Like 3
BEST3 belongs to the bestrophin family of anion channels, which includes BEST1 (MIM 607854), the gene mutant in vitelliform macular dystrophy (VMD; MIM 153700), and 2 other BEST1-like genes, BEST2 (MIM 607335) and BEST4 (MIM 607336). Bestrophins are transmembrane (TM) proteins that share a homology region containing a high content of aromatic residues, including an invariant arg-phe-pro (RFP) motif. The bestrophin genes share a conserved gene structure, with almost identical sizes of the 8 RFP-TM domain-encoding exons and highly conserved exon-intron boundaries. Each of the 4 bestrophin genes has a unique 3-prime end of variable length (Stohr et al., 2002 [PubMed 12032738]; Tsunenari et al., 2003 [PubMed 12907679]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Best2, HAD, VMD2L2, ACID, ARB
Papers on VMD2L3
Bestrophin-3 is differently expressed in normal and injured mouse glomerular podocytes.
Nilsson et al., Göteborg, Sweden. In Acta Physiol (oxf), Aug 2015
Recently, cell-protective functions for Bestrophin-3 (Best3) were proposed.
Bestrophin 3 ameliorates TNFα-induced inflammation by inhibiting NF-κB activation in endothelial cells.
He et al., Shanghai, China. In Plos One, 2013
Bestrophin 3 (Best-3) is involved in the regulation of cell proliferation, apoptosis and differentiation of a variety of physiological functions, but its function in cardiovascular system remains unclear.
Cadmium and cellular signaling cascades: interactions between cell death and survival pathways.
Lee et al., Witten, Germany. In Arch Toxicol, 2013
Severe ROS/Ca(2+) signals activate cell death effectors (ceramides, ASK1-JNK/p38, calpains, caspases) and/or cause irreversible damage to vital organelles, such as mitochondria and endoplasmic reticulum (ER), whereas low localized ROS/Ca(2+) levels act as 2nd messengers promoting cellular adaptation and survival through signal transduction (ERK1/2, PI3K/Akt-PKB) and transcriptional regulators (Ref1-Nrf2, NF-κB, Wnt, AP-1, bestrophin-3).
Mitochondria dependent pathway is involved in the protective effect of bestrophin-3 on hydrogen peroxide-induced apoptosis in basilar artery smooth muscle cells.
Guan et al., Guangzhou, China. In Apoptosis, 2013
Bestrophin 3 (Best-3) is expressed in a variety of tissues, such as cardiac, smooth muscle and renal tissues, and it is highly expressed in rat basilar arterial smooth muscle cells (BASMCs).
C-terminal membrane association of Bestrophin 3 and its activation as a chloride channel.
Jiang et al., Qingdao, China. In J Membr Biol, 2013
Bestrophin 3 (Best3), a member of the bestrophin Cl(-) channel family, is a candidate of cGMP-sensitive, Ca(2+)-activated Cl(-) channel in vascular smooth muscle cells.
ERK1/2-dependent bestrophin-3 expression prevents ER-stress-induced cell death in renal epithelial cells by reducing CHOP.
Thévenod et al., Witten, Germany. In Biochim Biophys Acta, 2012
ERK1/2-dependent Best-3 activation regulates cell fate decisions during endoplasmic reticulum stress by suppressing CHOP induction and death.
Downregulation of TMEM16A calcium-activated chloride channel contributes to cerebrovascular remodeling during hypertension by promoting basilar smooth muscle cell proliferation.
Guan et al., Guangzhou, China. In Circulation, 2012
METHODS AND RESULTS: Whole-cell patch-clamp studies showed that knockdown of TMEM16A but not bestrophin-3 attenuated CaCC currents in rat basilar smooth muscle cells.
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
Bestrophin-3 expression was significantly reduced compared with arteries transfected with mutated siRNA
Mechanisms of cellular synchronization in the vascular wall. Mechanisms of vasomotion.
Matchkov, Århus, Denmark. In Dan Med Bull, 2010
PCR and Western blot studies on different blood vessels demonstrated the presence of bestrophin-3 protein with the exception of pulmonary arteries where the cGMP-dependent current is also absent).
Inward-rectifier chloride currents in Reissner's membrane epithelial cells.
Marcus et al., Manhattan, United States. In Biochem Biophys Res Commun, 2010
Channel transcripts expressed include ClC-2, Slc26a7 and ClC-Ka, but not Cftr, ClC-1, ClCa1, ClCa2, ClCa3, ClCa4, Slc26a9, ClC-Kb, Best1, Best2, Best3 or the beta-subunit of ClC-K, barttin.
A PI3 kinase inhibitor found to activate bestrophin 3.
Li et al., Qingdao, China. In J Cardiovasc Pharmacol, 2010
Bestrophin 3 (Best3), a member of bestrophin Cl channel family, is a CaCl(cGMP) channel candidate in vascular smooth muscle cells.
Bestrophin expression and function in the human pancreatic duct cell line, CFPAC-1.
Winpenny et al., Norwich, United Kingdom. In J Physiol, 2009
Results provide evidence that the bestrophins are expressed in pancreatic duct cells and, more specifically, that hBest1 plays a role in the calcium activated chloride channels found in these cells.
Bestrophin-3 (vitelliform macular dystrophy 2-like 3 protein) is essential for the cGMP-dependent calcium-activated chloride conductance in vascular smooth muscle cells.
Nilsson et al., Århus, Denmark. In Circ Res, 2008
Bestrophin-3 (vitelliform macular dystrophy 2-like 3 protein) is essential for the cGMP-dependent calcium-activated chloride conductance in vascular smooth muscle cells.
A variant of the Ca2+-activated Cl channel Best3 is expressed in mouse exocrine glands.
Melvin et al., Rochester, United States. In J Membr Biol, 2008
We found that mouse exocrine glands expressed an alternately spliced variant of Best3, a member of the Bestrophin (Vmd2) Ca2+-activated Cl channel gene family, whereas the heart expressed full-length Best3.
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.
Small-conductance Cl- channels contribute to volume regulation and phagocytosis in microglia.
Schlichter et al., Toronto, Canada. In Eur J Neurosci, 2007
Microglia express several candidate genes, with relative mRNA expression levels of: CLIC1 > ClC3 > I(Cln) > or = ClC2 > Best2 > Best1 > or = Best3 > Best4.
Activation of bestrophin Cl- channels is regulated by C-terminal domains.
Hartzell et al., Atlanta, United States. In J Biol Chem, 2007
These results suggest that an auto-inhibitory mechanism in C termini of bestrophin 3 may be universal among bestrophins investigated in the study.
share on facebooktweetadd +1mail to friends