Disease relevance of Slc4a1

• Anion-exchange high-performance liquid chromatography of membrane proteins from liver and Morris hepatomas [1].
• Anion-exchange HPLC of the ConA-fractionated oligosaccharides corroborated the decreased sialylation in polyarthritis [2].

Psychiatry related information on Slc4a1

• It is concluded that AE1 and SLC26A7 are differentially regulated in OMCD in water deprivation [3].

High impact information on Slc4a1

• Anion exchange HPLC revealed rapid (15 s) and dose-dependent stimulation of inositol 1,4,5-trisphosphate (IP3) generation following exposure of [3H]myoinositol preloaded mesangial cells to 10-100 nM endothelin [4].
• Inhibition of Src family kinases in vivo by genistein, herbimycin A, or ST638 prevents purinergic activation of AE1 [5].
• The anion exchanger of erythrocytes (AE1) and Na+,K(+)-ATPase of polarized epithelial cells provide well studied examples of how integral membrane proteins are anchored via the linker molecule ankyrin to the spectrin-based membrane cytoskeleton [6].
• These motifs are highly conserved during evolution of both Na+,K(+)-ATPase and AE1, further underlining their potential role in cytoskeleton to membrane linkage [6].
• Anion exchange chromatography on Mono Q afforded the resolution of at least five peaks of insulin-stimulated myelin basic protein kinase activity [7].

Biological context of Slc4a1

• Selective biotinylation of the apical or basolateral membrane proteins in cultured IMCD cells revealed that both AE1 and AE2 are polarized to the basolateral membrane [8].
• Since both luminal membrane proton pumps are sensitive to small changes in cytosolic pH, variation in density of either AE1 or peritubular anion conductance can modulate OMCD proton secretory rate [9].
• AE1 was internalized when Pco(2) was reduced and exocytosed when Pco(2) was increased, and both mucosal wortmannin and methazolamide inhibited exocytosis [10].
• Anion exchange proteins underlie chloride/bicarbonate exchange, cell shape regulation and participate in removal of aged cells by the immune system [11].
• Three AE isoforms, AE1, AE2 and AE3, have been identified in cardiac membranes, but the function of each isoform on pH(i) homeostasis is still under investigation [12].

Anatomical context of Slc4a1

• The mobility of the lower molecular weight band was similar to that of AE1 in red blood cell ghosts and kidney homogenate and therefore probably represents AE1 [8].
• A spliced variant of AE1 gene encodes a truncated form of Band 3 in heart: the predominant anion exchanger in ventricular myocytes [13].
• Immunohistochemical analysis, using a rabbit polyclonal antibody against the carboxy-terminal 12 amino acids of anion exchanger 1 (AE1), revealed a distribution of immunoreactive protein that is consistent with a basolateral localization of AE in cultured cells and in alpha-intercalated cells identified in sections of rat kidney cortex [8].
• It is concluded that this cultured line of rat IMCD cells expresses two members of the anion exchanger gene family, AE1 and AE2, and both of these exchangers probably mediate the electroneutral Cl--dependent HCO3-transport observed in this cell line [8].
• Northern analysis of alveolar epithelial cell mRNA using anion exchanger (AE) isoform-specific cDNA probes indicates that alveolar epithelial cells express the AE2 isoform predominantly, if not exclusively, and do not express detectable AE1 (i.e., band-3 protein) or AE3.(ABSTRACT TRUNCATED AT 250 WORDS)[14]

Associations of Slc4a1 with chemical compounds

• Anion-exchange h.p.l.c. analysis of [3H]inositol phosphates derived from glucose-stimulated isolated pancreatic islets that had been prelabelled with myo-[3H]inositol revealed that the predominant inositol trisphosphate was the 1,3,4-isomer [Ins(1,3,4)P3] [15].
• Model calculations indicate that if all of the chloride entry via AE1 recycles across a peritubular chloride channel and if this channel is anything other than highly selective for chloride, then it should conduct a substantial fraction of the bicarbonate exit [9].
• Anion exchange chromatography completely separates a PI-selective from a PE-selective activity, indicating the presence of two different, apparently monoselective phospholipase A2 species [16].
• Anion exchange, hydroxylapatite, and gel filtration chromatography yielded a 100-fold purification of phosphatase from a low-salt extract [17].
• Anion-exchange high-performance liquid chromatography of water-soluble chromium (VI) and chromium (III) complexes in biological materials [18].

Regulatory relationships of Slc4a1

• Anion exchange chromatographic analysis of cadmium binding to low molecular mass cytosolic proteins showed that cells treated with cadmium and 5-azacytidine expressed at least 2 isoforms of metallothionein [19].

Other interactions of Slc4a1

• Chromosomal mapping of the rat Slc4a family of anion exchanger genes, Ae1, Ae2, and Ae3 [20].
• Anion-exchange chromatography on a Mono-Q column of the supernatant fraction, after ultracentrifugation, from a homogenate of rat cerebrum, prepared under isotonic conditions in the presence of protease inhibitors, yielded a novel isoenzyme of cyclic nucleotide phosphodiesterase (PDE) with properties unlike those of known PDEs [21].
• Anion-exchange HPLC showed radioactivity associated with the alpha 2u-globulin fraction in urine and renal cytosol of male SD rats; the radioactive compound was identified as HCBD bound to the protein [22].
• Anion-exchange chromatographic behavior of recombinant rat cytochrome b5. Thermodynamic driving forces and temperature dependence of the stoichiometric displacement parameter Z [23].
• Anion-exchange chromatography of liver extracts separated glucokinase from a fructose-6-phosphate-sensitive and fructose-1-phosphate-sensitive inhibitor of that enzyme [24].

Analytical, diagnostic and therapeutic context of Slc4a1

• RT-PCR revealed the presence of AE1, AE2 and AE3 mRNAs in both neonatal and adult rat cardiomyocytes [13].
• Northern blot analysis documented the expression of mRNA for AE1 and AE2 but not AE3 [8].
• AE1 is expressed both as the erythroid form (Band 3 or eAE1) and a novel alternate transcript (nAE1), which was more specifically characterized using a PCR mapping strategy [13].
• In situ hybridization indicated the exclusive expression of SLC26A7 in the outer medulla and double immunofluorescence labeling confirmed the co-localization of AE1 and SLC26A7 on the basolateral membrane of A-IC cells in OMCD [3].
• In situ hybridization study revealed that AE1 mRNA is expressed predominantly in surface but not crypt cells [25].

References