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Gene Review

SLC4A1  -  solute carrier family 4, anion exchanger,...

Gallus gallus

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Disease relevance of AE1

  • Four variant chicken erythroid AE1 anion exchangers. Role of the alternative N-terminal sequences in intracellular targeting in transfected human erythroleukemia cells [1].
 

High impact information on AE1

  • These studies, which represent the first description of tyrosine-dependent cytoplasmic sorting signal for a type III membrane protein, have suggested a critical role for the actin cytoskeleton in regulating AE1 anion exchanger localization and stability in this epithelial cell type [2].
  • Intracellular trafficking of variant chicken kidney AE1 anion exchangers: role Of alternative NH(2) termini in polarized sorting and Golgi recycling [2].
  • Treatment of cells with serine and threonine phosphatase inhibitors had no effect on ankyrin/AE1 complex formation [3].
  • At least some of this spectrin-independent pool of ankyrin is complexed with the AE1 anion exchanger, and the solubility properties of this pool are also regulated by phosphorylation [3].
  • Detergent extraction of erythroid cells in situ has suggested that a substantial fraction of the perinuclear pool of AE1 is cytoskeletal associated [4].
 

Biological context of AE1

  • These results represent the first demonstration of anion exchanger expression in the chick CAM, and they suggest a role for basolateral AE1 in bicarbonate reabsorption that is required in the embryo for maintaining acid-base balance during development [5].
  • Antibodies specific for the chicken AE1 anion exchanger have been used to determine the cell-type specific pattern of expression of this electroneutral transporter in the chick chorioallantoic membrane (CAM) during embryonic development [5].
  • Variant chicken kidney AE1 anion exchanger transcripts are derived from a single promoter by alternative splicing [6].
  • These results suggest that the pattern of accumulation of the variant kidney AE1 anion exchangers is regulated by a complex pattern of alternative transcriptional initiation and differential RNA splicing [7].
 

Anatomical context of AE1

  • Four variant AE1 anion exchangers with predicted molecular masses of approximately 99, approximately 102, approximately 104, and approximately 108 kDa are expressed in chicken erythroid cells [1].
  • Cell type-specific and developmentally regulated expression of the AE1 anion exchanger in the chicken chorioallantoic membrane [5].
  • Double immunostaining indicated that the AE1-positive cells in the chorionic and allantoic epithelia were also positive for the carbonic anhydrase isoform, CAII, which serves as a marker for the villus cavity (VC) cells of the chorionic epithelium and the mitochondria-rich cells of the allantoic epithelium [5].
  • In both, shelled and non-shelled epidermis, acidic alpha keratin (AE1 positive) was limited to tonofilament bundles of the basal and suprabasal layer, while basic keratin (AE3 positive) was present in basal, suprabasal, and less intensely, pre-corneus layers, but tended to disappear in the corneus layer [8].
 

Associations of AE1 with chemical compounds

  • Furthermore, AE1 anion exchangers become detergent insoluble more rapidly than they acquire endo F-resistant modifications in cells recovering from an ammonium chloride block [4].
  • Finally, AE1 was stimulated by oxygenation in HbA cells, but this stimulation by O2 was absent in HbS cells and pink ghosts prepared from HbA cells [9].
 

Other interactions of AE1

  • Immunohistochemical colocalization of HKalpha(2c) with carbonic anhydrase II, the Cl(-)/HCO exchanger AE1, and HKalpha(1) indicated that both type A and type B intercalated cells possessed intense apical HKalpha(2c) immunoreactivity, whereas principal cells and connecting segment cells had only a thin apical band of HKalpha(2c) [10].
  • AE1-, AE2-, or AE3-positive alpha-keratins are present in different epidermal layers with a pattern similar to that previously described in reptiles [11].
 

Analytical, diagnostic and therapeutic context of AE1

  • Reverse transcriptase polymerase chain reaction studies have indicated that the extensive diversity in the transcripts derived from the AE1 gene occurs both in primitive and definitive lineage erythroid cells [1].
  • Immunoelectron microscopy revealed that AE1 accumulated in extensive projections that extended from the lateral membrane of VC cells towards the adjacent capillary covering cells [5].
  • Immunoblotting analyses have demonstrated that antibodies specific for the chicken erythroid AE1 anion exchanger recognize multiple polypeptides ranging in size from approximately 95 to 112 kDa in chicken kidney [7].

References

  1. Four variant chicken erythroid AE1 anion exchangers. Role of the alternative N-terminal sequences in intracellular targeting in transfected human erythroleukemia cells. Cox, K.H., Adair-Kirk, T.L., Cox, J.V. J. Biol. Chem. (1995) [Pubmed]
  2. Intracellular trafficking of variant chicken kidney AE1 anion exchangers: role Of alternative NH(2) termini in polarized sorting and Golgi recycling. Adair-Kirk, T.L., Cox, K.H., Cox, J.V. J. Cell Biol. (1999) [Pubmed]
  3. Dynamics of ankyrin-containing complexes in chicken embryonic erythroid cells: role of phosphorylation. Ghosh, S., Cox, J.V. Mol. Biol. Cell (2001) [Pubmed]
  4. Chicken erythroid AE1 anion exchangers associate with the cytoskeleton during recycling to the Golgi. Ghosh, S., Cox, K.H., Cox, J.V. Mol. Biol. Cell (1999) [Pubmed]
  5. Cell type-specific and developmentally regulated expression of the AE1 anion exchanger in the chicken chorioallantoic membrane. Gabrielli, M.G., Cox, J.V., Materazzi, G., Menghi, G. Histochem. Cell Biol. (2004) [Pubmed]
  6. Variant chicken kidney AE1 anion exchanger transcripts are derived from a single promoter by alternative splicing. Cox, K.H., Adair-Kirk, T.L., Cox, J.V. Gene (1996) [Pubmed]
  7. Variant chicken AE1 anion exchangers possess divergent NH(2)-terminal cytoplasmic domains. Cox, K.H., Cox, J.V. Am. J. Physiol. (1995) [Pubmed]
  8. Immunocytochemical observations on the cornification of soft and hard epidermis in the turtle Chrysemys picta. Alibardi, L. Zoology (Jena) (2002) [Pubmed]
  9. Oxygen sensitivity of red cell membrane transporters revisited. Drew, C., Ball, V., Robinson, H., Clive Ellory, J., Gibson, J.S. Bioelectrochemistry (Amsterdam, Netherlands) (2004) [Pubmed]
  10. Immunohistochemical localization of H-K-ATPase alpha(2c)-subunit in rabbit kidney. Verlander, J.W., Moudy, R.M., Campbell, W.G., Cain, B.D., Wingo, C.S. Am. J. Physiol. Renal Physiol. (2001) [Pubmed]
  11. Formation of the corneous layer in the epidermis of the tuatara (Sphenodon punctatus, Sphenodontida, Lepidosauria, Reptilia). Alibardi, L. Zoology (Jena) (2004) [Pubmed]
 
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