Variant chicken AE1 anion exchangers possess divergent NH2-terminal cytoplasmic domains

Kathleen H. Cox, John Cox

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14 Citations (Scopus)

Abstract

Immunoblotting analyses have demonstrated that antibodies specific for the chicken erythroid AE1 anion exchanger recognize multiple polypeptides ranging in size from ∼95 to 112 kDa in chicken kidney. To determine the origin of this diversity, we have cloned and characterized the kidney AE1 anion exchangers. These studies have shown that the kidney AE1 polypeptides are encoded by at least three transcripts, AE1-3, AE1-4, and AE1-5, which differ from the erythroid AE1-1 and AE1-2 transcripts in the sequences present at their 5′-ends. The AE1-3 and AE1-5 transcripts encode predicted polypeptides of ∼94 kDa, which are identical to the erythroid AE1-1 anion exchanger except for the absence of the 78 NH2-terminal amino acids of the AE1-1 polypeptide. In contrast, the AE1-4 transcript encodes a predicted polypeptide of ∼101 kDa, whose 21 NH2-terminal amino acids are unique. Characterization of the AE1 cDNAs has suggested that the AE1-3 and AE1-4 transcripts are generated by alternative splicing of a single primary transcript, while DNA blotting analyses have shown that the putative transcription initiation sites of the variant AE1-4 and AE1-5 transcripts lie several kilobases downstream of the transcription initiation sites of the erythroid AE1-1 and AE1-2 transcripts. 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.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Renal Fluid and Electrolyte Physiology
Volume268
Issue number3 37-3
StatePublished - Mar 1995

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Erythrocyte Anion Exchange Protein 1
Chickens
polypeptides
chickens
Peptides
kidneys
Kidney
Transcription Initiation Site
transcription (genetics)
RNA splicing
RNA Splicing
Amino Acids
amino acids
alternative splicing
Alternative Splicing
immunoblotting
Immunoblotting
Complementary DNA
antibodies
Antibodies

All Science Journal Classification (ASJC) codes

  • Physiology
  • Agricultural and Biological Sciences(all)

Cite this

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title = "Variant chicken AE1 anion exchangers possess divergent NH2-terminal cytoplasmic domains",
abstract = "Immunoblotting analyses have demonstrated that antibodies specific for the chicken erythroid AE1 anion exchanger recognize multiple polypeptides ranging in size from ∼95 to 112 kDa in chicken kidney. To determine the origin of this diversity, we have cloned and characterized the kidney AE1 anion exchangers. These studies have shown that the kidney AE1 polypeptides are encoded by at least three transcripts, AE1-3, AE1-4, and AE1-5, which differ from the erythroid AE1-1 and AE1-2 transcripts in the sequences present at their 5′-ends. The AE1-3 and AE1-5 transcripts encode predicted polypeptides of ∼94 kDa, which are identical to the erythroid AE1-1 anion exchanger except for the absence of the 78 NH2-terminal amino acids of the AE1-1 polypeptide. In contrast, the AE1-4 transcript encodes a predicted polypeptide of ∼101 kDa, whose 21 NH2-terminal amino acids are unique. Characterization of the AE1 cDNAs has suggested that the AE1-3 and AE1-4 transcripts are generated by alternative splicing of a single primary transcript, while DNA blotting analyses have shown that the putative transcription initiation sites of the variant AE1-4 and AE1-5 transcripts lie several kilobases downstream of the transcription initiation sites of the erythroid AE1-1 and AE1-2 transcripts. 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.",
author = "Cox, {Kathleen H.} and John Cox",
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AU - Cox, John

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AB - Immunoblotting analyses have demonstrated that antibodies specific for the chicken erythroid AE1 anion exchanger recognize multiple polypeptides ranging in size from ∼95 to 112 kDa in chicken kidney. To determine the origin of this diversity, we have cloned and characterized the kidney AE1 anion exchangers. These studies have shown that the kidney AE1 polypeptides are encoded by at least three transcripts, AE1-3, AE1-4, and AE1-5, which differ from the erythroid AE1-1 and AE1-2 transcripts in the sequences present at their 5′-ends. The AE1-3 and AE1-5 transcripts encode predicted polypeptides of ∼94 kDa, which are identical to the erythroid AE1-1 anion exchanger except for the absence of the 78 NH2-terminal amino acids of the AE1-1 polypeptide. In contrast, the AE1-4 transcript encodes a predicted polypeptide of ∼101 kDa, whose 21 NH2-terminal amino acids are unique. Characterization of the AE1 cDNAs has suggested that the AE1-3 and AE1-4 transcripts are generated by alternative splicing of a single primary transcript, while DNA blotting analyses have shown that the putative transcription initiation sites of the variant AE1-4 and AE1-5 transcripts lie several kilobases downstream of the transcription initiation sites of the erythroid AE1-1 and AE1-2 transcripts. 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.

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