Cloning and structural characterization of a human non-erythroid band 3-like protein.

Demuth, Donald R.; Showe, Louise C.; Ballantine, M; Palumbo, Antônio; Fraser, Peter; Cioé, Livia; Rovera, Giovanni; Curtis, Peter J.

doi:10.1002/j.1460-2075.1986.tb04348.x

Cited by 152 publications

(66 citation statements)

References 62 publications

(39 reference statements)

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“…The hydropathy plot of the chicken band 3 polypeptide reveals 10 very hydrophobic regions (A through J in Fig. 4) in the C-terminal portion of the molecule that are similar to those previously demonstrated for the murine erythroid (30) and human nonerythroid (15) polypeptide. Hydrophobic peaks A, C, E, and G (Fig.…”

Section: Resultssupporting

confidence: 78%

“…These studies revealed that the transmembrane domain of the chicken erythroid band 3 polypeptide is greater than 70% identical to the membrane-spanning region of the band 3 polypeptides from other species. The hydropathy profile suggests that chicken erythroid band 3 traverses the membrane 12 to 14 times, in agreement with previous results (15,30). Furthermore, many of the amino acids implicated in anion transport through drug binding studies are conserved in the chicken erythroid band 3 polypeptide.…”

supporting

confidence: 90%

“…The recent isolation and characterization of cDNA clones for the murine erythroid (30) and human nonerythroid (15) band 3 polypeptides have revealed several features of band 3 that are conserved. The predicted sequences of the transmembrane domains of the murine erythroid and human nonerythroid band 3 polypeptides are very similar to each other and to the transmembrane regions of the human erythroid band 3 polypeptide that have been sequenced (8,35).…”

mentioning

confidence: 99%

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Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

Cox¹,

Lazarides²

1988

Mol. Cell. Biol.

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Isolation and characterization of the chicken erythroid anion transporter (band 3) cDNA clone, pCHB3-1, revealed that the chicken erythroid band 3 polypeptide is 844 amino acids in length with a predicted mass of 109,000 daltons. This polypeptide is composed of a hydrophilic N-terminal cytoplasmic domain and a hydrophobic C-terminal transmembrane domain. The -90 N-terminal amino acids of the human and murine erythroid band 3 polypeptides are absent in the predicted sequence of the chicken erythroid band 3 polypeptide. The absence of this very acidic N-terminal region is consistent with the lack of binding of glyceraldehyde-3-phosphate dehydrogenase to chicken erythroid band 3, as weH as the relatively basic isoelectric point observed for this molecule. The remainder of the cytoplasmic domain shows little similarity to the cytoplasmic domain of the murine and human erythroid band 3, with the exception of the putative ankyrin-binding site, which is highly conserved. In contrast, the transmembrane domain of the chicken band 3 polypeptide is very similar to that of the murine erythroid and human nonerythroid band 3 polypeptides. The transmembrane domain contains 10 hydrophobic regions that could potentially traverse the membrane 12 to 14 times. In addition, a variant of chicken erythroid band 3, pCHB3-2, was cloned in which one of the hydrophobic regions of pCHB3-1 is lacking. The transcript complementary to pCHB3-2 accumulated in chicken erythroid ceUs in a similar manner as the transcript complementary to pCHB3-1 during embryonic development. This is the first example of a transporter protein or ion channel with alternative primary structures in its membrane-spanning segments.

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Section: Resultssupporting

confidence: 78%

supporting

confidence: 90%

mentioning

confidence: 99%

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Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

Cox¹,

Lazarides²

1988

Mol. Cell. Biol.

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“…Recently, the cDNA encoding a nonerythroid analogue of band 3 has been isolated and sequenced (Demuth et al, 1987). Although the overall degree of sequence identity in the cytoplasmic domain between the nonerythroid and erythroid band 3 was only 35 %, these workers identified a highly conserved region in this domain spanning residues 157-177, which they proposed to be the ankyrin-binding region (Fig.…”

Section: Discussionmentioning

confidence: 99%

Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

Morrow

Cianci

Ardito

et al. 1989

The Journal of Cell Biology

263

113

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Abstract. In nonerythroid cells the distribution of the cortical membrane skeleton composed of fodrin (spectrin), actin, and other proteins varies both temporally with cell development and spatially within the cell and on the membrane. In monolayers of Madin-Darby canine kidney (MDCK) cells, it has previously been shown that fodrin and Na,K-ATPase are codistributed asymmetrically at the basolateral margins of the cell, and that the distribution of fodrin appears to be regulated posttranslationally when confluence is achieved (Nelson, W. J., and P. I. Veshnock. 1987. J. Cell Biol. 104:1527-1537. The molecular mechanisms underlying these changes are poorly understood. We find that (a) in confluent MDCK cells and intact kidney proximal tubule cells, Na,K-ATPase, fodrin, and analogues of human erythrocyte ankyrin are precisely colocalized in the basolateral domain at the ultrastructural level. (b) This colocalization is only achieved in MDCK cells after confluence is attained. (c) Erythrocyte ankyrin binds saturably to Na,K-ATPase in a molar ratio of ",d ankyrin to 4 Na,K-ATPase's, with a kD of 2.6/~M. (d) The binding of ankyrin to Na,K-ATPase is inhibited by the 43-kD cytoplasmic domain of erythrocyte band 3. (e) ~25I-labeled ankyrin binds to the alpha subunit of Na,K-ATPase in vitro. There also appears to be a second minor membrane protein of • 240 kD that is associated with both erythrocyte and kidney membranes that binds ~25I-labeled ankyrin avidly. The precise identity of this component is unknown. These results identify a molecular mechanism in the renal epithelial cell that may account for the polarized distribution of the fodrin-based cortical cytoskeleton.

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“…Human AE1 protein has been purified and characterized (Lukakovic et al 1981), and its cDNA has been cloned and sequenced as well (Tanner et al 1988;Lux et al 1989). AE2 and AE3 transcripts (and corresponding cDNAs) were identified by cross hybridization with AE1 cDNA probes (Demuth et al 1986;Alper et al 1988;Kopito et al 1989;Kudrycki et al 1990;Lindsey et al 1990). The complete coding sequence of human kidney AE2 cDNA has also been described (Gehrig et al 1992).…”

Section: Introductionmentioning

confidence: 99%

In situ detection of AE2 anion-exchanger mRNA in the human liver

García

Montuenga

Medina

et al. 1998

Cell and Tissue Research

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Na + -independent anion exchangers, a family of membrane proteins that mediate electroneutral exchanges of chloride and bicarbonate ions across the cell membrane, are considered to be involved in intracellular pH regulation as well as in transepithelial acid/base transport. Previous immunohistochemical data have shown that anion-exchanger-2 (AE2) protein is expressed in the liver parenchyma, localizing at both the canaliculi and the luminal surfaces of intrahepatic bile ducts, where it may have a role in the biliary secretion of bicarbonate. In the present study, we have carried out in situ hybridization experiments on biopsies of human liver using three overlapping antisense anion-exchanger-2 riboprobes. Anion-exchanger-2 mRNA signals were localized mainly in the cytoplasm of terminal and interlobular bile-duct cells, whereas weaker signals were observed in bile-duct cells of larger intrahepatic ducts. Furthermore, some hepatocytes, mostly periportal, contained detectable anion-exchanger-2 mRNA signals in their cytoplasm. No hybridization signals were observed in controls with sense riboprobes, with omission of the antisense probe, or with treatment of the sections with RNase before hybridizations. Finally, intense anion-exchanger-2 hybridization signals were observed in lymphomononuclear cells in sinusoids and in portal infiltrates. Immunocytochemical data from reverse-phase sections suggest that these cells correspond to some of the CD45R+ (UCHL1+) T lymphocytes resident in the liver.

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Cloning and structural characterization of a human non-erythroid band 3-like protein.

Cited by 152 publications

References 62 publications

Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

In situ detection of AE2 anion-exchanger mRNA in the human liver

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