Purification of stabilized band 3 protein of the human erythrocyte membrane and its reconstitution into liposomes

Lukacovic, Michael F.; Feinstein, Maurice B.; Sha'afi, R.I.; Perrie, S.

doi:10.1021/bi00514a025

Cited by 88 publications

(26 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…No monomer was detected. Since well-defined bands were observed at the expected positions of dimer and tetramer, with no material between the two bands, it appears that no significant dimer ~ tetramer interconversion took place during the 16-hr electrophoresis at 4~ The human band 3 as isolated by Lukacovic et al [81], however, is a mixture of monomer and stable dimer in Triton X-100.…”

Section: Cross-linking Studiesmentioning

confidence: 87%

“…Reconstitution experiments with purified band 3 [e.g. 75,81,118] have shown that the anion transport requires no other polypeptide. Although glycophorin was included in one of these reconstitutions [118], it is not necessary for anion transport, since En(a-) red cells, which lack glycophorin [44,142], have normal anion transport [143].…”

Section: General Aspects Of Band 3 Structure and Functionmentioning

confidence: 99%

See 1 more Smart Citation

Oligomeric structure and the anion transport function of human erythrocyte band 3 protein

Jennings

1984

J. Membrain Biol.

149

View full text Add to dashboard Cite

Section: Cross-linking Studiesmentioning

confidence: 87%

Section: General Aspects Of Band 3 Structure and Functionmentioning

confidence: 99%

Oligomeric structure and the anion transport function of human erythrocyte band 3 protein

Jennings

1984

J. Membrain Biol.

149

View full text Add to dashboard Cite

“…The common approach to investigate this in model systems, like lipid vesicles, is to study the magnitude of sulfate permeability of the vesicles and its sensitivity to anion transport-specific inhibitors like DIDS or DNDS [2][3][4][5]7,8]. However, in the band 3-erythrocyte lipid vesicles we could not demonstrate any inhibiting effect of 10 k~M DIDS on the SO42 permeability, whereas similar concentrations of DIDS inhibited the SO42-transport of erythrocytes completely (data not shown).…”

Section: Specific Permeability Properties Of Erythrocyte Lipidband 3 mentioning

confidence: 87%

“…1) is an attractive candidate for studying protein-lipid interactions in model toluene-phosphatidylcholine extraction [3], adsorption to Bio-Beads [2,[4][5][6] or after replacement of Triton X-100 by N-octylglycoside, by dialysis [7]. It has been reported that by the use of the Triton X-100-Bio-Bead method, band 3 was successfully reconstituted into lipid vesicles [2,[4][5][6].…”

Section: Introductionmentioning

confidence: 99%

The influence of lipid composition on the barrier properties of band 3-containing lipid vesicles

Hoogevest

Maine

Kruijff

et al. 1984

Biochimica et Biophysica Acta (BBA) - Biomembranes

View full text Add to dashboard Cite

Band 3 protein has been incorporated into lipid vesicles consisting of 94:6 (molar ratio) egg phosphatidylcholine-bovine heart phosphatidylserine or total erythrocyte lipids by means of a Triton X-100 Bio-Beads method, with an additional sonication step prior to the removal of the detergent. This method results, for both types of band 3 lipid vesicles, in rather homogeneous vesicles with comparable protein content and vesicle trap. Freeze-fracture electron microscopy revealed that band 3-egg phosphatidylcholine-bovine heart phosphatidylserine vesicles have considerably more intramembrane particles as compared to the band 3-erythrocyte lipid vesicles. The dimensions of the nonspecific permeation pathways present in the band 3-lipid vesicles were measured using an influx assay procedure for nonelectrolytes of different size, in which the vesicles were sampled and subsequently freed from nonenclosed labeled permeant by means of gel-filtration. The band 3-egg phosphatidylcholine-bovine heart phosphatidylserine vesicles have nonspecific permeation pathways (pores), with diameters of up to 60 ~,. In contrast, the band 3-total erythrocyte lipid vesicles are more homogeneous and show much smaller nonspecific permeation pathways, having a diameter of about 12 ji,. These results suggest that the nonspecific permeability of the band 3-lipid vesicles is strongly lipid-dependent. Increase in specific anion permeability expected as a consequence of the presence of band 3 in the erythrocyte lipid vesicles was found to be very limited. However, stereospecific, phioretin-inhibitable D-glucose permeability could clearly be demonstrated in these vesicles. The difference of the nonspecific permeability of the band 3-egg phosphatidylcholine-bovine heart phosphatidylserine vesicles and band 3-erythrocyte lipid vesicles, is discussed in the light of the presence of defects at the lipid/protein interface and protein aggregation, which may induce formation of pores.

show abstract

“…AE1 protein (also called ªband 3º) is the most abundant protein in the membranes of red blood cells (Fairbanks et al 1971). 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).…”

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

View full text Add to dashboard Cite

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.

show abstract

Purification of stabilized band 3 protein of the human erythrocyte membrane and its reconstitution into liposomes

Cited by 88 publications

References 28 publications

Oligomeric structure and the anion transport function of human erythrocyte band 3 protein

Oligomeric structure and the anion transport function of human erythrocyte band 3 protein

The influence of lipid composition on the barrier properties of band 3-containing lipid vesicles

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

Contact Info

Product

Resources

About