A relationship between anion transport and a structural transition of the human erythrocyte membrane

Snow, Julian W.; Vincentelli, Jean; Brandts, John F.

doi:10.1016/0005-2736(81)90457-0

Cited by 34 publications

(12 citation statements)

References 21 publications

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“…Indeed, there is now good evidence to sup port the idea that at least one transmembrane protein, band 3 in erythrocyte membranes, is folded into a structure consisting of three independent, or nearly independent, do mains [8,9] The only feature o f receptor structure which is important to this clustering model is that ligand interaction sites be physically at tached to the receptor, and that there be interaction sites on both sides o f the mem brane. The mechanism will be viable even for transmembrane proteins that are unable to undergo long-range conformational changes.…”

Section: Receptor Clusteringmentioning

confidence: 99%

A General Mechanism for Transmembrane Signalling Based on Clustering of Receptors

Brandts¹,

Jacobson

1983

Pathol Immunopathol Res

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Section: Receptor Clusteringmentioning

confidence: 99%

A General Mechanism for Transmembrane Signalling Based on Clustering of Receptors

Brandts¹,

Jacobson

1983

Pathol Immunopathol Res

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“…It should be noted that this entire budding and vesiculation process occurs without hemolysis. Enzymatic modification of the erythrocyte vesicle membrane proteins was carried out with (1) trypsin (EC 3.4.21.4) (Sigma, type XI) according to the procedure of Elgsaeter & Branton (1974), ( 2) chymotrypsin (EC 3.4.21.1) (Sigma, type II) by using the procedure of Siegel et al (1980), (3) neuraminidase (EC 3.2.1.18) (Sigma, type V) according to the method of Nigg et al (1980), and Pronase (Calbiochem, grade B) as described by Snow et al (1981), with the modification that NaTR" (pH 7.4) was used instead of Na-Tris (pH 7.4).…”

Section: Methodsmentioning

confidence: 99%

Roles of lipids and proteins in the calcium(2+)-phosphate-induced aggregation of cytoskeleton-free erythrocyte vesicle membranes

Leonards¹,

Ohki²

1984

Biochemistry

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The roles of lipids and proteins in Ca2+-PO4-induced membrane aggregation were investigated. Cytoskeleton-free vesicles derived from intact human and rabbit erythrocytes (HEves and REves, respectively) were employed as a model system. The HEves and REves have a simplified membrane protein composition [band 3 proteins and glycoproteins PAS-1, -2, and -3 (HEves)] and normal lipid composition. Optimal experimental conditions for pH, [PO4], and [CaCl2] were determined for quantitatively examining the dynamics and extent of HEves and REves aggregation, measured turbidimetrically. The aggregation process was found to be quite sensitive to small changes in pH and [PO4] and much less sensitive to [CaCl2]. The roles of membrane proteins in vesicle aggregation were examined by selectively modifying the proteins enzymatically. The roles of lipids were studied by using sonicated lipid vesicles [small unilamellar vesicles (SUVs)] made from Dodge ghost lipid extracts. Enzymatic treatment with trypsin, chymotrypsin, or Pronase had no effect on either the rates or the extent of vesicle aggregation (2-min incubation period). Neuraminidase treatment reduced both factors by approximately 20%. SUVs aggregated with Ca2+-PO4 in a way which depended on the PO4/lipid ratio. Together the results suggest the following: (1) PO4 is associated with the vesicle surface, involving the membrane lipids; (2) the vesicle + PO4 incubation time component of the PO4 effect is eliminated by enzymatically modifying the vesicle membrane proteins; (3) qualitative, rather than quantitative, properties of sialic acid containing molecules affect vesicle aggregation; and (4) with the exception of the incubation time effect, membrane proteins seem neither to promote nor to inhibit Ca2+-PO4-induced HEves or REves aggregation.

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“…4,4'diisothiocyanostilbene-2,2'-disulfonic acid (DIDS), pyridoxal phosphate, significantly stabilize the endotherm [7,8]. The noncovalent inhibitors of anion transport have generally been found to lower the temperature of the C transition, while the covalent inhibitors, e.g.…”

Section: Introductionmentioning

confidence: 99%

“…Although enormous numbers of studies characterizing lectin binding to high al'finity receptors on cell surfaces [9,10] and concerning the mechanism of Con A-mediated agglutination[l [1][2][3][4][5][6][7][8][9][10][11][12][13], it is still not clearly understood the relationships between the binding characteristic and the glycoprotein behavior at the molecular level. In this study, we have examined the changes of anion transport capability and the thermotropic behaviors of the C transition after binding of Con A to Band 3.…”

Section: Introductionmentioning

confidence: 99%

Concanavalin A binding to oligosaccharide chain leads to alterations in properties of Band 3

Zhang

Chen

1999

IUBMB Life

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Anion transport activity and thermotropic behavior of Band 3 are found to be altered after binding of concanavalin (Con A) to human erythrocyte ghosts and isolated Band 3. At lower Con A concentration, the rate coefficients of anion transport enhance with increasing Con A concentration, while noticeable changes of the largest calorimetric endotherm of human erythrocyte membranes termed the C transition (Band 3) can not be observed. With 50μg/ml of Con A, the rate coefficient of Con A‐modified ghosts increases 34.4% in comparison with that of normal ghosts. Binding of Con A in lower concentration to ghosts bring about increase of fluidity of lipid which maybe contribute to increase anion transport via Band 3. At higher Con A concentration, the C transition tend to lower temperature with increase in Con A concentration. the C transition is shifted from 69.25°C to 66.25°C with 2.5mg/ml Con A. It is suggested that the Con A‐modified Band 3 possess a looser structure than normal one.

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A relationship between anion transport and a structural transition of the human erythrocyte membrane

Cited by 34 publications

References 21 publications

A General Mechanism for Transmembrane Signalling Based on Clustering of Receptors

A General Mechanism for Transmembrane Signalling Based on Clustering of Receptors

Roles of lipids and proteins in the calcium(2+)-phosphate-induced aggregation of cytoskeleton-free erythrocyte vesicle membranes

Concanavalin A binding to oligosaccharide chain leads to alterations in properties of Band 3

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