A role for band 4.2 in human erythrocyte band 3 mediated anion transport

Saira Malik; Malkit Sami; Anthony Watts

doi:10.1021/bi00089a024

A kinetic study of the role of band 3 anion transport protein in the transport of salicylic acid and other hydroxybenzoic acids across the human erythrocyte membrane

Journal of Pharmaceutical Sciences ◽

10.1002/jps.2600810506 ◽

1992 ◽

Vol 81 (5) ◽

pp. 424-427 ◽

Cited By ~ 6

Author(s):

Tamie Minami ◽

David J. Cutler

Keyword(s):

Salicylic Acid ◽

Kinetic Study ◽

Erythrocyte Membrane ◽

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Protein ◽

Human Erythrocyte Membrane ◽

Hydroxybenzoic Acids

Further Studies on Zn2+-Mediated Domain–Domain Communication in Human Erythrocyte Band 3

Bioscience Reports ◽

10.1023/a:1020161032473 ◽

1998 ◽

Vol 18 (5) ◽

pp. 265-277

Author(s):

Hong Xu ◽

Xujia Zhang ◽

Fu Yu Yang

Keyword(s):

Conformational Change ◽

Human Erythrocyte ◽

Cytoplasmic Domain ◽

Band 3 ◽

Anion Transport ◽

Intrinsic Fluorescence ◽

Transport Activity ◽

Membrane Domain ◽

Nmr Study ◽

Anion Transport Activity

Human erythrocyte band 3 is purified and reconstituted into vesicles, forming right-side-out proteoliposomes. Zn2+ entrapped inside the proteoliposomes inhibits the anion transport activity of band 3, and removal of the cytoplasmic domain of band 3 is able to diminish Zn2+ inhibition. Thus, the inhibition of activity of band 3 results from the Zn2+ induced conformational change of the cytoplasmic domain, which in turn is transmitted to the membrane domain. The results of intrinsic fluorescence and its quenching by HB and the 35Cl NMR study indicate that the cytoplasmic domain is essential for the conformational change induced by Zn2+.SH-blocking reagents, CH3I and GSSG, are used to modify the cytoplasmic domain, where they specifically bind to Cys201 and Cys317. It is observed that the Zn2+ induced inhibition of anion transport activity is blocked. This demonstrates that Cys201 and Cys317 are required in Zn2+-mediated domain–domain communication.

Evidence That Eosin-5-maleimide Binds Close to the Anion Transport Site of Human Erythrocyte Band 3: A Fluorescence Quenching Study

Biochemistry ◽

10.1021/bi00014a045 ◽

1995 ◽

Vol 34 (14) ◽

pp. 4880-4888 ◽

Cited By ~ 12

Author(s):

Rui-jun Pan ◽

Richard J. Cherry

Keyword(s):

Fluorescence Quenching ◽

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Site

Studies on the interaction of matrix-bound inhibitor with Band 3, the anion transport protein of human erythrocyte membranes

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(88)90027-2 ◽

1988 ◽

Vol 942 (2) ◽

pp. 253-261 ◽

Cited By ~ 4

Author(s):

Sanjay W. Pimplikar ◽

Reinhart A.F. Reithmeier

Keyword(s):

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Protein ◽

Erythrocyte Membranes ◽

Human Erythrocyte Membranes ◽

Matrix Bound

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

The Journal of Membrane Biology ◽

10.1007/bf01868768 ◽

1984 ◽

Vol 80 (2) ◽

pp. 105-117 ◽

Cited By ~ 120

Author(s):

Michael L. Jennings

Keyword(s):

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Band 3 Protein ◽

Transport Function ◽

Oligomeric Structure

Reductive methylation of the two 4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonate-binding lysine residues of band 3, the human erythrocyte anion transport protein.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)34415-6 ◽

1982 ◽

Vol 257 (13) ◽

pp. 7554-7559 ◽

Cited By ~ 7

Author(s):

M L Jennings

Keyword(s):

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Protein ◽

Reductive Methylation ◽

Lysine Residues

Characterization of matrix-bound Band 3, the anion transport protein from human erythrocyte membranes.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)43526-5 ◽

1984 ◽

Vol 259 (2) ◽

pp. 785-790 ◽

Cited By ~ 4

Author(s):

A Boodhoo ◽

R A Reithmeier

Keyword(s):

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Protein ◽

Erythrocyte Membranes ◽

Human Erythrocyte Membranes ◽

Matrix Bound

The relationships between the oligomeric structure and the functions of human erythrocyte band 3 protein: the functional unit for the binding of ankyrin, hemoglobin and aldolase and for anion transport

The band 3 proteins: Anion transporters, binding proteins and senescent antigens - Progress in Cell Research ◽

10.1016/b978-0-444-89547-9.50025-4 ◽

1992 ◽

pp. 209-217 ◽

Cited By ~ 15

Author(s):

DIETER SCHUBERT ◽

ELFRIEDE HUBER ◽

SABINE LINDENTHAL ◽

KARLHEINZ MULZER ◽

PETER SCHUCK

Keyword(s):

Human Erythrocyte ◽

Functional Unit ◽

Band 3 ◽

Anion Transport ◽

Band 3 Protein ◽

Oligomeric Structure

Carboxypeptidase Y digestion of band 3, the anion transport protein of human erythrocyte membranes

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/0005-2736(87)90153-2 ◽

1987 ◽

Vol 903 (1) ◽

pp. 37-47 ◽

Cited By ~ 10

Author(s):

Debra M. Lieberman ◽

Michael Nattriss ◽

Reinhart A.F. Reithmeier

Keyword(s):

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Transport Protein ◽

Erythrocyte Membranes ◽

Carboxypeptidase Y ◽

Human Erythrocyte Membranes

Anion transport activity in the human erythrocyte membrane modulated by proteolytic digestion of the 38,000-dalton fragment in Band 3.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)43817-8 ◽

1983 ◽

Vol 258 (24) ◽

pp. 15376-15381 ◽

Cited By ~ 1

Author(s):

H Matsuyama ◽

Y Kawano ◽

N Hamasaki

Keyword(s):

Erythrocyte Membrane ◽

Human Erythrocyte ◽

Band 3 ◽

Anion Transport ◽

Proteolytic Digestion ◽

Transport Activity ◽

Human Erythrocyte Membrane ◽

Anion Transport Activity