Brain membrane protein band 3 performs the same functions as erythrocyte band 3

M. M.B. Kay, J. Hughes, I. Zagon, F. Lin

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

We report the presence of band 3 protein(s) in mammalian brain that performs the same functions as those of erythroid band 3. These functions are anion transport, ankyrin binding, and generation of senescent cell antigen, an aging antigen that terminates the life of cells. Structural similarity of brain and erythroid band 3 is suggested by the reaction of antibodies to synthetic peptides of erythroid band 3 with brain band 3, the inhibition of anion transport by the same inhibitors, and an equal degree of inhibition of brain and erythrocyte anion transport by synthetic peptides of erythroid band 3 (pep-ANION 2, residues 588-602; pep-COOH, residues 812-827; pep-COOH-N6, residues 813-818). One of these segments, pep-COOH, contains antigenic determinants of senescent cell antigen. These findings suggest that the transport domains of erythroid and neural band 3 are similar functionally and structurally and support the hypothesis that the immunological mechanism of maintaining homeostasis is a general physiologic process for removing senescent and damaged cells in mammals and other vertebrates.

Original languageEnglish (US)
Pages (from-to)2778-2782
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number7
DOIs
StatePublished - Jan 1 1991

Fingerprint

Erythrocyte Anion Exchange Protein 1
Membrane Proteins
Erythrocytes
Anions
Brain
Antigens
Ankyrins
Peptides
Cell Aging
Vertebrates
Epitopes
Mammals
Homeostasis
Antibodies

All Science Journal Classification (ASJC) codes

  • General

Cite this

@article{009e558c7ab448eb84fbab9b3a0243ac,
title = "Brain membrane protein band 3 performs the same functions as erythrocyte band 3",
abstract = "We report the presence of band 3 protein(s) in mammalian brain that performs the same functions as those of erythroid band 3. These functions are anion transport, ankyrin binding, and generation of senescent cell antigen, an aging antigen that terminates the life of cells. Structural similarity of brain and erythroid band 3 is suggested by the reaction of antibodies to synthetic peptides of erythroid band 3 with brain band 3, the inhibition of anion transport by the same inhibitors, and an equal degree of inhibition of brain and erythrocyte anion transport by synthetic peptides of erythroid band 3 (pep-ANION 2, residues 588-602; pep-COOH, residues 812-827; pep-COOH-N6, residues 813-818). One of these segments, pep-COOH, contains antigenic determinants of senescent cell antigen. These findings suggest that the transport domains of erythroid and neural band 3 are similar functionally and structurally and support the hypothesis that the immunological mechanism of maintaining homeostasis is a general physiologic process for removing senescent and damaged cells in mammals and other vertebrates.",
author = "Kay, {M. M.B.} and J. Hughes and I. Zagon and F. Lin",
year = "1991",
month = "1",
day = "1",
doi = "10.1073/pnas.88.7.2778",
language = "English (US)",
volume = "88",
pages = "2778--2782",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "7",

}

Brain membrane protein band 3 performs the same functions as erythrocyte band 3. / Kay, M. M.B.; Hughes, J.; Zagon, I.; Lin, F.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 7, 01.01.1991, p. 2778-2782.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Brain membrane protein band 3 performs the same functions as erythrocyte band 3

AU - Kay, M. M.B.

AU - Hughes, J.

AU - Zagon, I.

AU - Lin, F.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - We report the presence of band 3 protein(s) in mammalian brain that performs the same functions as those of erythroid band 3. These functions are anion transport, ankyrin binding, and generation of senescent cell antigen, an aging antigen that terminates the life of cells. Structural similarity of brain and erythroid band 3 is suggested by the reaction of antibodies to synthetic peptides of erythroid band 3 with brain band 3, the inhibition of anion transport by the same inhibitors, and an equal degree of inhibition of brain and erythrocyte anion transport by synthetic peptides of erythroid band 3 (pep-ANION 2, residues 588-602; pep-COOH, residues 812-827; pep-COOH-N6, residues 813-818). One of these segments, pep-COOH, contains antigenic determinants of senescent cell antigen. These findings suggest that the transport domains of erythroid and neural band 3 are similar functionally and structurally and support the hypothesis that the immunological mechanism of maintaining homeostasis is a general physiologic process for removing senescent and damaged cells in mammals and other vertebrates.

AB - We report the presence of band 3 protein(s) in mammalian brain that performs the same functions as those of erythroid band 3. These functions are anion transport, ankyrin binding, and generation of senescent cell antigen, an aging antigen that terminates the life of cells. Structural similarity of brain and erythroid band 3 is suggested by the reaction of antibodies to synthetic peptides of erythroid band 3 with brain band 3, the inhibition of anion transport by the same inhibitors, and an equal degree of inhibition of brain and erythrocyte anion transport by synthetic peptides of erythroid band 3 (pep-ANION 2, residues 588-602; pep-COOH, residues 812-827; pep-COOH-N6, residues 813-818). One of these segments, pep-COOH, contains antigenic determinants of senescent cell antigen. These findings suggest that the transport domains of erythroid and neural band 3 are similar functionally and structurally and support the hypothesis that the immunological mechanism of maintaining homeostasis is a general physiologic process for removing senescent and damaged cells in mammals and other vertebrates.

UR - http://www.scopus.com/inward/record.url?scp=0025862955&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025862955&partnerID=8YFLogxK

U2 - 10.1073/pnas.88.7.2778

DO - 10.1073/pnas.88.7.2778

M3 - Article

C2 - 2011587

AN - SCOPUS:0025862955

VL - 88

SP - 2778

EP - 2782

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 7

ER -