TY - JOUR
T1 - A 45-kDa protein antigenically related to band 3 is selectively expressed in kidney mitochondria
AU - Ostedgaard, Lynda S.
AU - Jennings, Michael L.
AU - Karniski, Lawrence P.
AU - Schuster, Victor L.
PY - 1991
Y1 - 1991
N2 - Anion exchange similar to that catalyzed by erythrocyte band 3 occurs across many nonerythroid cell membranes. To identify anton-exchange proteins structurally related to band 3, we immunobtotted rabbit kidney medullary membrane fractions with anti-band 3 antibodies. Immunoblots using antibodies to the cytoplasmic domain of band 3 revealed cross-reactive proteins in the plasma membrane fraction only. In contrast, two monoclonal antibodies against band 3 membrane domain labeled a 45-kDa protein; further immunoblotting and immunogold studies of membrane fractions and kidney sections using one of the anti-membrane domain antibodies showed that labeling was strongest in mitochondria of H+-secreting collecting duct cells. Tissue-to-tissue expression of the 45-kDa mitochondrial protein was variable: kidney medulla > heart > kidney cortex ≫ liver. We conclude that a 45-kDa protein with immunological cross-reactivity to the erythrocyte band 3 membrane domain is expressed in mitochondria in a highly cell-specific fashion and speculate that the protein may play a role in mitochondrial anion transport. (.
AB - Anion exchange similar to that catalyzed by erythrocyte band 3 occurs across many nonerythroid cell membranes. To identify anton-exchange proteins structurally related to band 3, we immunobtotted rabbit kidney medullary membrane fractions with anti-band 3 antibodies. Immunoblots using antibodies to the cytoplasmic domain of band 3 revealed cross-reactive proteins in the plasma membrane fraction only. In contrast, two monoclonal antibodies against band 3 membrane domain labeled a 45-kDa protein; further immunoblotting and immunogold studies of membrane fractions and kidney sections using one of the anti-membrane domain antibodies showed that labeling was strongest in mitochondria of H+-secreting collecting duct cells. Tissue-to-tissue expression of the 45-kDa mitochondrial protein was variable: kidney medulla > heart > kidney cortex ≫ liver. We conclude that a 45-kDa protein with immunological cross-reactivity to the erythrocyte band 3 membrane domain is expressed in mitochondria in a highly cell-specific fashion and speculate that the protein may play a role in mitochondrial anion transport. (.
KW - Anion exchange
KW - Renal acidification
UR - http://www.scopus.com/inward/record.url?scp=0026031479&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026031479&partnerID=8YFLogxK
U2 - 10.1073/pnas.88.3.981
DO - 10.1073/pnas.88.3.981
M3 - Article
C2 - 1704136
AN - SCOPUS:0026031479
SN - 0027-8424
VL - 88
SP - 981
EP - 985
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
IS - 3
ER -