TY - JOUR
T1 - Interaction of membrane skeletal protein, protein 4.1B and p55, and sodium bicarbonate cotransporterl in mouse renal S1-S2 proximal tubules
AU - Terada, Nobuo
AU - Ohno, Nobuhiko
AU - Saitoh, Sei
AU - Seki, George
AU - Komada, Masayuki
AU - Suzuki, Tatsuo
AU - Yamakawa, Hisashi
AU - Soleimani, Manoocher
AU - Ohno, Shinichi
N1 - Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/12
Y1 - 2007/12
N2 - Our recent studies demonstrated the localization of protein 4.1B, a member of the 4.1 skeletal membrane proteins, to the basolateral membranes of the S1-S2 renal proximal tubules. In the present studies, we investigated the presence of binding partners that could form a molecular complex with the 4.1B protein. Immunohistochemistry revealed the localization of p55, a membrane-associated guanylate kinase, and the sodium bicarbonate cotransporterl (NBC1), to the basolateral membrane domain of S1-S2 in mouse renal proximal tubules. Using immunoprecipitation of kidney lysates with anti-p55 antibody, a positive band was blotted with anti-4.1B antibody. GST fusion proteins including the NBC1 and 4.1B regions were confirmed to bind with each other by electrophoresis after mixing. Both NBC1- and 4.1B-specific bands were detected in renal protein mixtures immunoprecipated by either anti-4.1 B- or NBC1-specific antibodies. It is likely that NBC1,4.1 B, and p55 form a molecular complex in the basolateral membrane of the kidney S1-S2 proximal tubules. We propose that the 4.1B-containing membrane skeleton may play a role in regulating the Na + and HCO3- reabsorption in S1-S2 proximal tubules.
AB - Our recent studies demonstrated the localization of protein 4.1B, a member of the 4.1 skeletal membrane proteins, to the basolateral membranes of the S1-S2 renal proximal tubules. In the present studies, we investigated the presence of binding partners that could form a molecular complex with the 4.1B protein. Immunohistochemistry revealed the localization of p55, a membrane-associated guanylate kinase, and the sodium bicarbonate cotransporterl (NBC1), to the basolateral membrane domain of S1-S2 in mouse renal proximal tubules. Using immunoprecipitation of kidney lysates with anti-p55 antibody, a positive band was blotted with anti-4.1B antibody. GST fusion proteins including the NBC1 and 4.1B regions were confirmed to bind with each other by electrophoresis after mixing. Both NBC1- and 4.1B-specific bands were detected in renal protein mixtures immunoprecipated by either anti-4.1 B- or NBC1-specific antibodies. It is likely that NBC1,4.1 B, and p55 form a molecular complex in the basolateral membrane of the kidney S1-S2 proximal tubules. We propose that the 4.1B-containing membrane skeleton may play a role in regulating the Na + and HCO3- reabsorption in S1-S2 proximal tubules.
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U2 - 10.1369/jhc.7A7266.2007
DO - 10.1369/jhc.7A7266.2007
M3 - Article
C2 - 17712176
AN - SCOPUS:36349037047
VL - 55
SP - 1199
EP - 1206
JO - Journal of Histochemistry and Cytochemistry
JF - Journal of Histochemistry and Cytochemistry
SN - 0022-1554
IS - 12
ER -