Interaction of membrane skeletal protein, protein 4.1B and p55, and sodium bicarbonate cotransporterl in mouse renal S1-S2 proximal tubules

Nobuo Terada, Nobuhiko Ohno, Sei Saitoh, George Seki, Masayuki Komada, Tatsuo Suzuki, Hisashi Yamakawa, Manoocher Soleimani, Shinichi Ohno

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1199-1206
Number of pages8
JournalJournal of Histochemistry and Cytochemistry
Volume55
Issue number12
DOIs
Publication statusPublished - 12-2007
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Anatomy
  • Histology

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