Abstract
We have used synthetic peptides to study the location of the amino acid sequences in the human erythrocyte anion transport protein (band 3) which are recognized by four murine monoclonal antibodies, BRIC 130, 132, 154 and 155. These antibodies are known to react with epitopes in the protein which are on the cytoplasmic side of the membrane. The results suggest that the amino acid residues important for the reaction of BRIC 130 and BRIC 154/155 are located within amino acids 899-908 and 895-901 respectively in the cytoplasmic tail of the protein. The BRIC 132 epitope is located within amino acid residues 813-824. This is part of a surface loop in the protein which probably extends from residue 814 to residue 832 and is located on the cytoplasmic side of the membrane. These results provide direct evidence for the topographical location of a sequence in a poorly understood region of the protein.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bjerrum P. J. Chemical modification of the anion-transport system with phenylglyoxal. Methods Enzymol. 1989;173:466–494. doi: 10.1016/s0076-6879(89)73033-0. [DOI] [PubMed] [Google Scholar]
- Cox J. V., Lazarides E. Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter. Mol Cell Biol. 1988 Mar;8(3):1327–1335. doi: 10.1128/mcb.8.3.1327. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DODGE J. T., MITCHELL C., HANAHAN D. J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100:119–130. doi: 10.1016/0003-9861(63)90042-0. [DOI] [PubMed] [Google Scholar]
- Jay D., Cantley L. Structural aspects of the red cell anion exchange protein. Annu Rev Biochem. 1986;55:511–538. doi: 10.1146/annurev.bi.55.070186.002455. [DOI] [PubMed] [Google Scholar]
- Jennings M. L., Anderson M. P., Monaghan R. Monoclonal antibodies against human erythrocyte band 3 protein. Localization of proteolytic cleavage sites and stilbenedisulfonate-binding lysine residues. J Biol Chem. 1986 Jul 5;261(19):9002–9010. [PubMed] [Google Scholar]
- Jennings M. L. Kinetics and mechanism of anion transport in red blood cells. Annu Rev Physiol. 1985;47:519–533. doi: 10.1146/annurev.ph.47.030185.002511. [DOI] [PubMed] [Google Scholar]
- Jennings M. L. Structure and function of the red blood cell anion transport protein. Annu Rev Biophys Biophys Chem. 1989;18:397–430. doi: 10.1146/annurev.bb.18.060189.002145. [DOI] [PubMed] [Google Scholar]
- Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N. Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein. J Biol Chem. 1988 Jun 15;263(17):8232–8238. [PubMed] [Google Scholar]
- Kim H. R., Yew N. S., Ansorge W., Voss H., Schwager C., Vennström B., Zenke M., Engel J. D. Two different mRNAs are transcribed from a single genomic locus encoding the chicken erythrocyte anion transport proteins (band 3). Mol Cell Biol. 1988 Oct;8(10):4416–4424. doi: 10.1128/mcb.8.10.4416. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kopito R. R., Lodish H. F. Primary structure and transmembrane orientation of the murine anion exchange protein. Nature. 1985 Jul 18;316(6025):234–238. doi: 10.1038/316234a0. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lieberman D. M., Nattriss M., Reithmeier R. A. Carboxypeptidase Y digestion of band 3, the anion transport protein of human erythrocyte membranes. Biochim Biophys Acta. 1987 Sep 18;903(1):37–47. doi: 10.1016/0005-2736(87)90153-2. [DOI] [PubMed] [Google Scholar]
- Lieberman D. M., Reithmeier R. A. Localization of the carboxyl terminus of Band 3 to the cytoplasmic side of the erythrocyte membrane using antibodies raised against a synthetic peptide. J Biol Chem. 1988 Jul 15;263(20):10022–10028. [PubMed] [Google Scholar]
- Passow H. Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane. Rev Physiol Biochem Pharmacol. 1986;103:61–203. doi: 10.1007/3540153330_2. [DOI] [PubMed] [Google Scholar]
- Tanner M. J., Martin P. G., High S. The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence. Biochem J. 1988 Dec 15;256(3):703–712. doi: 10.1042/bj2560703. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tanner M. J. Proteolytic cleavage of the anion transporter and its orientation in the membrane. Methods Enzymol. 1989;173:423–432. doi: 10.1016/s0076-6879(89)73030-5. [DOI] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wainwright S. D., Tanner M. J., Martin G. E., Yendle J. E., Holmes C. Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues. Biochem J. 1989 Feb 15;258(1):211–220. doi: 10.1042/bj2580211. [DOI] [PMC free article] [PubMed] [Google Scholar]