Integral band 7 protein of the human erythrocyte membrane.

نویسندگان

  • G W Stewart
  • A C Argent
چکیده

15. Invest. 82,617-723 Ducluzeau, M. T., Guetarni, D., Pothier, B., Baklouti, Gallagher, P. G., Tse, W. T., Marchesi, S. L., F., Ghanem, A., Kastally, R. & Delaunay, J. (1991) Zarkowsky, H. S. & Forget, B. G. (1991) Clin. Res. 39, J. Clin. Invest. 87,2 169-2 177 313A (Abstr.) 16. Speicher, D. W., Werglarz, I,. & DeSilva, T. M. Hanspal, M.. Hanspal, J., Fibach, F. & Palek. J. (1 99 1) (1992) J. Biol. Chem., 267, 14775-14782 Blood 78, (Suppl. l), 84a (Abstr.) Alloisio, N., MorE, I,., Markchal, J., Roux, A. F., 785

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Cytosolic protein binding to band-3 protein inhibits endocytosis of isolated human erythrocyte membranes.

Recent studies of haemoglobin binding to the cytoplasmic side of the erythrocyte membrane have shown that the predominant high-affinity interaction occurs with the major integral membrane protein known as band-3 protein and that this interaction may occur within the intact erythrocyte in a manner regulated by cell pH. We report here that haemoglobin and glyceraldehyde 3-phosphate dehydrogenase ...

متن کامل

Oxygen regulates the band 3-ankyrin bridge in the human erythrocyte membrane.

The oxygenation state of erythrocytes is known to impact several cellular processes. As the only known O2-binding protein in red blood cells, haemoglobin has been implicated in the oxygenation-mediated control of cell pathways and properties. Band 3, an integral membrane protein linked to the spectrin/actin cytoskeleton, preferentially binds deoxygenated haemoglobin at its N-terminus, and has b...

متن کامل

Analysis of integral membrane protein contributions to the deformability and stability of the human erythrocyte membrane.

Three major hypotheses have been proposed to explain the role of membrane-spanning proteins in establishing/maintaining membrane stability. These hypotheses ascribe the essential contribution of integral membrane proteins to (i) their ability to anchor the membrane skeleton to the lipid bilayer, (ii) their capacity to bind and stabilize membrane lipids, and (iii) their ability to influence and ...

متن کامل

RED CELLS Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes

Tyr phosphorylation of the multifunctional transmembrane protein band 3 has been implicated in several erythrocyte functions and disorders. We previously demonstrated that pervanadate treatment of human erythrocytes induces band-3 Tyr phosphorylation, which is catalyzed by the sequential action of tyrosine kinase Syk and tyrosine kinase(s) belonging to the Src family. In this study, we show tha...

متن کامل

Relationship of the human erythrocyte Wrb antigen to an interaction between glycophorin A and band 3.

The Wrb antigen is a high-frequency human erythrocyte antigen invariably absent from En (a-) erythrocytes, which lack glycophorin A. However, glycophorin A from En (a+) Wr (a+b-) red cells has an amino acid sequence identical to that of glycophorin A from Wr (b+) erythrocytes. Evidence has suggested that the Wrb antigen may require the interaction of glycophorin A with either a lipid moiety or ...

متن کامل

Glycophorin A dimerization and band 3 interaction during erythroid membrane biogenesis: in vivo studies in human glycophorin A transgenic mice.

Band 3 and glycophorin A (GPA) are the 2 most abundant integral proteins in the human erythrocyte membrane. Earlier studies suggested that the 2 proteins may associate not only in the mature erythrocyte membrane, but also during their posttranslational processing and intracellular trafficking. The purpose of this study was to directly examine the GPA-band 3 interaction in vivo and determine the...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical Society transactions

دوره 20 4  شماره 

صفحات  -

تاریخ انتشار 1992