PMID: 2497782May 19, 1989Paper

Low-pH association of proteins with the membranes of intact red blood cells. I. Exogenous glycophorin and the CD4 molecule

Biochimica Et Biophysica Acta
T ArvinteC Nicolau

Abstract

Glycophorin and CD4 proteins are tightly associated with intact human erythrocyte membranes after a short-time incubation at low pH (1-2 min, pH lower than 5, 37 degrees C). Flow cytometry and epifluorescence microscope observations showed that after incubation of red cells with fluorescein isothiocyanate (FITC) labeled glycophorin at pH values lower than 5, the erythrocyte membrane and subsequently formed ghost membranes were fluorescent. Unlabeled glycophorin was reacted with mouse erythrocytes using the same low-pH conditions. Flow cytometry and fluorescence microscopy showed that anti-glycophorin monoclonal antibodies were able to recognize the epitopes of glycophorin associated with the mouse erythrocytes. Kinetic experiments showed that the interaction of FITC-glycophorin with red cell membranes can be monitored by a decrease in the fluorescence intensity. Erythrocyte associated glycophorin was not removed from the membranes after 24 h incubation in human plasma (in vitro, 39 degrees C). A glycoprotein extract containing CD4 was isolated from a T4-lymphoma cell line (CEM). This protein extract was incubated with erythrocytes using the same low-pH conditions. Fluorescently labeled monoclonal antibodies against CD4 stained ...Continue Reading

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Citations

Oct 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·N R WebbM D Summers
Feb 7, 2001·Clinical Microbiology Reviews·A Alvarez-BarrientosM Sánchez-Pérez
Feb 22, 2012·Cellular & Molecular Biology Letters·Svitlana RozanovaOleg Nardid
Aug 10, 1990·Biochimica Et Biophysica Acta·Y MouneimneC Nicolau
Feb 28, 1989·Biochemical and Biophysical Research Communications·Y MouneimneC Nicolau

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