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Absence of high-affinity band 4.1 binding sites from membranes of
glycophorin C- and D-deficient (Leach phenotype) erythrocytes
P Gascard and CM Cohen
Department of Biomedical Research, St Elizabeth's Medical Center, Boston,
MA 02135.
We investigated the role of glycophorins C and D in the association of band
4.1 with the erythrocyte membrane by measuring the binding of band 4.1 to
erythrocyte inside-out vesicles stripped of endogenous band 4.1. Vesicles
were prepared from either normal erythrocytes or erythrocytes completely
lacking glycophorins C and D (Leach phenotype). Band 4.1 binding to
vesicles from normal erythrocytes gave rise to a nonlinear Scatchard plot,
indicative of two classes of binding sites: a low- capacity, high-affinity
class of sites (about 10% of the total) and a high-capacity, low-affinity
class of sites. Vesicles prepared from Leach erythrocytes had a binding
capacity for band 4.1 that was, on average, 32% lower than that of vesicles
from normal erythrocytes. This difference was caused by the complete
absence of the high-affinity binding sites as well as by a decrease in the
number of low-affinity binding sites. Reduction of membrane
phosphatidylinositol 4,5- biphosphate (PIP2) content by adenosine
triphosphate depletion or activation of phosphoinositidase C resulted in a
decrease in band 4.1 binding capacity to a similar extent in both control
and Leach vesicles. The principal effect of PIP2 depletion was a reduction
in the number of low-affinity band 4.1 binding sites in control and Leach
vesicles. The fact that PIP2 depletion induced a decrease in band 4.1
binding to Leach vesicles shows that glycophorin C or D is not required for
the formation of PIP2-sensitive band 4.1 binding sites, and may not be
involved in PIP2-sensitive band 4.1 binding sites even when they are
present. Our studies give new insights into the involvement of glycophorins
and of PIP2 in modulating cytoskeletal-membrane interactions.
Volume 83,
Issue 4,
pp. 1102-1108,
02/15/1994
Copyright © 1994 by The American Society of Hematology
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