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Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the
red blood cell [see comments]
JC Pinder, A Chung, ME Reid and WB Gratzer
Medical Research Council Muscle and Cell Motility Unit, King's College,
London, UK.
The identity of the membrane binding sites for the membrane cytoskeletal
protein 4.1 of the human red blood cell has been investigated. Exhaustive
proteolysis of the membrane with a range of proteases led to the
elimination of only some 60% of all binding sites. The predominant integral
membrane protein, band 3, as well as glycophorin A, was totally digested at
levels of proteolysis that were essentially without effect on the number of
4.1 binding sites. Proteolysis caused scission of the polypeptide chain of
glycophorin C (together with the minor product, glycophorin D, of the same
gene), but left a fragment from the region of the C-terminus still attached
to the membrane. We have found a low-molecular weight protein, possessing
an epitope (recognized by an antibody directed against the cytoplasmic
domain of glycophorin C) in common with this proteolytic fragment, in cells
of a Leach phenotype, which are characterized by lack of extracellular
epitopes of glycophorin C. When these membranes were extracted at low ionic
strength to dissociate the membrane cytoskeleton, approximately half the
content of 4.1 was liberated, compared with only some 25% from normal
membranes. Cells of a different variant of the Leach phenotype, which are
totally devoid of glycophorin C, lost close to 70% of their 4.1 under these
circumstances. The Rh(D) transmembrane protein, which interacts with the
membrane cytoskeleton, is also resistant to proteolysis of the cytoplasmic
membrane surface, but Rhnull cells, devoid of this protein, showed no
decreased retention of 4.1. The results suggest that glycophorin C (with D)
may contain two types of binding site for 4.1, which would be sufficient in
number to account for all the strong binding of 4.1 on normal membranes;
modulation of binding at one of the sites by another protein or by lipid is
not excluded. A possible site for reinitiation of translation overlapping
the premature stop codon in the mutant expressing the truncated glycophorin
C can be discerned.
Volume 82,
Issue 11,
pp. 3482-3488,
12/01/1993
Copyright © 1993 by The American Society of Hematology
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