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Asynchronous synthesis of membrane skeletal proteins during terminal
maturation of murine erythroblasts
M Hanspal, JS Hanspal, R Kalraiya, SC Liu, KE Sahr, D Howard and J Palek
Department of Biomedical Research, St Elizabeth's Hospital of Boston, Tufts
University School of Medicine, MA 02135.
To study the changes in the synthesis of the major membrane skeletal
proteins, their assembly on the membrane, and their turnover during
terminal red blood cell maturation in vivo, we have compared early
proerythroblasts and late erythroblasts obtained from the spleens of mice
at different times after infection with the anemia-inducing strain of
Friend virus (FVA). Metabolic labeling of these cells indicates striking
differences between early and late erythroblasts. In early erythroblasts,
spectrin and ankyrin are synthesized in large amounts in the cytosol with
proportionately high levels of spectrin and ankyrin messenger RNA (mRNA).
In contrast, only small amounts of these polypeptides are incorporated into
the skeleton, which is markedly unstable. In late erythroblasts, however,
the synthesis of spectrin and ankyrin and their mRNA levels are
substantially reduced, yet the net amounts of these polypeptides assembled
in the membrane skeleton are markedly increased, and the membrane skeleton
becomes stable with no detectable protein turnover. The mRNA levels and the
synthesis of the band 3 and 4.1 proteins are increased considerably in
terminally differentiated normoblasts with a concomitant increase in the
net amount and the half-life of the newly assembled spectrin and ankyrin.
Thus, the increased accumulation of spectrin and ankyrin at the late
erythroblast stage is a consequence of an increased recruitment of these
proteins on the membrane and an increase in their stability rather than a
transcriptional upregulation. This is in contrast to band 3 and 4.1
proteins, which accumulate in direct proportion to their mRNA levels and
rates of synthesis. These results suggest a key role for the band 3 and 4.1
proteins in conferring a long-term stability to the membrane skeleton
during terminal red blood cell differentiation.
Volume 80,
Issue 2,
pp. 530-539,
07/15/1992
Copyright © 1992 by The American Society of Hematology
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