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Apoptosis, or programmed cell death (PCD), recently has emerged
as an important homeostatic mechanism within several hematopoietic
lineages. This process is subject to both positive and negative
modulation by cytokines and within the erythroid lineage is inhibited
by interleukin-3, stem cell factor, and erythropoietin (Epo). Through
the expression of carboxyl-truncated Epo receptor mutants in FDC-P1
cells, a receptor form possessing 80 membrane-proximal cytoplasmic
residues is shown to efficiently mediate Epo-dependent inhibition of
PCD. This is in contrast to previous studies that attributed this
activity to a distal carboxyl-terminal receptor subdomain (and/or
heterodimerization of wild type Epo receptors with a truncated
non-functional receptor form). Epo-dependent inhibition of PCD also is
shown to be blocked by ectopic expression of kinase-deficient
dominant-negative forms of Jak2 (Jak2
Volume 270,
Number 24,
Issue of June 16, pp. 14500-14504, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
VIII and Jak2-829),
further underlining a role of this membrane-proximal subdomain of the
Epo receptor in the inhibition of PCD. To our knowledge, this comprises
the first direct evidence for an essential role for a Jak tyrosine
kinase (Jak2) in this apoptotic response pathway.
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