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Blood, 15 August 2001, Vol. 98, No. 4, pp. 925-933
CHEMOKINES
Blocking of c-FLIPL-independent
cycloheximide-induced apoptosis or Fas-mediated apoptosis by the CC
chemokine receptor 9/TECK interaction
Byung-S. Youn,
Young J. Kim,
Charlie Mantel,
Kang-Yeol Yu, and
Hal E. Broxmeyer
From the Department of Microbiology, Department of
Immunology and Medicine, and Department of Biochemistry and Molecular
Biology, Indiana University School of Medicine; and the Walther
Oncology Center, Indianapolis, IN 46202.
Chemokines play a pivotal role in regulating leukocyte migration as
well as other biological functions. CC chemokine receptor 9 (CCR9) is a
specific receptor for thymus-expressed CC chemokine (TECK). It
is shown here that engagement of CCR9 with TECK leads to
phosphorylation of Akt (protein kinase B), mitogen-activated protein kinases (MAPKs), glycogen synthase kinase-3 (GSK-3), and
a forkhead transcription factor, FKHR, in a human T-cell line, MOLT4, that naturally expresses CCR9. By means of chemical inhibitors, it is shown that phosphoinositide-3 kinase (PI-3 kinase), but not MAPK,
is required for CCR9-mediated chemotaxis. Akt, GSK-3, FKHR, and MAPK
have been previously implicated in cell survival signals in response to
an array of death stimuli. When MOLT4 cells, which expressed
Fas as well as CXCR4, were stimulated with cycloheximide (CHX), an
agonistic anti-Fas antibody, or a combination of these, the
cells rapidly underwent apoptosis. However, costimulation of MOLT4
cells with TECK or stromal derived factor-1 significantly blocked
CHX-mediated apoptosis, whereas stimulation only with TECK partially
blocked Fas-mediated apoptosis. Concomitant with this blocking,
cleavage of poly (adenosine 5'-diphosphate-ribose) polymerase and
activation of caspase 3 were significantly attenuated, but the
expression level of FLICE inhibitory protein c-FLIPL, which
had been shown to be regulated by CHX, was unchanged. This demonstrates
that activation of CCR9 leads to phosphorylation of GSK-3 and FKHR
and provides a cell survival signal to the receptor expressing cells
against CHX. It also suggests the existence of a novel pathway leading
to CHX-induced apoptosis independently of c-FLIPL.
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