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Blood, Vol. 93 No. 5 (March 1), 1999:
pp. 1540-1548
H-Ras Is Involved in the Inside-out Signaling Pathway of
Interleukin-3-Induced Integrin Activation
Hirohiko Shibayama,
Naoyuki Anzai,
Stephen E. Braun,
Seiji Fukuda,
Charlie Mantel, and
Hal E. Broxmeyer
From the Departments of Microbiology/Immunology, Medicine, and the
Walther Oncology Center, Indiana University School of Medicine,
Indianapolis; and the Walther Cancer Institute, Indianapolis, IN.
The proto-oncogene product, p21ras, has been implicated
in the cellular mechanism of adhesion, although its precise role has been controversial. Numerous cytokines and growth-factors activate Ras,
which is an important component of their growth-promoting signaling
pathways. On the other hand, the role of Ras in cytokine-induced adhesion has not been elucidated. We therefore investigated the function of H-Ras in the inside-out signaling pathway of interleukin-3 (IL-3)-induced integrin activation in the murine Baf3 cell line after
transfection of cells with either constitutively active, dominant-negative, or wild-type H-Ras cDNAs. Adhesion of Baf3 cells to
fibronectin was induced by IL-3 in a dose-dependent manner via very
late antigen-4 (VLA-4;  4 1 integrins) and VLA-5
(51 integrins) activation. On the other hand, IL-4 did not induce the adhesion of Baf3 cells to fibronectin, although IL-4 did stimulate the cell proliferation of Baf3 cells. Constitutively active
H-Ras-transfected Baf3 cells adhered to fibronectin without IL-3
stimulation through VLA-4 and VLA-5, whereas dominant-negative
H-Ras-transfected Baf3 cells showed significantly less adhesion
induced by IL-3 compared with wild-type and constitutively active
H-Ras-transfected Baf3 cells. Anti-1 integrin antibody (clone;
9EG7), which is known to change integrin conformation and activate
integrins, induced the adhesion of dominant-negative
H-Ras-transfected Baf3 cells as much as the other types of
H-Ras-transfected Baf3 cells. 8-Br-cAMP, Dibutyryl-cAMP, Ras-Raf-1
pathway inhibitors, and PD98059, a MAPK kinase inhibitor, suppressed
proliferation and phosphorylation of MAPK detected by Western blotting
with anti-phospho-MAPK antibody, but not adhesion of any type of
H-Ras-transfected Baf3 cells, whereas U-73122, a phospholipase C (PLC)
inhibitor, suppressed adhesion of these cells completely. These data
indicate that H-Ras and PLC, but not Raf-1, MAPK kinase, or the MAPK
pathway, are involved in the inside-out signaling pathway of
IL-3-induced VLA-4 and VLA-5 activation in Baf3 cells.
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