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Blood, Vol. 93 No. 11 (June 1), 1999:
pp. 3723-3735
A Common Signaling Pathway Via Syk and Lyn Tyrosine Kinases Generated
From Capping of the Sialomucins CD34 and CD43 in Immature Hematopoietic
Cells
Jun-ichi Tada,
Mitsuhiro Omine,
Toshio Suda, and
Naoto Yamaguchi
From the Department of Cell Differentiation, Institute of Molecular
Embryology and Genetics, Kumamoto University School of Medicine,
Kumamoto, Japan; and the Division of Hematology, Fujigaoka Hospital,
Showa University School of Medicine, Yokohama, Japan.
The sialomucin CD34 is a useful marker for hematopoietic
stem/progenitor cells. However, the role of CD34 remains poorly
understood. Here we investigate the functions of CD34 and another
sialomucin CD43 coexpressed on hematopoietic stem/progenitor cells.
Stimulation of undifferentiated hematopoietic KG1a cells with anti-CD34
or anti-CD43 induced homotypic cytoadhesion, accompanied by formation of a long-lived cap of CD34 and CD43 respectively, which colocalized with F-actin. Stimulation with either antibody specifically increased tyrosine phosphorylation of the identical set of proteins of Lyn, Syk,
pp60, pp69, and pp77 at the capping site. These events were similar to
those observed in monocytic U937 cells ectopically expressing CD34.
After stimulation of KG1a cells, coimmunoprecipitation of Lyn with pp69
and pp77 and of Syk with pp37 was detected in the membrane fraction.
Blockade of antibody-induced cap formation by treatment with
cytochalasin D leads to inhibition of tyrosine phosphorylation of Syk
and pp77 and homotypic cytoadhesion. Moreover, normal human
CD34+ bone marrow cells showed cap formation of CD34 or
CD43 after stimulation. These results suggest that crosslinking of
either CD34 or CD43 activates the same signaling pathway for
cytoadhesion through Lyn, Syk, and the novel tyrosine-phosphorylated
proteins within hematopoiesis.
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