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J Biol Chem, Vol. 273, Issue 5, 2517-2525, January 30, 1998
From the Pacific Northwest Research Foundation, Seattle, Washington
98122 and the Departments of Pathobiology and Microbiology,
University of Washington, Seattle, Washington 98195
Undifferentiated human embryonal carcinoma cells
are characterized by high expression of
lactoneotetraosylceramide (nLc4), globoside
(Gb4), and extended globo-series glycosphingolipids (GSLs) termed
"stage-specific embryonic antigens 3 and 4" (SSEA-3 and -4).
Expression of these GSLs declines in association with a decline of
homotypic adhesion during the differentiation process. Therefore, these
GSLs may play an essential role in adhesion among these cells. As an
example, human embryonal carcinoma 2102 cells display strong adhesion
to plates coated with Gb4 ("Gb4-dependent cell
adhesion"). This adhesion, which simulates homotypic 2102 cell
aggregation, is based on interaction between Gb4 and nLc4, or between Gb4 and GalGb4 (IV3GalGb4; the major SSEA-3
epitope), as indicated by the following observations: (i) adhesion of
2102 cells or GSL-liposomes to GSL-coated plates in various
combinations; (ii) inhibition of Gb4-dependent 2102 cell
adhesion by preincubation of cells with anti-SSEA-3 or
anti-nLc4 antibodies, or by pretreatment of Gb4-coated
plates with aqueous micellar solution of nLc4 or GalGb4;
(iii) decline of the cell adhesion in association with retinoic
acid-induced differentiation, whereby SSEA-3 and nLc4
levels are reduced. Since cell adhesion is an essential prerequisite
for induction of differentiation, as observed at each step of
embryogenesis, expression of seven transcription factors following
adhesion of 2102 cells to Gb4-coated plates, and to detergent-insoluble
substrate adhesion matrix prepared from 2102 cells, were studied. In
both types of adhesion, a strong enhancement of AP1 and CREB site
binding activity was observed during the early stage (15-60 min
following initial adhesion). Although 2102 cells showed strong adhesion
to Gg3-coated plates, based on interaction between Gg3 and Gb4,
adhesion of the cells to Gg3 did not cause changes of AP1 and CREB
activity. No other transcription factors showed changes induced by Gg3-
or Gb4-dependent adhesion.
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