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Localization of ligands for L-selectin in mouse peripheral lymph node high
endothelial cells by colloidal gold conjugates
A Kikuta and SD Rosen
Department of Anatomy, Okayama University Medical School, Japan.
L-selectin, a Ca(2+)-dependent lectin-like receptor, mediates lymphocyte
attachment to high endothelial venules (HEV) of peripheral lymph nodes
(PLN) during the process of lymphocyte homing. Two endothelial-derived
ligands for L-selectin, known as GlyCAM-1 (Sgp50) and CD34 (Sgp90), have
been identified by affinity precipitation of lymph node extracts with a
chimeric molecule that combines the extracellular domains of L-selectin
with the human IgG1 Fc region (L- selectin-IgG) (J Cell Biol 110:2221,
1990). Here, using a histologic probe based on colloidal gold conjugated to
L-selectin-IgG (LS-Ig), we performed morphologic mapping of the HEV ligands
in PLN at both the light and electron microscopic levels. With a
postembedding labeling method, intense LS-Ig-gold staining of PLN HEV was
observed, while the HEV of Peyer's patches (PP) were negative. The
specificity of LS-Ig- gold staining was established by pretreatment of
sections with sialidase and coincubation of sections with EGTA, fucoidin,
or L- selectin-IgG itself. In ultrastructural studies of high endothelial
cells(HEC), gold particles were bound to the trans-Golgi network(TGN) and
to peripheral vesicles in the cytoplasm. Gold labeling was also detected in
a patchy distribution on the entire luminal vascular surface of HEC.
Although the perivascular fibroreticular sheath of HEV was frequently
labeled limited labeling was observed on the basolateral surfaces of the
HEC. In most cases, the HEC membrane surrounding migrating lymphocytes was
negative. These results show that L-selectin ligands pass through the Golgi
apparatus during their biosynthesis, are stored in secretory granules, and
are expressed on the vascular luminal surface of the HEC. A polyclonal
antiserum to GlyCAM-1 intensely stained intracellular organelles in the
biosynthetic pathway including cytoplasmic vesicles, but failed to stain
the cell surface of HEC. Given its presence in serum as a soluble factor,
GlyCAM-1 is likely to be a secretory product.
Volume 84,
Issue 11,
pp. 3766-3775,
12/01/1994
Copyright © 1994 by The American Society of Hematology
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