scholarly journals Affinity and Kinetic Analysis of L-selectin (CD62L) Binding to Glycosylation-dependent Cell-adhesion Molecule-1

1998 ◽  
Vol 273 (2) ◽  
pp. 763-770 ◽  
Author(s):  
Martin W. Nicholson ◽  
A. Neil Barclay ◽  
Mark S. Singer ◽  
Steven D. Rosen ◽  
P. Anton van der Merwe
Keyword(s):  
Cell Adhesion ◽  
Kinetic Analysis ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dependent Cell ◽  
Cell Adhesion Molecule 1

scholarly journals Glycosylation dependent cell adhesion molecule 1-like protein and l-selectin expression in sheep interplacentomal and placentomal endometrium

Reproduction ◽  
2006 ◽  
Vol 131 (4) ◽  
pp. 751-761 ◽  
Author(s):  
Jésus J Muniz ◽  
Margaret M Joyce ◽  
James D Taylor ◽  
James R Burghardt ◽  
Robert C Burghardt ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Smooth Muscle Actin ◽  
Alpha Smooth Muscle Actin ◽  
Stromal Fibroblasts ◽  
Pregnant Sheep ◽  
Dependent Cell ◽  
Cell Adhesion Molecule 1

Glycosylation dependent cell adhesion molecule 1 (GlyCAM-1), a mucin component of sheep histotroph produced by glandular epithelium (GE) during early pregnancy, is hypothesized to function in implantation. However, GlyCAM-1 is present in uterine tissues subsequent to implantation suggesting additional functions of thisl-selectin-binding ligand. This study focused on uterine GlyCAM-1 expression during placentome development in sheep. Western blot analysis of day 50 pregnant sheep identified 45, 40, and 25 kDa bands in interplacentomal endometrium, 40 and 25 kDa bands in placentomes, and 80 and 40 kDa bands in chorioallantois. The GlyCAM-1 proteins in interplacentomal regions were comparable to those detected in day 15–19 pregnant sheep, however, the 80 kDa form was unique to chorioallantois, and the absence of the 45 kDa GlyCAM-1 in placentomes indicated differences between interplacentomal and placentomal endometrium. Immunofluorescence identified GlyCAM-1 in lumenal epithelium (LE), stromal fibroblasts, and vascular smooth muscle cells. To better define its cellular distribution, GlyCAM-1 was co-localized with either epithelium-specific cytokeratin, smooth muscle-specific alpha-smooth muscle actin (α SMA), or stromal-specific vimentin. In interplacentomal endometrium, GlyCAM-1 co-localized with cytokeratin in LE but not in GE. GlyCAM-1 did not co-localize with α SMA, and was localized in the extracellular matrix of vimentin-positive stroma. In placentomes, GlyCAM-1 did not co-localize with cytokeratin, but did co-localize with α SMA and vimentin. Thus, in contrast to interplacentomal regions, GlyCAM-1 in placentomes was predominantly localized in vasculature rather than epithelial cells. Further, leukocytes expressing L-selectin were localized to the endothelial surface of GlyCAM-1-expressing vessels within placentomes. These data suggest that GlyCAM-1 assumes distinct functions in compartment-specific regions of the sheep uterus.

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