Document Detail

E-selectin-dependent adhesion efficiency of colonic carcinoma cells is increased by genetic manipulation of their cell surface lysosomal membrane glycoprotein-1 expression levels.
MedLine Citation:
PMID:  7685349     Owner:  NLM     Status:  MEDLINE    
Lysosomal membrane glycoprotein (lamp)-1 and lamp-2 are the most abundant glycoproteins within the lysosomal membrane. A small amount of lamp-1 and lamp-2 molecules, however, can be present on the cell surface. We have shown previously that highly metastatic colonic carcinoma L4 cells express more lamp-1 and lamp-2 on the cell surface than low metastatic SP cells (Saitoh, O., Wang, W.-L., Lotan, R., and Fukuda, M. (1992) J. Biol. Chem. 267, 5700-5711). Since lamp-1 and lamp-2 are the major carriers for poly-N-acetyllactosamines that are able to display sialyl-Le(x) termini, we sought to determine if an increased amount of lamp-1 on the cell surface would lead to increased expression of cell surface sialyl-Le(x) determinants and to the increased adhesion of those cells to E-selectin. Expression of increased amounts of lamp-1 on the cell surface was achieved either by overexpression of lamp-1 or by expressing a mutant lamp-1 molecule preferentially at the plasma membrane, rather than in lysosomes. Cells that express variable amounts of cell surface lamp-1 were tested for their adhesion to activated endothelial cells or E-selectin expressing Chinese hamster ovary cells. The results clearly show that the extent of adhesion to E-selectin and cell surface sialyl-Le(x) determinants is proportional to the amount of cell surface lamp-1. Moreover, it was demonstrated that such adhesion can be inhibited by soluble lamp-1 generated from Chinese hamster ovary cells expressing sialyl-Le(x) structures. These results indicate that lamp-1 can efficiently present ligands for E-selectin and at the same time can be a useful reagent for inhibition of E-selectin (and possibly P-selectin)-mediated interaction.
R Sawada; J B Lowe; M Fukuda
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  268     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1993 Jun 
Date Detail:
Created Date:  1993-07-13     Completed Date:  1993-07-13     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  12675-81     Citation Subset:  IM    
La Jolla Cancer Research Foundation, California 92037.
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MeSH Terms
Antigens, CD*
Antigens, CD15 / biosynthesis,  metabolism*
Base Sequence
CHO Cells
Carbohydrate Conformation
Carbohydrate Sequence
Cell Adhesion*
Cell Adhesion Molecules / metabolism*
Colonic Neoplasms
DNA Mutational Analysis
Endothelium, Vascular / metabolism
Flow Cytometry
Gene Expression
Gene Library
Interleukin-1 / pharmacology
Lysosome-Associated Membrane Glycoproteins
Membrane Glycoproteins / biosynthesis,  metabolism*
Molecular Sequence Data
Tumor Cells, Cultured
Grant Support
Reg. No./Substance:
0/Antigens, CD; 0/Antigens, CD15; 0/Cell Adhesion Molecules; 0/E-Selectin; 0/Interleukin-1; 0/Lysosome-Associated Membrane Glycoproteins; 0/Membrane Glycoproteins; 0/Oligodeoxyribonucleotides; 9007-49-2/DNA

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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