Identification of human endomucin-1 and -2 as membrane-bound O-sialoglycoproteins with anti-adhesive activity.
Using a signal sequence trap method and database search, we identified a series of human cDNAs encoding two structurally related type I membrane proteins of approximately 25 kDa with multiple glycosylation motifs. These genes, termed endomucin-1/-2, are expressed in several human tissues including heart, kidney, and lung. Exogenously expressed human ... endomucin-1/-2 proteins were modified into 80-120 kDa glycoproteins, which were susceptible to O-sialoglycoprotein endopeptidase digestion. Transient overexpression of endomucin-1/-2 reduced the number of adhesion plaques and reduced cell attachment to the substrate. This phenotype was suppressed by laminin or the protein kinase inhibitor staurosporine. Our findings suggest that human endomucin-1/-2 negatively regulate cell adhesion to the extracellular matrix.
Mesh Terms:
Amino Acid Sequence, Animals, Cell Adhesion, Cell Line, Cell Membrane, Cell Size, Cloning, Molecular, DNA, Complementary, Extracellular Matrix Proteins, Fluorescent Antibody Technique, Focal Adhesions, Gene Expression Profiling, Glycosylation, Humans, Mice, Molecular Sequence Data, Mucins, Protein Transport, RNA, Messenger, Recombinant Fusion Proteins, Sequence Alignment, Sialoglycoproteins, Sialomucins, Staurosporine
Amino Acid Sequence, Animals, Cell Adhesion, Cell Line, Cell Membrane, Cell Size, Cloning, Molecular, DNA, Complementary, Extracellular Matrix Proteins, Fluorescent Antibody Technique, Focal Adhesions, Gene Expression Profiling, Glycosylation, Humans, Mice, Molecular Sequence Data, Mucins, Protein Transport, RNA, Messenger, Recombinant Fusion Proteins, Sequence Alignment, Sialoglycoproteins, Sialomucins, Staurosporine
FEBS Lett.
Date: Jun. 15, 2001
PubMed ID: 11418125
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