@entity9820 (TM) is an integral membrane glycoprotein that is a potent anticoagulant factor. TM may also possess functions distinct from its anticoagulant activity. Here the influence of TM on cell adhesion was studied in TM-negative @entity320 A2058 cells transfected with green fluorescent protein-tagged TM (TMG) or lectin domain-deleted TM (TMG(DeltaL)). Confocal microscopy demonstrated that both TMG and TMG(DeltaL) were distributed in the plasma membrane. TMG-expressed cells grew as closely clustered colonies, with TM localized prominently in the intercellular boundaries. TMG(DeltaL)-expressed cells grew singly. Overexpression of TMG, but not TMG(DeltaL), decreased monolayer permeability in vitro and @entity5 growth in vivo. The cell-to-cell adhesion in TMG-expressed cells was @entity141 -dependent and was inhibited by monoclonal antibody against the lectin-like domain of TM. The effects of TM-mediated cell adhesion were abolished by the addition of @entity3913 , chondroitin sulfate A, or chondroitin sulfate C. In addition, anti-lectin-like domain antibody disrupted the close clustering of the endogenous TM-expressed keratinocyte HaCaT cell line derived from normal @entity1 epidermis. Double-labeling immunofluorescence staining revealed similar distributions of TM and actin filament in the cortex region of the TMG-expressed cells. Thus, TM can function as a @entity141 -dependent cell-to-cell adhesion molecule. Binding of specific carbohydrates to the lectin-like domain is essential for this specific function.

XXXX -mediated cell adhesion: involvement of its lectin-like domain.

@entity1 :: ('9606', 'Species') :: ['human'] @entity5 :: ('MESH:D009369', 'Disease') :: ['tumor'] @entity3913 :: ('MESH:D008358', 'Chemical') :: ['mannose'] @entity9820 :: ('7056', 'Gene') :: ['Thrombomodulin'] @entity141 :: ('CHEBI:29108', 'Chemical') :: ['Ca2+'] @entity320 :: ('MESH:D008545', 'Disease') :: ['melanoma']
@entity9820 :: (7056,Gene) :: ['Thrombomodulin']
