PMID: 2107104Jan 1, 1990Paper

Thrombospondin binding by keratinocytes: modulation under conditions which alter thrombospondin biosynthesis

Dermatologica
B L RiserV M Dixit

Abstract

Our recent studies have shown that thrombospondin (TSP) is a potent adhesion factor for normal human keratinocytes. Stimulation of adhesion is presumed to result from the binding of TSP to high-affinity receptors on the surface of responsive cells. The present study indicates that keratinocytes bind TSP in a receptor-like manner. Binding is time- and concentration-dependent, saturable, reversible and specific. Approximately 180 ng of TSP can be bound per 1 x 10(5) cells at saturation and half-maximal binding occurs at 22 nM. A series of monoclonal antibodies to various regions of the TSP molecule were examined for effects on TSP binding and TSP-induced adhesion. An antibody directed against the heparian-binding domain of the TSP molecule significantly inhibited TSP binding but had no effect on adhesion. In contrast, three antibodies which recognize epitopes in the 140-kDa fragment of the molecule inhibited both binding and adhesion. In a previous study we showed that treatment of keratinocytes with interferon-gamma inhibited TSP production and inhibited adhesion under unstimulated conditions as well as in response to TSP. The present study shows that interferon-gamma also inhibits TSP binding by keratinocytes. When the data fro...Continue Reading

Citations

Jul 1, 1991·Experimental Cell Research·J VaraniP A Ward
Aug 5, 2004·The Journal of Biological Chemistry·Maria J CalzadaDavid D Roberts
Jun 1, 1993·The Journal of Investigative Dermatology·A ReanoD Schmitt

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