Galectin 1 modulates attachment, spreading and migration of cultured vascular smooth muscle cells via interactions with cellular receptors and components of extracellular matrix
Ep. Moiseeva et al., Galectin 1 modulates attachment, spreading and migration of cultured vascular smooth muscle cells via interactions with cellular receptors and components of extracellular matrix, J VASC RES, 36(1), 1999, pp. 47-58
Citations number
51
Categorie Soggetti
Cardiovascular & Respiratory Systems","Cardiovascular & Hematology Research
Galectin 1 (Gal-1), a lactose-binding lectin, is a component of vascular ex
tracellular matrix and secreted by human vascular smooth muscle cells (SMCs
). The purpose of this study was to investigate a possible role of Gal-1 in
controlling adhesion and migration of cultured human vascular SMCs, Gal-1
co-localised with laminin and cellular fibronectin in extracellular matrix
(ECM) secreted by cultured human vascular SMCs, Recombinant glutathione S-t
ransferase (GST)-Gal-1 fusion protein bound to laminin and cellular fibrone
ctin in ELISA, GST-Gal-1 inhibited SMC attachment to laminin via interactio
ns with both SMCs and laminin, GST-Gal-1 inhibited SMC spreading on plastic
or on laminin, but not on cellular fibronectin. GST-Gal-1 modulated SMC mi
gration on laminin and inhibited migration on cellular fibronectin. GST-Gal
-1 bound to several S-35-labelled proteins in SMC extracts including lamini
n and alpha 1 beta 1 integrin, identified by depletion of SMC protein extra
cts with respective antibodies. We conclude that Gal-1 is able to modulate
SMC attachment, spreading and migration via interactions with ECM proteins
and alpha 1 beta 1 integrin.