... internalization is dystroglycan, a laminin receptor that is functionally perturbed in muscular dystrophies and in many cancers. Correspondingly, laminin internalization was found to be deficient in aggressive cancer cells displaying non-functional dystroglycan, and restoration of dystroglycan function strongly...

...Dmitri Leonoudakis; Manisha Singh; Roozbeh Mohajer; Pouya Mohajer; Jimmie E. Fata; Kevin P. Campbell; John L. Muschler Receptors for basement membrane (BM) proteins, including dystroglycan (DG), coordinate tissue development and function by mechanisms that are only partially defined. To further...

...Oliver Thompson; Chris J. Moore; Sadaf-Ahmahni Hussain; Iivari Kleino; Michelle Peckham; Erhard Hohenester; Kathryn R. Ayscough; Kalle Saksela; Steve J. Winder Dystroglycan is a ubiquitously expressed cell adhesion protein. Its principal role has been determined as a component of the dystrophin...

... that the laminin receptor dystroglycan (DG) plays in these processes, we assayed cell responses to laminin-111 following conditional ablation of DG gene ( Dag1 ) expression in cultured mammary epithelial cells. Strikingly, DG loss disrupted laminin-111-induced polarity and β-casein production, and abolished...

...Rita Barresi; Kevin P. Campbell α- and β-dystroglycan constitute a membrane-spanning complex that connects the extracellular matrix to the cytoskeleton. Although a structural role for dystroglycan had been identified, biochemical and genetic discoveries have recently highlighted the significance...

...Peter D. Yurchenco; Yi-Shan Cheng; Kevin Campbell; Shaohua Li Basement membrane laminins bearing the α2-subunit interact with α-dystroglycan and β1-integrins, cell-surface receptors that are found within the rectilinear costameric lattices of skeletal muscle sarcolemma. Mutations of the α2 subunit...

... and non-muscle tissues and is now considered to be not only a mechanical component of cells, but also a highly dynamic multifunctional structure that can serve as a scaffold for signaling proteins ( Rando, 2001 ). The DPC can be subdivided into three distinct sub-complexes: the dystroglycan complex...

...Hiroshi Hosokawa; Haruaki Ninomiya; Yukisato Kitamura; Keigi Fujiwara; Tomoh Masaki We have earlier shown that dystroglycan (DG) is a lamininbinding protein and as such is a cell adhesion molecule. DG is a heterodimer of α andβ DG subunits. β-dystroglycan (βDG) is the membrane spanning subunit...

...-integrin laminin receptors, dystroglycan and the polypeptide on which the Lutheran blood group antigens are expressed, are also often colocalized with CD151, but no association with CD151-α3β1 complexes was found with biochemical analysis. The anti-CD151 antibody TS151R detects an epitope at a site...

... by laminin polymerization. Assembly of one, a densely-distributed reticular matrix, was accompanied by a redistribution of cell-surface dystroglycan and cytoskeletal utrophin into matrix-receptor-cytoskeletal complexes. The other, a fibrillar matrix,accumulated in separate zones associated with pre-existing...