Human osteoclast-like cells recognize laminin via an RGD independent mechanism.
Interactions between cells from human giant cell tumors of bone and the extracellular matrix protein laminin were studied. Cells were capable of recognizing this substratum via a RGD-independent mechanism. Recognition induces adhesion and spreading onto laminin. This protein triggered the release of cellular FN which in turn enhanced recruitment of the beta 1 chain-containing integrin receptor.
Colucci
S
S
Istituto di Anatomia Umana Normale, Università di Bari.
Grano
M
M
Zigrino
P
P
Santacroce
G
G
Zambonin
G
G
Teti
A
A
Zambonin Zallone
A
A
D000595:Amino Acid Sequence; D001859:Bone Neoplasms / Q000473:pathology; D002448:Cell Adhesion / Q000187:drug effects; D005353:Fibronectins / Q000378:metabolism; D018212:Giant Cell Tumor of Bone / Q000473:pathology; D006801:Humans; D019012:Integrin beta1; D016023:Integrins / Q000378:metabolism; D007797:Laminin / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology*; D010010:Osteoclasts / Q000187:drug effects / Q000378:metabolism*; D017474:Receptors, Laminin / Q000378:metabolism; D014407:Tumor Cells, Cultured
D005353:Fibronectins; D019012:Integrin beta1; D016023:Integrins; D007797:Laminin; D009842:Oligopeptides; D017474:Receptors, Laminin; C047981:arginyl-glycyl-aspartic acid; C058161:glycyl-arginyl-glycyl-aspartyl-seryl-proline; C058347:glycyl-arginyl-glycyl-glutamyl-seryl-proline