Compounds > glycyl-arginyl-glycyl-glutamyl-seryl-proline

glycyl-arginyl-glycyl-glutamyl-seryl-proline and Bone-Neoplasms

glycyl-arginyl-glycyl-glutamyl-seryl-proline has been researched along with Bone-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for glycyl-arginyl-glycyl-glutamyl-seryl-proline and Bone-Neoplasms

Article	Year
Human osteoclast-like cells recognize laminin via an RGD independent mechanism. Bollettino della Societa italiana di biologia sperimentale, 1993, Volume: 69, Issue:5 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. Topics: Amino Acid Sequence; Bone Neoplasms; Cell Adhesion; Fibronectins; Giant Cell Tumor of Bone; Humans; Integrin beta1; Integrins; Laminin; Molecular Sequence Data; Oligopeptides; Osteoclasts; Receptors, Laminin; Tumor Cells, Cultured	1993

Article

Year

Human osteoclast-like cells recognize laminin via an RGD independent mechanism.

Bollettino della Societa italiana di biologia sperimentale, 1993, Volume: 69, Issue:5

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.

Topics: Amino Acid Sequence; Bone Neoplasms; Cell Adhesion; Fibronectins; Giant Cell Tumor of Bone; Humans; Integrin beta1; Integrins; Laminin; Molecular Sequence Data; Oligopeptides; Osteoclasts; Receptors, Laminin; Tumor Cells, Cultured

1993