[Role of tripeptide Arg-Gly-Asp (RGD) on adhesiveness of human pancreatic cancer cell, PANC-1 to extracellular matrix].
Tumor cell invasion and metastasis are likely to be complex processes involving a variety of cell surface receptors mediating interactions with a number of extracellular matrix molecules, including fibronectin, laminin, and collagen. We have applied this interaction of receptors for specific adhesive substrates in vitro, using specific monoclonal antibody and biologically active synthetic peptides with human pancreatic carcinoma cell, PANC-1. Tripeptide Arg-Gly-Asp (RGD) inhibited adhesion on PANC-1 cells to fibronectin but less effective in blocking adhesion to laminin and collagen, although anti beta 1-integrin antibody significantly inhibited adhesion of fibronectin but less inhibited to laminin, collagen. Our studies emphasize the importance of synthetic tripeptide RGD in adhesion on PANC-1 to extracellular matrix protein, as well as indicating the specificity of cell surface receptor, beta 1 integrin.
Sogabe
T
T
First Department of Surgery, Osaka City University Medical School.
Nishimura
S
S
Chung
Y S
YS
Sowa
M
M
D000595:Amino Acid Sequence; D002448:Cell Adhesion; D005109:Extracellular Matrix / Q000502:physiology*; D006801:Humans; D016023:Integrins / Q000502:physiology; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology*; D010190:Pancreatic Neoplasms / Q000473:pathology*; D014407:Tumor Cells, Cultured
D016023:Integrins; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid