title: Organ-specific adhesion of neuroblastoma cells in vitro: correlation with their hepatic metastasis potential.
abstract: Neuroblastoma (NB) is the most common solid malignant tumor found in pediatric patients and the liver is one of the major sites of metastasis. To investigate the organ specificity of metastatic distribution, the adherence behavior of tumor cells was studied. The data presented are based on studies using a metastatic murine cell line C1300. In vivo, not only intrasplenic but also intravascular injection of C1300 NB cells consistently results in hepatic metastasis formation in syngeneic A/J mice. An in vitro assay was used in which C1300 NB cell attachment to cryostat sections of liver, spleen, brain, kidney and lung obtained from normal A/J mice was measured to compare organ-specific adhesion. A good correlation was found between their metastatic potential in the liver and the adhesion to the liver sections; C1300 NB cells adhered preferentially to liver cryostat sections. Enzyme assays indicated that cell surface glycoproteins were involved in cell adhesion. An adhesion assay with extracellular matrix proteins demonstrated that C1300 NB cells adhered preferentially to vitronectin and fibronectin, and the adherence was strongly inhibited by Arg-Gly-Asp (RGD)-containing peptides. Furthermore, adhesion of C1300 NB cells to liver cryostat sections could be blocked by the synthetic peptide GRGDS. This indicates that the interaction between RGD-containing matrix adhesion protein and cells has an important role for the specific adhesion of C1300 NB cells. The results suggested that tumor cell adhesion to liver cryostat sections could provide a useful tool in the study of host-tumor interactions in the metastasis of NB.
authors.affiliation: Department of Surgery 1, The Jikei University School of Medicine, Tokyo, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Kuwashima
mesh_terms: D000818:Animals; D002448:Cell Adhesion; D016326:Extracellular Matrix Proteins / Q000502:physiology; D005260:Female; D005353:Fibronectins / Q000502:physiology; D007668:Kidney / Q000166:cytology / Q000503:physiopathology; D008099:Liver / Q000473:pathology / Q000503:physiopathology; D008113:Liver Neoplasms / Q000473:pathology / Q000503:physiopathology / Q000556:secondary*; D008168:Lung / Q000166:cytology / Q000503:physiopathology; D008546:Melanoma, Experimental / Q000503:physiopathology; D008562:Membrane Glycoproteins / Q000502:physiology; D051379:Mice; D008815:Mice, Inbred Strains; D009368:Neoplasm Transplantation; D009439:Neuraminidase / Q000494:pharmacology; D009447:Neuroblastoma / Q000473:pathology / Q000503:physiopathology* / Q000556:secondary*; D009842:Oligopeptides / Q000494:pharmacology; D009928:Organ Specificity; D013154:Spleen / Q000166:cytology / Q000503:physiopathology; D014185:Transplantation, Isogeneic; D014407:Tumor Cells, Cultured; D014415:Tunicamycin / Q000494:pharmacology; D019096:Vitronectin / Q000502:physiology; D001616:beta-Galactosidase / Q000494:pharmacology
chemical_list: D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D008562:Membrane Glycoproteins; D009842:Oligopeptides; D019096:Vitronectin; D014415:Tunicamycin; C047981:arginyl-glycyl-aspartic acid; C049554:glycyl-arginyl-glycyl-aspartyl-serine; D009439:Neuraminidase; D001616:beta-Galactosidase