title: Ameloblastoma induces osteoclastogenesis: a possible role of ameloblastoma in expanding in the bone.
abstract: Ameloblastoma, a tumor located in bone, when neglected, can perforate the bone and, ultimately, spread into the soft tissues. To expand in the bone, ameloblastoma must have a mechanism of resorbing the surrounding bone. However, the mechanism for bone resorption is poorly understood. In the present study, we found that RANKL and TNFalpha were expressed and secreted by ameloblastoma cells, and was proven to induce osteoclastogenesis. Our present results also showed that phosphorylation of p38, SAPK, p44/42 and Akt were upregulated under treatment of 10xCM (concentrated conditioned media of AM-1 cells). We also noticed formation of resorption lacunae on dentin slice by 10xCM-induced osteoclast-like MNCs. These results suggested that ameloblastoma by secreting RANKL and TNFalpha could induce osteoclastogenesis.
authors.affiliation: Laboratory of Oral Cellular and Molecular Biology, Faculty of Dental Science, Kyushu University, Fukuoka, Japan. ferry@dent.kyushu-u.ac.jp
authors.forename: Ferry
authors.initials: F
authors.lastname: Sandra
authors.forename: Laifa
authors.initials: L
authors.lastname: Hendarmin
authors.forename: Toshio
authors.initials: T
authors.lastname: Kukita
authors.forename: Yu
authors.initials: Y
authors.lastname: Nakao
authors.forename: Norifumi
authors.initials: N
authors.lastname: Nakamura
authors.forename: Seiji
authors.initials: S
authors.lastname: Nakamura
mesh_terms: D000564:Ameloblastoma / Q000378:metabolism / Q000503:physiopathology*; D001862:Bone Resorption / Q000503:physiopathology*; D002352:Carrier Proteins / Q000378:metabolism; D002454:Cell Differentiation; D018920:Coculture Techniques; D017077:Culture Media, Conditioned; D003804:Dentin / Q000378:metabolism; D006801:Humans; D048031:JNK Mitogen-Activated Protein Kinases / Q000378:metabolism; D007573:Jaw Neoplasms / Q000378:metabolism / Q000503:physiopathology*; D008562:Membrane Glycoproteins / Q000378:metabolism; D048052:Mitogen-Activated Protein Kinase 3 / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism; D010010:Osteoclasts / Q000502:physiology*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt; D053245:RANK Ligand; D053246:Receptor Activator of Nuclear Factor-kappa B; D014407:Tumor Cells, Cultured; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism; D048051:p38 Mitogen-Activated Protein Kinases / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D017077:Culture Media, Conditioned; D008562:Membrane Glycoproteins; D009363:Neoplasm Proteins; D011518:Proto-Oncogene Proteins; D053245:RANK Ligand; D053246:Receptor Activator of Nuclear Factor-kappa B; C505686:TNFRSF11A protein, human; C505688:TNFSF11 protein, human; D014409:Tumor Necrosis Factor-alpha; C494918:AKT1 protein, human; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt; D048031:JNK Mitogen-Activated Protein Kinases; D048052:Mitogen-Activated Protein Kinase 3; D048051:p38 Mitogen-Activated Protein Kinases