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	Ferry Sandra, Laifa Hendarmin, Toshio Kukita, Yu Nakao, Norifumi Nakamura, Seiji Nakamura
Journal	Oral oncology (Oral Oncol) Vol. 41 Issue 6 Pg. 637-44 (Jul 2005) ISSN: 1368-8375 [Print] England
PMID	15935726 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Carrier Proteins Culture Media, Conditioned Membrane Glycoproteins Neoplasm Proteins Proto-Oncogene Proteins RANK Ligand Receptor Activator of Nuclear Factor-kappa B TNFRSF11A protein, human TNFSF11 protein, human Tumor Necrosis Factor-alpha AKT1 protein, human Protein Serine-Threonine Kinases Proto-Oncogene Proteins c-akt JNK Mitogen-Activated Protein Kinases Mitogen-Activated Protein Kinase 3 p38 Mitogen-Activated Protein Kinases
Topics	Ameloblastoma (metabolism, physiopathology) Bone Resorption (physiopathology) Carrier Proteins (metabolism) Cell Differentiation Coculture Techniques Culture Media, Conditioned Dentin (metabolism) Humans JNK Mitogen-Activated Protein Kinases (metabolism) Jaw Neoplasms (metabolism, physiopathology) Membrane Glycoproteins (metabolism) Mitogen-Activated Protein Kinase 3 (metabolism) Neoplasm Proteins (metabolism) Osteoclasts (physiology) Phosphorylation Protein Serine-Threonine Kinases (metabolism) Proto-Oncogene Proteins (metabolism) Proto-Oncogene Proteins c-akt RANK Ligand Receptor Activator of Nuclear Factor-kappa B Tumor Cells, Cultured Tumor Necrosis Factor-alpha (metabolism) p38 Mitogen-Activated Protein Kinases (metabolism)

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