title: Advances in osteoclast biology resulting from the study of osteopetrotic mutations.
abstract: Osteopetrosis is the result of mutations affecting osteoclast function. Careful analyses of osteopetrosis have provided instrumental information on bone remodeling, including the coupling of bone formation to bone resorption. Based on a range of novel genetic mutations and the resulting osteoclast phenotypes, we discuss how osteopetrosis models have clarified the function of the coupling of bone formation to bone resorption, and the pivotal role of the osteoclast and their function in this phenomenon. We highlight the distinct possibility that osteoclast activities can be divided into two separate avenues: bone resorption and control of bone formation.
authors.affiliation: Nordic Bioscience A/S, Herlev, Denmark.
authors.forename: T
authors.initials: T
authors.lastname: Segovia-Silvestre
authors.forename: A V
authors.initials: AV
authors.lastname: Neutzsky-Wulff
authors.forename: M G
authors.initials: MG
authors.lastname: Sorensen
authors.forename: C
authors.initials: C
authors.lastname: Christiansen
authors.forename: J
authors.initials: J
authors.lastname: Bollerslev
authors.forename: M A
authors.initials: MA
authors.lastname: Karsdal
authors.forename: K
authors.initials: K
authors.lastname: Henriksen
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000172:deficiency / Q000235:genetics; D000818:Animals; D000071183:Autophagy-Related Proteins; D016723:Bone Remodeling / Q000235:genetics / Q000502:physiology; D001862:Bone Resorption / Q000235:genetics / Q000503:physiopathology; D024402:Carbonic Anhydrase II / Q000172:deficiency / Q000235:genetics; D056657:Cathepsin K; D002403:Cathepsins / Q000235:genetics; D018118:Chloride Channels / Q000235:genetics; D004195:Disease Models, Animal; D006801:Humans; D008562:Membrane Glycoproteins / Q000172:deficiency / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics; D051379:Mice; D008954:Models, Biological; D009154:Mutation; D010006:Osteoblasts / Q000473:pathology / Q000502:physiology; D010010:Osteoclasts / Q000473:pathology / Q000502:physiology*; D010022:Osteopetrosis / Q000209:etiology / Q000235:genetics* / Q000473:pathology / Q000503:physiopathology; D053245:RANK Ligand / Q000172:deficiency / Q000235:genetics; D053246:Receptor Activator of Nuclear Factor-kappa B / Q000172:deficiency / Q000235:genetics; D044767:Ubiquitin-Protein Ligases / Q000235:genetics; D025262:Vacuolar Proton-Translocating ATPases / Q000235:genetics
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D000071183:Autophagy-Related Proteins; C097540:CLCN7 protein, human; D018118:Chloride Channels; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C489946:OSTM1 protein, human; C476215:PLEKHM1 protein, human; D053245:RANK Ligand; D053246:Receptor Activator of Nuclear Factor-kappa B; C472421:TCIRG1 protein, human; C505686:TNFRSF11A protein, human; C505688:TNFSF11 protein, human; D044767:Ubiquitin-Protein Ligases; D002403:Cathepsins; C534130:CTSK protein, human; D056657:Cathepsin K; C534132:Ctsk protein, mouse; D025262:Vacuolar Proton-Translocating ATPases; D024402:Carbonic Anhydrase II