title: Immunolocalization of DMP1 and sclerostin in the epiphyseal trabecule and diaphyseal cortical bone of osteoprotegerin deficient mice.
abstract: In order to define the osteocytic function in accelerated bone remodeling, we examined the distribution of the osteocytic lacunar-canalicular system (OLCS) and osteocyte-secreting molecules--dentin matrix protein (DMP) 1 and sclerostin--in the epiphyses and cortical bones of osteoprotegerin deficient (OPG(-/-)) mice. Silver impregnation visualized a well-arranged OLCS in the wild-type epiphyses and cortical bone, whereas OPG(-/-) mice had an irregular OLCS in the epiphyses, but well-arranged canaliculi in the cortical bone. DMP1-positive osteocytes were evenly distributed throughout the wild-type epiphyses and cortical bone, as well as the OPG(-/-) cortical bone. However, OPG(-/-) epiphyses revealed weak DMP1-immunoreactivity. Thus, osteocytes appear to synthesize more DMP1 as the OLCS becomes regular. In contrast, sclerostin-immunoreactivity was significantly diminished in the OPG(-/-) epiphyses and cortical bone. In OPG(-/-) epiphyses and cortical bone, triple staining demonstrated few sclerostin-positive osteocytes in the periphery of a thick cell layer of alkaline phosphatase-positive osteoblasts and many tartrate resistant acid phosphatase-positive osteoclasts. Summarizing, the regular distribution of OLCS may affect DMP1 synthesis, while the cellular activities of osteoclasts and osteoblasts rather than the regularity of OLCS may ultimately influence sclerostin synthesis.
authors.affiliation: Department of Developmental Biology of Hard Tissue, Graduate School of Dental Medicine, Hokkaido University, Sapporo, Japan. i-elm@aria.ocn.ne.jp
authors.forename: Hideo
authors.initials: H
authors.lastname: Masuki
authors.forename: Minqi
authors.initials: M
authors.lastname: Li
authors.forename: Tomoka
authors.initials: T
authors.lastname: Hasegawa
authors.forename: Reiko
authors.initials: R
authors.lastname: Suzuki
authors.forename: Guo
authors.initials: G
authors.lastname: Ying
authors.forename: Liu
authors.initials: L
authors.lastname: Zhusheng
authors.forename: Kimimitsu
authors.initials: K
authors.lastname: Oda
authors.forename: Tsuneyuki
authors.initials: T
authors.lastname: Yamamoto
authors.forename: Masamitsu
authors.initials: M
authors.lastname: Kawanami
authors.forename: Norio
authors.initials: N
authors.lastname: Amizuka
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D019485:Bone Morphogenetic Proteins / Q000378:metabolism*; D016723:Bone Remodeling / Q000502:physiology; D001842:Bone and Bones / Q000166:cytology / Q000378:metabolism*; D018483:Diaphyses / Q000378:metabolism; D004838:Epiphyses / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005819:Genetic Markers; D006023:Glycoproteins; D007150:Immunohistochemistry; D036341:Intercellular Signaling Peptides and Proteins; D007527:Isoenzymes / Q000378:metabolism; D008297:Male; D051379:Mice; D018345:Mice, Knockout; D010006:Osteoblasts / Q000378:metabolism; D010010:Osteoclasts / Q000378:metabolism; D053244:Osteoprotegerin / Q000172:deficiency* / Q000235:genetics; D000071681:Tartrate-Resistant Acid Phosphatase
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D019485:Bone Morphogenetic Proteins; C513308:Dmp1 protein, mouse; D016326:Extracellular Matrix Proteins; D005819:Genetic Markers; D006023:Glycoproteins; D036341:Intercellular Signaling Peptides and Proteins; D007527:Isoenzymes; D053244:Osteoprotegerin; C486030:Sost protein, mouse; C506031:Tnfrsf11b protein, mouse; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D000071681:Tartrate-Resistant Acid Phosphatase