Decreased Trabecular Bone Mass in Col22a1-Deficient Mice
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Decreased Trabecular Bone Mass in Col22a1-Deficient Mice. / Zhao, Wenbo; Wiedemann, Philip; Wölfel, Eva Maria; Neven, Mona; Peters, Stephanie; Imhof, Thomas; Koch, Manuel; Busse, Björn; Amling, Michael; Schinke, Thorsten; Yorgan, Timur Alexander.
in: CELLS-BASEL, Jahrgang 10, Nr. 11, 3020, 04.11.2021.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Decreased Trabecular Bone Mass in Col22a1-Deficient Mice
AU - Zhao, Wenbo
AU - Wiedemann, Philip
AU - Wölfel, Eva Maria
AU - Neven, Mona
AU - Peters, Stephanie
AU - Imhof, Thomas
AU - Koch, Manuel
AU - Busse, Björn
AU - Amling, Michael
AU - Schinke, Thorsten
AU - Yorgan, Timur Alexander
PY - 2021/11/4
Y1 - 2021/11/4
N2 - The bone matrix is constantly remodeled by the coordinated activities of bone-forming osteoblasts and bone-resorbing osteoclasts. Whereas type I collagen is the most abundant bone matrix protein, there are several other proteins present, some of them specifically produced by osteoblasts. In a genome-wide expression screening for osteoblast differentiation markers we have previously identified two collagen-encoding genes with unknown function in bone remodeling. Here we show that one of them, Col22a1, is predominantly expressed in bone, cultured osteoblasts, but not in osteoclasts. Based on this specific expression pattern we generated a Col22a1-deficient mouse model, which was analyzed for skeletal defects by µCT, undecalcified histology and bone-specific histomorphometry. We observed that Col22a1-deficient mice display trabecular osteopenia, accompanied by significantly increased osteoclast numbers per bone surface. In contrast, cortical bone parameters, osteoblastogenesis or bone formation were unaffected by the absence of Col22a1. Likewise, primary osteoblasts from Col22a1-deficient mice did not display a cell-autonomous defect, and they did not show altered expression of Rankl or Opg, two key regulators of osteoclastogenesis. Taken together, we provide the first evidence for a physiological function of Col22a1 in bone remodeling, although the molecular mechanisms explaining the indirect influence of Col22a1 deficiency on osteoclasts remain to be identified.
AB - The bone matrix is constantly remodeled by the coordinated activities of bone-forming osteoblasts and bone-resorbing osteoclasts. Whereas type I collagen is the most abundant bone matrix protein, there are several other proteins present, some of them specifically produced by osteoblasts. In a genome-wide expression screening for osteoblast differentiation markers we have previously identified two collagen-encoding genes with unknown function in bone remodeling. Here we show that one of them, Col22a1, is predominantly expressed in bone, cultured osteoblasts, but not in osteoclasts. Based on this specific expression pattern we generated a Col22a1-deficient mouse model, which was analyzed for skeletal defects by µCT, undecalcified histology and bone-specific histomorphometry. We observed that Col22a1-deficient mice display trabecular osteopenia, accompanied by significantly increased osteoclast numbers per bone surface. In contrast, cortical bone parameters, osteoblastogenesis or bone formation were unaffected by the absence of Col22a1. Likewise, primary osteoblasts from Col22a1-deficient mice did not display a cell-autonomous defect, and they did not show altered expression of Rankl or Opg, two key regulators of osteoclastogenesis. Taken together, we provide the first evidence for a physiological function of Col22a1 in bone remodeling, although the molecular mechanisms explaining the indirect influence of Col22a1 deficiency on osteoclasts remain to be identified.
U2 - 10.3390/cells10113020
DO - 10.3390/cells10113020
M3 - SCORING: Journal article
C2 - 34831244
VL - 10
JO - CELLS-BASEL
JF - CELLS-BASEL
SN - 2073-4409
IS - 11
M1 - 3020
ER -