caa a22 4500 605521050 CHVBK 20210128100738.0 cr unu---uuuuu 210128e20150101xx s 000 0 eng 10.1007/s00223-014-9938-4 doi (NATIONALLICENCE)springer-10.1007/s00223-014-9938-4 Tgfbi Deficiency Leads to a Reduction in Skeletal Size and Degradation of the Bone Matrix [Elektronische Daten] [Jung-Mi Lee, Eun-Hye Lee, In-San Kim, Jung-Eun Kim] Transforming growth factor-β-induced gene product-h3 (TGFBI/BIGH3) is an extracellular matrix protein expressed in a wide variety of tissues. TGFBI binds to type I, II, and IV collagens, as well as to biglycan and decorin and plays important roles in cell-to-cell, cell-to-collagen, and cell-to-matrix interactions. Furthermore, TGFBI is involved in cell growth and migration, tumorigenesis, wound healing, and apoptosis. To investigate whether TGFBI is involved in the maintenance of skeletal tissues, Tgfbi knockout mice were generated by crossing male and female Tgfbi heterozygous mice. Skeletal preparation showed that the skeletal size in Tgfbi knockout mice was smaller than in wild-type and heterozygous mice. However, chondrocytic cell alignment in the growth plates, bone mineral density, and bone forming rates were similar in Tgfbi knockout, wild-type, and heterozygous mice. Alterations in skeletal tissue arrangements in Tgfbi knockout mice were estimated from safranin O staining, trichrome staining, and immunohistochemistry for type II and X collagen, and matrix metalloproteinase 13 (MMP13). Cartilage matrix degradation was observed in the articular cartilage of Tgfbi knockout mice. Although the detection of type II collagen in the articular cartilage was lower in Tgfbi knockout mice than wild-type mice, the detection of MMP13 was markedly higher, indicating that Tgfbi deficiency is associated with the degradation of cartilage matrix. These results suggest that TGFBI plays an important role in maintaining skeletal tissues and the cartilage matrix in mice. Springer Science+Business Media New York, 2014 TGFBI nationallicence Tgfbi nationallicence Knockout nationallicence Skeletal size nationallicence Matrix degradation nationallicence Lee Jung-Mi Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut Lee Eun-Hye Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut Kim In-San Department of Biochemistry and Cell Biology, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut Kim Jung-Eun Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut Calcified Tissue International Springer US; http://www.springer-ny.com 96/1(2015-01-01), 56-64 0171-967X 96:1<56 2015 96 223 https://doi.org/10.1007/s00223-014-9938-4 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00223-014-9938-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lee Jung-Mi Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut NATIONALLICENCE 700 1- Lee Eun-Hye Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut NATIONALLICENCE 700 1- Kim In-San Department of Biochemistry and Cell Biology, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut NATIONALLICENCE 700 1- Kim Jung-Eun Department of Molecular Medicine, Kyungpook National University School of Medicine, 700-422, Daegu, Republic of Korea aut NATIONALLICENCE 773 0- Calcified Tissue International Springer US; http://www.springer-ny.com 96/1(2015-01-01), 56-64 0171-967X 96:1<56 2015 96 223