Peroxidase Enzymes Regulate Collagen Biosynthesis and Matrix Mineralization by Cultured Human Osteoblasts

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• 作者：Mark O. DeNichilo ; Alexandra J. Shoubridge…
• 关键词：Peroxidase enzymes ; Osteoblasts ; Collagen biosynthesis ; Matrix mineralization
• 刊名：Calcified Tissue International
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：98
• 期：3
• 页码：294-305
• 全文大小：1,200 KB
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• 作者单位：Mark O. DeNichilo (1) (4)
  Alexandra J. Shoubridge (1)
  Vasilios Panagopoulos (1)
  Vasilios Liapis (1)
  Aneta Zysk (1)
  Irene Zinonos (1)
  Shelley Hay (1)
  Gerald J. Atkins (2)
  David M. Findlay (2)
  Andreas Evdokiou (1) (3)
  
  1. Breast Cancer Research Unit, Discipline of Surgery, The University of Adelaide, Adelaide, Australia
  4. TQEH, Basil Hetzel Research Institute, 28 Woodville Road, Woodville, SA, 5011, Australia
  2. Discipline of Orthopaedics and Trauma, The University of Adelaide, Adelaide, Australia
  3. Centre for Personalized Cancer Medicine, The University of Adelaide, Adelaide, Australia
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Endocrinology
  Orthopedics
  Cell Biology
  
• 出版者：Springer New York
• ISSN：1432-0827

文摘

The early recruitment of inflammatory cells to sites of bone fracture and trauma is a critical determinant in successful fracture healing. Released by infiltrating inflammatory cells, myeloperoxidase (MPO) and eosinophil peroxidase (EPO) are heme-containing enzymes, whose functional involvement in bone repair has mainly been studied in the context of providing a mechanism for oxidative defense against invading microorganisms. We report here novel findings that show peroxidase enzymes have the capacity to stimulate osteoblastic cells to secrete collagen I protein and generate a mineralized extracellular matrix in vitro. Mechanistic studies conducted using cultured osteoblasts show that peroxidase enzymes stimulate collagen biosynthesis at a post-translational level in a prolyl hydroxylase-dependent manner, which does not require ascorbic acid. Our studies demonstrate that osteoblasts rapidly bind and internalize both MPO and EPO, and the catalytic activity of these peroxidase enzymes is essential to support collagen I biosynthesis and subsequent release of collagen by osteoblasts. We show that EPO is capable of regulating osteogenic gene expression and matrix mineralization in culture, suggesting that peroxidase enzymes may play an important role not only in normal bone repair, but also in the progression of pathological states where infiltrating inflammatory cells are known to deposit peroxidases. Keywords Peroxidase enzymes Osteoblasts Collagen biosynthesis Matrix mineralization