Relaxin stimulates MMP-2 and α-smooth muscle actin expression by human periodontal ligament cells
作者： S. Henneman , M.M. Bildt , J. DeGroot , A.M. Kuijpers-Jagtman , J.W. Von den Hoff
DOI: 10.1016/J.ARCHORALBIO.2007.08.010
关键词: Extracellular matrix 、 Fibroblast 、 Biology 、 Tissue inhibitor of metalloproteinase 、 Gelatinase 、 Cell culture 、 Periodontal fiber 、 Matrix metalloproteinase 、 Internal medicine 、 Endocrinology 、 Relaxin
摘要: The main cells in the periodontal ligament (PDL) are fibroblasts, which play an important role remodelling. Matrix metalloproteinases (MMPs) largely responsible for degradation of extracellular matrix proteins PDL. Previous studies have indicated that MMP production can be stimulated by hormone relaxin. This facilitates delivery softening connective tissues reproductive tract, and it prepares mammary gland lactation. Periodontal remodelling takes place during orthodontic tooth movement, might enhanced Therefore, we investigated effects relaxin on gelatinase expression human PDL cells. Cultures were incubated with Gelatinase (MMP-2 -9) expression, α-smooth muscle actin (α-SMA), total activity DNA content measured. Both proMMP-2 active MMP-2 was identified cultures. There a clear trend showing dose-dependent increase production, significant at 250 ng/ml. Total not affected. A stimulation α-SMA found 50 results indicate activates actin. © 2007 Elsevier Ltd. All rights reserved.
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