Elastin-derived peptides and TGF-β1 induce osteogenic responses in smooth muscle cells
Autor: | Agneta Simionescu, Katherine Philips, Narendra R. Vyavahare |
---|---|
Rok vydání: | 2005 |
Předmět: |
Vascular smooth muscle
Myocytes Smooth Muscle Biophysics Matrix metalloproteinase Matrix (biology) Biochemistry Muscle Smooth Vascular Transforming Growth Factor beta1 Osteogenesis Transforming Growth Factor beta Gene expression Animals Molecular Biology Cells Cultured Dose-Response Relationship Drug biology Chemistry Cell Differentiation Cell Biology Peptide Fragments In vitro Elastin Rats Cell biology Bone Morphogenetic Proteins cardiovascular system Osteocalcin biology.protein Alkaline phosphatase |
Zdroj: | Biochemical and Biophysical Research Communications. 334:524-532 |
ISSN: | 0006-291X |
DOI: | 10.1016/j.bbrc.2005.06.119 |
Popis: | Elastin degradation associated with matrix metalloproteinase activity is a cell-mediated process, observed in almost all types of vascular calcification. In this study, we tested the hypothesis that elastin-derived peptides induce an osteogenic response in vascular smooth muscle cells (SMCs) in vitro. Using RT-PCR and specific protein assays, we demonstrated that rat aortic SMCs incubated with elastin peptides exhibited an increased expression of the 67 kDa elastin laminin receptor (ELR) and matrix metalloproteinase-2 and typical bone proteins, such as core binding factor α-1, osteocalcin, and alkaline phosphatase. The osteogenic gene expression in SMCs was further enhanced by the addition of TGF-β1 along with the elastin peptides, in the absence of any other mineralizing agent. Conversely, lactose (an ELR antagonist) down-regulated expression of most investigated proteins. In conclusion, elastin-derived peptides and TGF-β1 up-regulate the expression of typical bone proteins in cultured rat aortic SMCs, possibly via the ELR signaling. |
Databáze: | OpenAIRE |
Externí odkaz: |