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Type I collagen-induced osteoblastic differentiation of bone-marrow cells mediated by collagen-alpha2beta1 integrin interaction.

Authors: Mizuno, M  Fujisawa, R  Kuboki, Y 
Citation: Mizuno M, etal., J Cell Physiol. 2000 Aug;184(2):207-13.
Pubmed: (View Article at PubMed) PMID:10867645
DOI: Full-text: DOI:10.1002/1097-4652(200008)184:2<207::AID-JCP8>3.0.CO;2-U

Bone marrow cells are multipotent cells. When bone marrow cells were cultured with type I collagen matrix gels, they showed high alkaline phosphatase activity, collagen synthesis, and formed mineralized tissues. Furthermore, cells expressed osteocalcin and bone sialoprotein genes, which are osteoblast-specific genes. These findings indicate that type I collagen matrix gels induce osteoblastic differentiation of bone marrow cells. Type I collagen interacts with the alpha 2 beta 1 integrin receptor on the cell membrane and mediates extracellular signals into cells. DGEA peptide is a cell-binding domain of type I collagen molecule. When collagen-integrin interaction was interrupted by the addition of Asp-Gly-Glu-Ala (DGEA) peptide to the culture, the expression of osteoblastic phenotypes of bone marrow cells was inhibited. Furthermore, anti-alpha 2 integrin antibody, which interacts with alpha subunit of integrin and blocks the binding of integrin with collagen, suppressed the expression of osteoblastic phenotypes. These findings imply that collagen-alpha 2 beta 1 integrin interaction is an important signal for the osteoblastic differentiation of bone marrow cells.

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CRRD Object Information
CRRD ID: 2307406
Created: 2009-06-01
Species: All species
Last Modified: 2009-06-01
Status: ACTIVE



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