Muramyl dipeptide enhances osteoclast formation induced by lipopolysaccharide, IL-1 alpha, and TNF-alpha through nucleotide-binding oligomerization domain 2-mediated signaling in osteoblasts.

@article{Yang2005MuramylDE,
  title={Muramyl dipeptide enhances osteoclast formation induced by lipopolysaccharide, IL-1 alpha, and TNF-alpha through nucleotide-binding oligomerization domain 2-mediated signaling in osteoblasts.},
  author={Shuhua Yang and Naoyuki Takahashi and Teruhito Yamashita and Nobuaki Sato and Masahiro Takahashi and Makio Mogi and Takashi Uematsu and Yasuhiro Kobayashi and Yuko Nakamichi and Kiyoshi Takeda and Shizuo Akira and Haruhiko Takada and Nobuyuki Udagawa and Kiyofumi Furusawa},
  journal={Journal of immunology},
  year={2005},
  volume={175 3},
  pages={1956-64}
}
Muramyl dipeptide (MDP) is the minimal essential structural unit responsible for the immunoadjuvant activity of peptidoglycan. As well as bone-resorbing factors such as 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3) and PGE2, LPS and IL-1alpha stimulate osteoclast formation in mouse cocultures of primary osteoblasts and hemopoietic cells. MDP alone could not induce osteoclast formation in the coculture, but enhanced osteoclast formation induced by LPS, IL-1alpha, or TNF-alpha but not 1alpha… CONTINUE READING

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