User:Bs20dp/Muramyl dipeptide
Muramyl dipeptide (MDP) is a component of bacterial peptidoglycan, a recognition structure or activator for nucleotide-binding oligomerization domain 2 (NOD2) protein.[1] MDP is a constituent of both Gram-positive and Gram-negative bacteria composed of N-acetylmuramic acid linked by its lactic acid moiety to the N-terminus of an L-alanine D-isoglutamine dipeptide.[1] MDP can be recognized by the immune system as a pathogen-associated molecular pattern (MAMP) and activate the NALP3 inflammasome which, in turn, leads to cytokine activation, IL-1α and IL-1β especially.[2] Human NOD2 protein of the nucleotide binding leucine-rich repeats (NLR) family, is a cytoplasmic receptor involved in host innate immune system defense. Mutations in the CARD15 gene encoding NOD2 protein have been observed in Crohn's disease patients, decreasing the immune systems of these patients ability to recognize Muramyl dipeptide (MDP). MDP analogous and their potential for immune response therapies in cancer and disease are being investigated. The Journal of Clinical Investigation published literature by Watanabe., & Strober., et al., in 2008 about MDP-mediated scientific experiments in mice successfully providing protection against colitis. Further study of the NOD2-MDP pathway is necessary.
See also
[edit]- Dipeptide
- Mifamurtide, a synthetic analogue for the treatment of osteosarcoma
References
[edit]- ^ a b Inohara N, Ogura Y, Fontalba A, Gutierrez O, Pons F, Crespo J, et al. (February 2003). "Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease". The Journal of Biological Chemistry. 278 (8): 5509–5512. doi:10.1074/jbc.C200673200. PMID 12514169.
- ^ Martinon F, Agostini L, Meylan E, Tschopp J (November 2004). "Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome". Current Biology : CB. 14 (21): 1929–1934. doi:10.1016/j.cub.2004.10.027. PMID 15530394.
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