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Details on Person Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are in...

Class:IdSummation:6799979
_displayNamePeptidoglycan recognition proteins (PGRPs or PGLYRPs) are in...
_timestamp2016-08-04 22:13:15
created[InstanceEdit:6799986] Shamovsky, Veronica, 2015-09-26
literatureReference[LiteratureReference:6789223] A peptidoglycan recognition protein in innate immunity conserved from insects to humans
[LiteratureReference:6788956] Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidase
[LiteratureReference:6789060] Identification of serum N-acetylmuramoyl-l-alanine amidase as liver peptidoglycan recognition protein 2
[LiteratureReference:6789211] Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules
[LiteratureReference:6799982] Peptidoglycan recognition protein 2 (N-acetylmuramoyl-L-Ala amidase) is induced in keratinocytes by bacteria through the p38 kinase pathway
[LiteratureReference:6799987] Differential expression of peptidoglycan recognition protein 2 in the skin and liver requires different transcription factors
[LiteratureReference:6789099] Human peptidoglycan recognition proteins require zinc to kill both gram-positive and gram-negative bacteria and are synergistic with antibacterial peptides
[LiteratureReference:6799983] Inflammatory properties of peptidoglycan are decreased after degradation by human N-acetylmuramyl-L-alanine amidase
[LiteratureReference:8933063] Characterization of human serum N-acetylmuramyl-L-alanine amidase purified by affinity chromatography
[Book:8933045] Peptidoglycan Recognition Proteins and Lysozyme Encyclopedia of Immunobiology Ratcliffe, Michael 9780123742797
[LiteratureReference:6799985] Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies
[LiteratureReference:8933065] Peptidoglycan recognition proteins: modulators of the microbiome and inflammation
[LiteratureReference:6799827] Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences
modified[InstanceEdit:6802979] Shamovsky, Veronica, 2015-10-03
[InstanceEdit:8867536] Jupe, Steve, 2016-04-15
[InstanceEdit:8933084] Shamovsky, Veronica, 2016-08-02
[InstanceEdit:8933467] Shamovsky, Veronica, 2016-08-04
textPeptidoglycan recognition proteins (PGRPs or PGLYRPs) are innate immunity molecules that contain a conserved peptidoglycan-binding type 2 amidase domain that is homologous to bacteriophage and bacterial type 2 amidases (Kang D et al. 1998; Liu C et al. 2001; Royet J and Dziarski R 2007; Royet J et al. 2011; Dziarski R et al. 2016). Mammals have a family of four PGRPs (PGLYRP1, 2, 3 & 4) that are differentially expressed in a cell-type or tissue-specific manner. PGLYRP2 (also known as PGRP-L) is constitutively produced in the liver and secreted into the blood (Liu C et al. 2001; Zhang Y et al. 2005; De Pauw P et al. 1995; Hoijer MA et al. 1996). PGLYRP2 expression can also be induced in the skin and intestine upon exposure to bacteria or pro-inflammatory cytokines (Wang H et al. 2005; Li X et al. 2006). Constitutive and inducible expression of PGLYRP2 in the liver and skin respectively required different transcription factors (Li X et al. 2006). PGLYRP2 is a (Zn2+)-dependent N-acetylmuramoyl-L-alanine amidase that hydrolyzes the amide bond between the MurNAc and L-alanine in bacterial cell wall peptidoglycan (Wang ZM et al. 2003; Zhang Y et al. 2005). The minimal peptidoglycan fragment hydrolyzed by PGLYRP2 is MurNAc-tripeptide (Wang ZM et al. 2003). Due to its amidase activity, human PGLYRP2 is thought to reduce inflammatory properties of bacterial peptidoglycan by cleaving it into biologically inactive fragments (Hoijer MA et al. 1997; Wang ZM et al. 2003; Royet J and Dziarski R 2007).
(summation)[BlackBoxEvent:6799977] PGLYRP2 hydrolyzes bacterial peptidoglycan [Homo sapiens]
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