Search results for PGLYRP2

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Protein (1 results from a total of 1)

Identifier: R-HSA-6799296
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: PGLYRP2: Q96PD5

Complex (2 results from a total of 2)

Identifier: R-HSA-8933468
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-6799988
Species: Homo sapiens
Compartment: extracellular region

Reaction (2 results from a total of 2)

Identifier: R-HSA-6799981
Species: Homo sapiens
Compartment: extracellular region, cell wall
Peptidoglycan 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 expressed in the liver, from which it is secreted into blood as non-disulfide‑linked dimers (Liu C et al. 2001; Zhang Y et al. 2005; De Pauw P et al. 1995; Hoijer MA et al. 1996). PGLYRP2 expression can be also induced in the skin and intestine upon exposure to bacteria or pro-inflammatory cytokines (Wang H et al. 2005; Li X et al. 2006). The constitutive expression of PGLYRP2 in the liver and induced expression in epithelial cells is regulated by different transcription factors, the binding sequences for which are located in different regions of the pglyrp2 promoter (Li X et al. 2006). PGRP2 binds to bacterial cell wall peptidoglycan and functions as N‑acetylmuramoyl‑L‑alanine amidase that hydrolyzes the amide bond between the MurNAc and L‑alanine in 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). PGLYRP2 has a conserved Zn(2+)‑binding site in the peptidoglycan‑binding groove, which is also present in bacteriophage type 2 amidases, and PGLYRP2 requires Zn(2+) for its amidase activity (Wang ZM et al. 2003). The amidase activity of mammalian PGLYRP2 is though to eliminate the pro‑inflammatory peptidoglycan and, therefore, prevent over‑activation of the immune system and excessive inflammation (Hoijer MA et al. 1997; Royet J and Dziarski R 2007). In addition to its amidase activity, PGLYRP2 also has antibacterial activity against both Gram-positive and Gram-negative bacteria and Chlamydia (Bobrovsky P et al. 2016), similar to PGLYRP1, PGLYRP3, and PGLYRP4 (Lu X et al. 2006; Wang M et al. 2007).
Identifier: R-HSA-6799977
Species: Homo sapiens
Compartment: extracellular region
Peptidoglycan 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).
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