The Cloning of a Rat Peptidoglycan Recognition Protein (Pgrp) and Its Induction in Brain by Sleep Deprivation

Rehman, Abdur; Taishi, Ping; Fang, Jidong; Majde, Jeannine A.; Krueger, James M.

doi:10.1006/cyto.2000.0800

Cited by 44 publications

(27 citation statements)

References 28 publications

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“…As shown in Fig. 3, the homology between the Hd-PGRP-1, Hd-PGRP-2, and those in the National Center for Biotechnology Information data base showed that Hd-PGRP-1 is similar to Bombyx mori PGRP (Bm-PGRP, 42.2% identity) (9), Trichoplusia ni PGRP (Tn-PGRP, 43.1%) (8), Drosophila melanogaster PGRP-SA (Dm-PGRP, 45.7%) (35), human PGRP (39.1%) (8), mouse PGRP (40.2%) (8), rat PGRP (37.0%) (36), and bovine oligosaccharide-binding protein (bovine OBP, 39.2%) (37). Four cysteine and four tryptophan residues of Hd-PGRP-1 are conserved as in all insect PGRPs as well as in human (indicated by closed circles and closed reverse triangles in Fig.…”

Section: Pgrp-2 Are Not Likely To Have N-acetylmuramyl-l-alanine Amidmentioning

confidence: 99%

Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Lee

Osaki

Lee

et al. 2004

Journal of Biological Chemistry

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Section: Pgrp-2 Are Not Likely To Have N-acetylmuramyl-l-alanine Amidmentioning

confidence: 99%

Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Lee

Osaki

Lee

et al. 2004

Journal of Biological Chemistry

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“…To date, mammalian PGRPs have been identified in humans (6,7,13), rats (18), mice (13), cattle (10), camels (19), and pigs. PGRPs have structural homology to bacteriophage T7 lysozyme, and several PGRPs are reported to digest PGN (16, 20 -24).…”

mentioning

confidence: 99%

Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Tydell

Yuan²,

Tran³

et al. 2006

The Journal of Immunology

104

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Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern recognition molecules of innate immunity that are conserved from insects to humans. Various PGRPs are reported to have diverse functions: they bind bacterial molecules, digest PGN, and are essential to the Toll pathway in Drosophila. One family member, bovine PGN recognition protein-S (bPGRP-S), has been found to bind and kill microorganisms in a PGN-independent manner, raising questions about the identity of the bPGRP-S ligand. Addressing this, we have determined the binding and microbicidal properties of bPGRP-S in a range of solutions approximating physiologic conditions. In this study we show that bPGRP-S interacts with other bacterial components, including LPS and lipoteichoic acid, with higher affinities than for PCP, as determined by their abilities to inhibit bPGRP-S-mediated killing of bacteria. Where and how PGRPs act in vivo is not yet clear. Using Immunogold electron microscopy, PGRP-S was localized to the dense/large granules of naive neutrophils, which contain the oxygen-independent bactericidal proteins of these cells, and to the neutrophil phagolysosome. In addition, Immunogold staining and secretion studies demonstrate that neutrophils secrete PGRP-S when exposed to bacteria. Bovine PGRP-S can mediate direct lysis of heat-killed bacteria; however, PGRP-S-mediated killing of bacteria is independent of this activity. Evidence that bPGRP-S has multiple activities and affinity to several bacterial molecules challenges the assumption that the PGRP family of proteins recapitulates the evolution of TLRs. Mammalian PGRPs do not have a single antimicrobial activity against a narrow range of target organisms; rather, they are generalists in their affinity and activity.

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“…Unlike mammalian TLRs, none of the nine Drosophila TLRs described to date appear to bind directly to microbial macromolecules. Instead, a group of at least 13 proteins similar to the peptidoglycan recognition proteins (PGRPs) of Bombyx mori, Trichoplusia ni, rats, and humans are present in Drosophila (11)(12)(13)(14)(15)(16). These PGRPs, along with Gram-negative (G Ϫ ) bacteria-binding protein and scavenger receptor class C, type I, are thought to represent the PRRs of Drosophila.…”

mentioning

confidence: 99%

Differential Activation of the NF-κB-like Factors Relish and Dif in Drosophila melanogaster by Fungi and Gram-positive Bacteria

Hedengren-Olcott

Olcott

Mooney

et al. 2004

Journal of Biological Chemistry

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The current model of immune activation in bacteria. Various fungi stimulated antimicrobial peptides through at least two different pathways requiringRelish and/or Dif. Induction of Attacin A by Geotrichum candidum required Relish, whereas activation by Beauvaria bassiana required Dif, suggesting that the Drosophila immune system can distinguish between at least these two fungi. We conclude that the Drosophila immune system is more complex than the current model. We propose a new model to account for this immune system complexity, incorporating distinct pattern recognition receptors of the Drosophila immune system, which can distinguish between various fungi and G ؉ bacteria, thereby leading to selective induction of antimicrobial peptides via differential activation of Relish and Dif.

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The Cloning of a Rat Peptidoglycan Recognition Protein (Pgrp) and Its Induction in Brain by Sleep Deprivation

Cited by 44 publications

References 28 publications

Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Peptidoglycan Recognition Proteins Involved in 1,3-β-D-Glucan-dependent Prophenoloxidase Activation System of Insect

Bovine Peptidoglycan Recognition Protein-S: Antimicrobial Activity, Localization, Secretion, and Binding Properties

Differential Activation of the NF-κB-like Factors Relish and Dif in Drosophila melanogaster by Fungi and Gram-positive Bacteria

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