The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

PGLYRP2  -  peptidoglycan recognition protein 2

Homo sapiens

Synonyms: HMFT0141, N-acetylmuramoyl-L-alanine amidase, PGLYRPL, PGRP-L, PGRPL, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of PGLYRP2

 

High impact information on PGLYRP2

  • In this study we identified the transcription start site for pglyrp2 and demonstrated that the differential expression of PGLYRP2 in hepatocytes and keratinocytes is regulated by different transcription factors whose binding sequences are located in different regions of the pglyrp2 promoter [3].
  • Induction of pglyrp2 in keratinocytes is regulated by sequences in the distal region of the promoter and requires transcription factors NF-kappaB and Sp1, whereas constitutive expression of pglyrp2 in a hepatocyte cell line is regulated by sequences in the proximal region of the promoter and requires transcription factors c-Jun and ATF2 [3].
  • The minimum PGN fragment hydrolyzed by PGRP-L is MurNAc-tripeptide [2].
  • We report that human PGRP-L is a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase (EC 3.5.1.28), an enzyme that hydrolyzes the amide bond between MurNAc and l-Ala of bacterial PGN [2].
  • One mammalian PGRP, PGLYRP-2, is an N-acetylmuramoyl-L-alanine amidase that hydrolyses bacterial peptidoglycan and reduces its proinflammatory activity [4].
 

Biological context of PGLYRP2

  • Digestion of serum NAMLAA with trypsin, chymotrypsin, or trypsin plus V8 protease, or with CNBr yielded, respectively, 37, 40, and 3 overlapping peptides that matched 100% and covered 81% of the deduced amino acid sequence of mature PGLYRP2 [5].
 

Anatomical context of PGLYRP2

 

Associations of PGLYRP2 with chemical compounds

  • Liver PGLYRP2 and serum NAMLAA had the same mass determined by mass spectrometry and polyacrylamide gel electrophoresis, and both proteins and recombinant PGLYRP2 reacted with polyclonal anti-NAMLAA and anti-PGLYRP2 antibodies, and with monoclonal anti-NAMLAA antibodies [5].
 

Other interactions of PGLYRP2

References

  1. Peptidoglycan recognition protein 2 (N-acetylmuramoyl-L-Ala amidase) is induced in keratinocytes by bacteria through the p38 kinase pathway. Wang, H., Gupta, D., Li, X., Dziarski, R. Infect. Immun. (2005) [Pubmed]
  2. Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidase. Wang, Z.M., Li, X., Cocklin, R.R., Wang, M., Wang, M., Fukase, K., Inamura, S., Kusumoto, S., Gupta, D., Dziarski, R. J. Biol. Chem. (2003) [Pubmed]
  3. Differential expression of peptidoglycan recognition protein 2 in the skin and liver requires different transcription factors. Li, X., Wang, S., Wang, H., Gupta, D. J. Biol. Chem. (2006) [Pubmed]
  4. Mammalian PGRPs: novel antibacterial proteins. Dziarski, R., Gupta, D. Cell. Microbiol. (2006) [Pubmed]
  5. Identification of serum N-acetylmuramoyl-l-alanine amidase as liver peptidoglycan recognition protein 2. Zhang, Y., van der Fits, L., Voerman, J.S., Melief, M.J., Laman, J.D., Wang, M., Wang, H., Wang, M., Li, X., Walls, C.D., Gupta, D., Dziarski, R. Biochim. Biophys. Acta (2005) [Pubmed]
 
WikiGenes - Universities