Linked Life Data

20980996

Source:http://linkedlifedata.com/resource/pubmed/id/20980996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-4-19
pubmed:abstractText
Innate immune recognition of the bacterial cell wall constituent peptidoglycan by the cytosolic nucleotide-binding oligomerization domain 2 (Nod2) receptor has a pivotal role in the maintenance of intestinal mucosal homeostasis. Whereas peptidoglycan cleavage by gut-derived lysozyme preserves the recognition motif, the N-acetylmuramoyl-L-alanine amidase activity of the peptidoglycan recognition protein 2 (PGLYRP-2) destroys the Nod2-detected muramyl dipeptide structure. PGLYRP-2 green fluorescent protein (GFP) reporter and wild-type mice were studied by flow cytometry and quantitative RT-PCR to identify Pglyrp-2 expression in cells of the intestinal mucosa and reveal a potential regulatory function on epithelial peptidoglycan recognition. CD3(+)/CD11c(+) T lymphocytes revealed significant Pglyrp-2 expression, whereas epithelial cells and intestinal myeloid cells were negative. The mucosal Pglyrp-2-expressing lymphocyte population demonstrated a mixed T-cell receptor (TCR) ?? or ?? phenotype with predominant CD8? and less so CD8? expression, as well as significant staining for the activation markers B220 and CD69, presenting a typical intraepithelial lymphocyte phenotype. Importantly, exposure of peptidoglycan to PGLYRP-2 significantly reduced Nod2/Rip2-mediated epithelial activation. Also, moderate but significant alterations of the intestinal microbiota composition were noted in Pglyrp-2-deficient animals. PGLYRP-2 might thus have a significant role in regulation of the enteric host-microbe homeostasis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1935-3456
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
325-34
pubmed:meshHeading
pubmed-meshheading:20980996-Animals, pubmed-meshheading:20980996-Antigens, CD, pubmed-meshheading:20980996-Cells, Cultured, pubmed-meshheading:20980996-Genetic Engineering, pubmed-meshheading:20980996-Green Fluorescent Proteins, pubmed-meshheading:20980996-Host-Pathogen Interactions, pubmed-meshheading:20980996-Intestinal Mucosa, pubmed-meshheading:20980996-Lymphocyte Activation, pubmed-meshheading:20980996-Metagenome, pubmed-meshheading:20980996-Mice, pubmed-meshheading:20980996-Mice, Inbred C57BL, pubmed-meshheading:20980996-Mice, Knockout, pubmed-meshheading:20980996-N-Acetylmuramoyl-L-alanine Amidase, pubmed-meshheading:20980996-Nod2 Signaling Adaptor Protein, pubmed-meshheading:20980996-Peptidoglycan, pubmed-meshheading:20980996-Proteins, pubmed-meshheading:20980996-Receptors, Antigen, T-Cell, pubmed-meshheading:20980996-T-Lymphocytes
pubmed:year
2011
pubmed:articleTitle
Control of intestinal Nod2-mediated peptidoglycan recognition by epithelium-associated lymphocytes.
pubmed:affiliation
Institute of Medical Microbiology and Hospital Epidemiology, Hannover Medical School, Hannover, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural