Abstract:
:The mucosal epithelium secretes a variety of antimicrobial peptides that act as part of the innate immune system to protect against invading microbes. Here, we describe the functional properties of human defensin (HD) 5, the major antimicrobial peptide produced by Paneth cells in the ileum, in relation to its structure. The antimicrobial activity of HD-5 against Escherichia coli proved to be independent of its structure, whereas the unstructured peptide showed greatly reduced antimicrobial activity against Staphylococcus aureus. We find that HD-5 binds to the cell membrane of intestinal epithelial cells and induced secretion of the chemokine interleukin (IL)-8 in a concentration- and structure-dependent fashion. Incubation of HD-5 in the presence of tumor necrosis factor alpha further increased IL-8 secretion synergistically, suggesting that HD-5 may act as a regulator of the intestinal inflammatory response.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
de Leeuw E,Burks SR,Li X,Kao JP,Lu Wdoi
10.1016/j.febslet.2006.12.036subject
Has Abstractpub_date
2007-02-06 00:00:00pages
515-20issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01492-Xjournal_volume
581pub_type
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