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Cathelicidins: a novel protein family with a common proregion and a variable C‐terminal antimicrobial domain
Author(s) -
Zanetti Margherita,
Gennaro Renato,
Romeo Domenico
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01050-o
Subject(s) - antimicrobial , terminal (telecommunication) , domain (mathematical analysis) , chemistry , microbiology and biotechnology , biology , computer science , mathematics , telecommunications , mathematical analysis
A novel protein family, showing a conserved proregion and a variable C‐terminal antimicrobial domain, and named0 cathelicidin, has been identified in mammalian myeloid cells. The conserved proregion shows sequence similarity to members of the cystatin superfamily of cysteine proteinase inhibitors. Cathelicidins are stored in the cytoplasmic granules of neutrophil leukocytes and release the antimicrobial peptides upon leukocyte activation. Some of these peptides can assume an α‐helical conformation, others contain one or two disulfide bonds, still others are Pro‐ and Arg‐rich, or Trp‐rich. In addition to bacterial killing, some of these peptides exert additional functions related to host defense such as LPS‐neutralization and promotion of wound healing.