Cathelicidin

From Wikipedia, the free encyclopedia

Members of the Cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain. Cathelicidin peptides have been isolated from many different species of mammals. Cathelicidins were originally found in neutrophils but have since been found in many other cells (e.g., in macrophages activated by bacteria, viruses, fungi, or the hormone 1,25-D).[1] Members of the cathelicidin family include cathepsins.

Antimicrobial peptides

  1. ^ Philip T. Liu, et al., Toll-Like receptor...
  • Chromek, M., et al. The antimicrobial cathelicidin protects the urinary tract against invasive bacterial infection. Nature Medicine (June 2006) 12, 636-641. - http://dx.doi.org/10.1038/nm1407.
  • Gombart, A.F., et al. Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly upregulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB Journal (July 2005) 19, 1067-1077. - http://www.fasebj.org/cgi/content/full/19/9/1067.
  • López-García, B., et al. Expression and potential function of cathelicidin antimicrobial peptides in dermatophytosis and tinea versicolor. Journal of Antimicrobial Chemotherapy (May 2006) 57, 877-882. - http://dx.doi.org/10.1093/jac/dkl078.


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