Processing site and gene structure for the murine antimicrobial peptide CRAMP

Peptides. 2001 Oct;22(10):1643-50. doi: 10.1016/s0196-9781(01)00499-5.


Cathelicidins are a mammalian gene family notable for the presence of an antibiotic peptide encoded at the carboxy-terminal domain of the nascent pre-pro-protein. Following proteolytic release, this peptide has direct antimicrobial activity. To understand the function and regulation of cathelicidin we investigated the peptide processing site and gene structure of the mouse cathelicidin CRAMP. Amino acid sequencing of the purified native 5 kDa peptide identified the functionally critical amino terminal sequence of mature CRAMP. Characterization of the CRAMP gene (Cnlp) showed homology in structure and sequence identity in several potential transcription factors binding sites found in the human cathelicidin LL-37. Overall, CRAMP shows striking similarities with LL-37, making it a useful model for study of human cathelicidin function and regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antimicrobial Cationic Peptides / genetics*
  • Antimicrobial Cationic Peptides / isolation & purification*
  • Antimicrobial Cationic Peptides / metabolism
  • Base Sequence / genetics
  • Binding Sites / genetics
  • Binding Sites / physiology
  • Blood Proteins / genetics*
  • Blood Proteins / immunology
  • Blood Proteins / metabolism
  • Bone Marrow / metabolism
  • Genes / genetics*
  • Genes / physiology
  • Humans
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Prodrugs / metabolism
  • Protein Precursors / genetics*
  • Protein Precursors / immunology
  • Protein Precursors / metabolism
  • Transcription Factors / genetics


  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Prodrugs
  • Protein Precursors
  • Transcription Factors
  • cathelicidin 2 protein, mammal

Associated data

  • GENBANK/AF035680