The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes

Gudmundur H. Gudmundsson*, Birgitta Agerberth, Jacob Odeberg, Tomas Bergman, Berit Olsson, Rosalba Salcedo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

436 Citations (Scopus)


The peptide FA-LL-37, previously termed FALL-39, was originally predicted from an ORF of a cDNA clone isolated from a human bone marrow library. This peptide was synthesized and found to have antibacterial activity. We have now characterized and sequenced the complete gene for FA-LL-37, termed FALL39. It is a compact gene of 1963 bp with four exons. Exons 1-3 code for a signal sequence and the cathelin region. Exon 4 contains the information for the mature antibacterial peptide. Our results indicate that FALL39 is the only member of the cathelin gene family present in the human genome. Potential binding sites for acute-phase-response factors are identified in the promoter and in intron 2. A possible role for the cytokine interleukin-6 in the regulation of FALL39 is discussed. Anti-(FA-LL-37) IgG located the peptide in granulocytes and we isolated the mature peptide from these cells after degranulation. Structural analysis determined the mature peptide to be LL-37. To obtain LL-37 for antibacterial assays, synthetic FA-LL-37 was degraded with dipeptidyl-peptidase 1. This analysis showed that mature LL-37 is a potent antibacterial peptide.

Original languageEnglish
Pages (from-to)325-332
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number2
Publication statusPublished - 1996

Other keywords

  • dipeptidyl-peptidase I
  • flow cytometry
  • genomic cloning
  • peptide antibiotic
  • precursor processing


Dive into the research topics of 'The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes'. Together they form a unique fingerprint.

Cite this