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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
Overview Studies Clinical Trials
Score 2
2001 pubmed

Processing site and gene structure for the murine antimicrobial peptide CRAMP.

Pestonjamasp. V K VK; Huttner. K H KH; Gallo. R L RL

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Key Findings

  • The mature CRAMP peptide starts with a specific amino‑terminal sequence that was identified by sequencing.
  • The mouse CRAMP gene (Cnlp) shares structural features and transcription‑factor binding sites with the human LL‑37 gene.
  • Overall similarity suggests CRAMP is a useful animal model for investigating human cathelicidin function and regulation.

Practical Outcomes

  • For biohackers, the main takeaway is that mouse CRAMP can be used in lab experiments to explore how LL‑37 might be regulated or enhanced, but the study does not provide direct dosing or supplementation advice for humans. It confirms that insights gained from mouse studies are likely relevant to human LL‑37 research.

Summary

Scientists mapped the mouse antimicrobial peptide called CRAMP and showed it looks a lot like the human peptide LL-37, especially in the part that becomes active and in the gene’s control regions. This means mouse CRAMP can serve as a good stand‑in for studying how LL-37 works in the body.

Abstract

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.

Study Information

Provider

pubmed

Year

2001

DOI

10.1016/s0196-9781(01)00499-5