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Significance of the LL-37 Peptide Delivered from Human Cathelicidin in the Pathogenesis, Treatment, and Diagnosis of Sepsis

Angelika Mańkowska

Angelika Mańkowska

Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
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Mańkowska, Angelika
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Paulina Paprocka

Paulina Paprocka

Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
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Paprocka, Paulina
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Grzegorz Król

Grzegorz Król

Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
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Król, Grzegorz
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Agata Lesiak

Agata Lesiak

Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
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Lesiak, Agata
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Jakub Spałek

Jakub Spałek

  • Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
  • Department of Otolaryngology, Holy-Cross Oncology Center of Kielce, Head and Neck SurgeryKielce, Poland
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Spałek, Jakub
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Ewelina Piktel

Ewelina Piktel

Independent Laboratory of Nanomedicine, Medical University of BiałystokBiałystok, Poland
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Piktel, Ewelina
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Sławomir Okła

Sławomir Okła

  • Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
  • Department of Otolaryngology, Holy-Cross Oncology Center of Kielce, Head and Neck SurgeryKielce, Poland
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Okła, Sławomir
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Piotr Bijak

Piotr Bijak

Department of Medical Microbiology and Nanobiomedical Engineering, Medical University of BiałystokBiałystok, Poland
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Bijak, Piotr
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Wiesława Niklińska

Wiesława Niklińska

Department of Histology and Embryology, Medical University of BiałystokBiałystok, Poland
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Niklińska, Wiesława
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Bonita Durnaś

Bonita Durnaś

  • Department of Microbiology and Immunology, Institute of Medical Science, Collegium Medicum, Jan Kochanowski University in KielceKielce, Poland
  • Department of Clinical Microbiology, Holy-Cross Oncology Center of KielceKielce, Poland
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Durnaś, Bonita
 und 
Robert Bucki

Robert Bucki

Department of Medical Microbiology and Nanobiomedical Engineering, Medical University of BiałystokBiałystok, Poland
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Bucki, Robert
  
07. Sept. 2025
Significance of the LL-37 Peptide Delivered from Human Cathelicidin in the Pathogenesis, Treatment, and Diagnosis of Sepsis's Cover Image
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Artikel-Kategorie: Review
Online veröffentlicht: 07. Sept. 2025
Eingereicht: 17. Apr. 2025
Akzeptiert: 07. Juni 2025
DOI: https://doi.org/10.2478/aite-2025-0025
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© 2025 Angelika Mańkowska et al., published by Sciendo
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Fig 1.

The pleiotropic function of human cathelicidin LL-37. In the extracellular environment, the LL-37 peptide has various functions resulting from its ability to activate certain plasma membrane receptors and/or to insert into the plasma membrane, thereby disrupting the integrity of the plasma membrane. LL-37 may also interact with substances that build microbial cells and components of the biofilm matrix. IL, interleukin; LPS, lipopolysaccharide; NETs, neutrophil extracellular traps; TNF-α, tumor necrosis factor-α.
The pleiotropic function of human cathelicidin LL-37. In the extracellular environment, the LL-37 peptide has various functions resulting from its ability to activate certain plasma membrane receptors and/or to insert into the plasma membrane, thereby disrupting the integrity of the plasma membrane. LL-37 may also interact with substances that build microbial cells and components of the biofilm matrix. IL, interleukin; LPS, lipopolysaccharide; NETs, neutrophil extracellular traps; TNF-α, tumor necrosis factor-α.

Fig 2.

Scheme of LL-37 peptide expression by immune cells during homeostatic balance (A) and during sepsis (B).
Scheme of LL-37 peptide expression by immune cells during homeostatic balance (A) and during sepsis (B).

Fig 3.

Ability of the peptide LL-37 to regulate the stiffness and cytoskeleton organization of the endothelial cell. EDHF, endothelium-derived hyperpolarizing factor; FPRL1/ALX, formyl peptide receptor-like 1/lipoxin A4 receptor; NO, nitric oxide; P2X7/purinergic channel receptor.
Ability of the peptide LL-37 to regulate the stiffness and cytoskeleton organization of the endothelial cell. EDHF, endothelium-derived hyperpolarizing factor; FPRL1/ALX, formyl peptide receptor-like 1/lipoxin A4 receptor; NO, nitric oxide; P2X7/purinergic channel receptor.
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