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LL-37

Potential Benefits of LL-37

  • Significantly boosts immune function [1-19]
  • Fights inflammation [20-29]
  • Prevents cancer progression [30-59]
  • Accelerates wound healing [60-67]
  • Lowers the risk of heart disease [68-70]
  • Prevents lung injury [71-72]
  • Promotes bone repair [73-77]

What is LL-37?

LL-37, also known as Human Cathelicidin Antimicrobial Peptide (CAMP), is touted as a “mammal’s core tool” to fight off various harmful microorganisms in the body. It’s produced by many cell types including natural killer (NK) cells, white blood cells, and skin cells. In addition, different body systems such as the respiratory system, gastrointestinal tract, testes, and ocular surface also produce LL-37. This powerful peptide has piqued the interest of the research community because its immune-modulating activities have the potential to accelerate tissue recovery and significantly improve the survival rate of patients with chronic debilitating medical conditions.

How LL-37 Works?

The human cathelicidin LL-37 serves a critical role in the innate immune system by defending against bacterial infections. LL-37 can interact with the molecules of the cell wall and perforate cytoplasmic membranes resulting in bacterial cell death. In addition, LL-37 helps promote wound closure by stimulating the formation of new blood vessels (angiogenesis).

Research on LL-37

Significantly Boosts Immune Function

An overwhelming body of research shows that this antimicrobial peptide regulates various important mechanisms involved in immune function:

  1. LL-37 boosts immune function by limiting the damage caused by bacterial products and recruiting immune cells to the site of infection. [1]
  2. A cell study found that LL-37 has the ability to inhibit the formation of bacterial biofilms (densely packed communities of microbial cells). [2]
  3. A cell study also found that LL-37 may help enhance the immunomodulatory function of human placenta-derived MSCs (pMSCs). [3]
  4. A study found that LL-37 was deadly against Staphylococcus aureus, the most common cause of upper respiratory tract infections. [4]
  5. LL-37 demonstrated strong antimicrobial activity against eye pathogens (infectious microorganisms). [5]
  6. Studies showed that LL-37 destroyed harmful microorganisms by inducing programmed cell death (apoptosis). [6-8]
  7. A study found that LL-37 can kill a broad spectrum of bacteria. [9-10]
  8. LL-37 boosts immune response by attracting immune cells including T cells, monocytes, neutrophils, and mast cells to the site of infection. [11-12]
  9. LL-37 also affects the maturation of dendritic cells (antigen-presenting cells). [13]
  10. LL-37 stimulates the production of immune cells such as cytokines, chemokines, and their receptors. [14-15]
  11. Higher blood levels of LL-37 were associated with a lower risk of death from infection in dialysis patients. [16]
  12. In patients with psoriasis, LL-37 worked synergistically with human beta-defensin 2 (HBD-2) in killing Staphylococcus aureus (S. aureus) bacteria. [17]
  13. A study showed that LL-37 may be beneficial in treating patients with sepsis. [18]
  14. A study showed that LL-37 enhanced the effects of lysozyme against S. aureus. [19]

Fights Inflammation

Aside from its immune-boosting properties, LL-37 also has potent anti-inflammatory activity according to high-quality studies:

  1. In patients who had surgical removal of the tonsils, those with high levels of LL-37 had lesser inflammation compared to those with low LL-37. [20]
  2. LL-37 suppresses the translocation of NF-kB to the nucleus, which creates an anti-inflammatory effect. [21]
  3. In mice, LL-37 administration reduced the risk of inflammatory disease. [22]
  4. LL-37 reduces inflammation by modulating inflammatory pathways in the body. [23-25]
  5. In human gum cells, LL-37 strongly reduced the levels of pro-inflammatory cytokines and chemokines. [26]
  6. LL-37 also modulates the inflammatory and host defense response of human white blood cells. [27]
  7. In mouse models, LL-37 provided protection against collagen damage which normally occurs in inflammatory arthritis. [28]
  8. A study showed that LL-37 was effective in regulating inflammation induced by interleukin-32. [29]

Prevents Cancer Progression

Studies show that LL-37 can help ward off deadly cancers:

  1. A cell study found that LL-37 has the potential to suppress cancer growth. [30]
  2. In another cell study, LL-37 suppressed the growth of colon cancer by inducing programmed cell death. [31]
  3. A study found that LL-37 has an anti-cancer effect in colon cancer, gastric cancer, skin cancer, ovarian cancer, lung cancer, breast cancer, prostate cancer, hematologic malignancy, and oral cancer. [32]
  4. In various human cancer cell lines, LL-37 exhibited anti-cancer effects similar to chemotherapeutic drugs. [33]
  5. In human lung cancer cell lines, LL-37 suppressed cancer progression by reducing the production of pro-inflammatory cytokines. [34]
  6. Cell studies have shown that LL-37 can inhibit the migration and invasiveness of prostate cancer cells. [35-40]
  7. In colon cancer, gastric cancer, and skin cancer cell lines, treatment with LL-37 prevented cancer cell progression.[41-46]
  8. In colon cancer cell lines, LL-37 destroyed cancer cells by stimulating signaling pathways involved in programmed cell death. [47-51]
  9. In gastric cancer cell lines, LL-37 inhibited gastric cancer cell proliferation through activation of signaling pathways involved in cell cycle arrest. [52-55]
  10. In leukemic cell lines, recombinant LL-37 treatment killed malignant cells by activating programmed cell death. [56-57]
  11. In human oral cancer cell lines, treatment with LL-37 destroyed malignant cells by damaging their DNA. [58-59]

Accelerates Wound Healing

Studies also show that this peptide can help stimulate faster regeneration of wounds:

  1. In patients with venous leg ulcers, LL-37 treatment was associated with a faster healing rate (almost six-fold higher) compared to placebo. [60]
  2. In mice, LL-37 treatment promoted wound healing through the production of new blood vessels. [61]
  3. A cell study found that LL-37 induces wound healing by stimulating the proliferation and migration of cells necessary for regeneration. [62]
  4. In mice, LL-37 treatment improved re-epithelialization and granulation tissue formation – both of these processes are necessary for wound healing. [63-64]
  5. Cell studies found that LL-37 improves wound healing through its antimicrobial activity. [65-66]
  6. In patients with venous leg ulcers, low-dose LL-37 treatment markedly decreased the mean ulcer area. [67]

Lowers the Risk of Heart Disease

LL-37 has also been found to possess cardioprotective effects:

  1. A study showed that LL-37 can protect against atherosclerosis (plaque build-up within the heart arteries). [68]
  2. A study also found that LL-37 inhibited cell death in the heart, suggesting that increasing its level might have therapeutic benefits against heart failure. [69]
  3. In mice, heart failure was associated with a decrease in LL-37 levels and this deficiency worsened the condition. [70]

Prevents Lung Injury

Studies found that LL-37 is essential for healthy lungs:

  1. In mice, LL-37 attenuated the progression of lung injury by controlling inflammation and preventing infection. [71]
  2. A study reported that LL-37 is an effective inflammatory regulator in various lung diseases. [72]

Promotes Bone Repair

Evidence also suggests that LL-37 is vital for bone repair:

  1. A mice study found that LL-37-treated white blood cells promoted bone formation. [73]
  2. Cell studies also found that LL-37 can help prevent bone disorders by inhibiting bone breakdown. [74-75]
  3. In rats with bone defects, LL-37 treatment markedly induced newly formed bones. [76]
  4. A cell study reported that LL-37 induced bone formation by recruiting stem cells into the site of injury. [77]

Associated Side Effects of LL-37

LL-37 side effects are very uncommon. There have been some side effects associated with the use of this drug wherein the patient had one of the issues listed below at some point while being on LL-37. However, these side effects weren’t confirmed to be associated with the treatment and could have been a coincidence and not related to the use of LL-37. Despite this, it was listed as a side effect associated with LL-37 even though these associated side effects are very uncommon.

Side effects associated with LL-37 may include the following:

  • Increased inflammation
  • Induction of autoimmune disease
  • Depression
  • Damage to sperm surface membranes

Reference

  1. Scott MG, Davidson DJ, Gold MR, Bowdish D, Hancock RE. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J Immunol. 2002;169(7):3883-91.
  2. Overhage J, Campisano A, Bains M, Torfs EC, Rehm BH, Hancock RE. Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect Immun. 2008;76(9):4176-82.
  3. Oliveira-Bravo M, Sangiorgi BB, Schiavinato JL, et al. LL-37 boosts immunosuppressive function of placenta-derived mesenchymal stromal cells. Stem Cell Res Ther. 2016;7(1):189. Published 2016 Dec 30. doi:10.1186/s13287-016-0448-3.
  4. Aboualaiwa MH, Reznikov LR, Gansemer ND, et al. pH modulates the activity and synergism of the airway surface liquid antimicrobials β-defensin-3 and LL-37. ProcNatlAcadSci USA. 2014;111(52):18703-8.
  5. Huang LC, Petkova TD, Reins RY, Proske RJ, Mcdermott AM. Multifunctional roles of human cathelicidin (LL-37) at the ocular surface. Invest Ophthalmol Vis Sci. 2006;47(6):2369-80.
  6. De yang, Chen Q, Schmidt AP, et al. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med. 2000;192(7):1069-74.
  7. Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev. 2003;55(1):27-55.
  8. Cassagnes LE, Hervé V, Nepveu F, Hureau C, Faller P, Collin F. The catalytically active copper-amyloid-Beta state: coordination site responsible for reactive oxygen species production. AngewChemInt Ed Engl. 2013;52(42):11110-3.
  9. Dürr UHN, Sudheendra US, Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. BiochimBiophysActa. 2006 Sep;1758:1408–1425.
  10. Duplantier AJ, van Hoek ML. The Human Cathelicidin Antimicrobial Peptide LL-37 as a Potential Treatment for Polymicrobial Infected Wounds. Front Immunol. 2013;4:143.
  11. De Yang, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, et al. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med. 2000 Oct 2;192:1069–1074
  12. Niyonsaba F, Iwabuchi K, Someya A, Hirata M, Matsuda H, Ogawa H, et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology. 2002 May;106:20–26.
  13. Davidson DJ, Currie AJ, Reid GSD, Bowdish DME, MacDonald KL, Ma RC, et al. The cationic antimicrobial peptide LL-37 modulates dendritic cell differentiation and dendritic cell-induced T cell polarization. J ImmunolBaltimMd 1950. 2004 Jan 15;172:1146–1156.
  14. Pistolic J, Cosseau C, Li Y, Yu JJ, Filewod NCJ, Gellatly S, et al. Host defence peptide LL-37 induces IL-6 expression in human bronchial epithelial cells by activation of the NF-kappaB signaling pathway. J Innate Immun. 2009;1:254–267.
  15. Montreekachon P, Chotjumlong P, Bolscher JGM, Nazmi K, Reutrakul V, Krisanaprakornkit S. Involvement of P2X(7) purinergic receptor and MEK1/2 in interleukin-8 up-regulation by LL-37 in human gingival fibroblasts. J Periodontal Res. 2011 Jun;46:327–337.
  16. Gombart AF, Bhan I, Borregaard N, et al. Low plasma level of cathelicidin antimicrobial peptide (hCAP18) predicts increased infectious disease mortality in patients undergoing hemodialysis. Clin Infect Dis. 2009;48(4):418-24
  17. Ong PY, Ohtake T, Brandt C, Strickland I, Boguniewicz M, Ganz T, Gallo RL, Leung DY. Endogenous antimicrobial peptides and skin infections in atopic dermatitis. N Engl J Med. 2002 Oct 10;347(15):1151-60. doi: 10.1056/NEJMoa021481. PMID: 12374875.
  18. Ciornei CD, Sigurdardóttir T, Schmidtchen A, Bodelsson M. Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob Agents Chemother. 2005 Jul;49(7):2845-50. doi: 10.1128/AAC.49.7.2845-2850.2005. PMID: 15980359; PMCID: PMC1168709.
  19. Chen X, Niyonsaba F, Ushio H, Okuda D, Nagaoka I, Ikeda S, Okumura K, Ogawa H. Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli. J Dermatol Sci. 2005 Nov;40(2):123-32. doi: 10.1016/j.jdermsci.2005.03.014. Epub 2005 Jun 15. PMID: 15963694.
  20. Elenius V, Palomares O, Waris M, et al. The relationship of serum vitamins A, D, E and LL-37 levels with allergic status, tonsillar virus detection and immune response. PLoS ONE. 2017;12(2):e0172350.
  21. Mookherjee, N. et al. Modulation of the TLR-mediated inflammatory response by the endogenous human host defense peptide LL-37. J Immunol 176, 2455–2464 (2006).
  22. Pancreatic β-Cells Limit Autoimmune Diabetes via an Immunoregulatory Antimicrobial Peptide Expressed under the Influence of the Gut Microbiota. Sun J, Furio L, Mecheri R, van der Does AM, Lundeberg E, Saveanu L, Chen Y, van Endert P, Agerberth B, Diana J. Immunity. 2015 Aug 18;43(2):304-17.
  23. Kahlenberg JM, Kaplan MJ. Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease. J Immunol. 2013;191(10):4895-901.
  24. Yu X, Quan J, Long W, et al. LL-37 inhibits LPS-induced inflammation and stimulates the osteogenic differentiation of BMSCs via P2X7 receptor and MAPK signaling pathway. Exp Cell Res. 2018;372(2):178-187.
  25. Tjabringa GS, Rabe KF, Hiemstra PS. The human cathelicidin LL-37: a multifunctional peptide involved in infection and inflammation in the lung. PulmPharmacolTher. 2005;18(5):321-7.
  26. Jönsson D, Nilsson BO. The antimicrobial peptide LL-37 is anti-inflammatory and proapoptotic in human periodontal ligament cells. J Periodont Res. 2012;47(3):330-5.
  27. Alalwani SM, Sierigk J, Herr C, et al. The antimicrobial peptide LL-37 modulates the inflammatory and host defense response of human neutrophils. Eur J Immunol. 2010;40(4):1118–1126. doi:10.1002/eji.200939275.
  28. Chow LN, Choi KY, Piyadasa H, Bossert M, Uzonna J, Klonisch T, Mookherjee N. Human cathelicidin LL-37-derived peptide IG-19 confers protection in a murine model of collagen-induced arthritis. Mol Immunol. 2014 Feb;57(2):86-92. doi: 10.1016/j.molimm.2013.08.011. Epub 2013 Oct 1. PMID: 24091294.
  29. Choi KY, Napper S, Mookherjee N. Human cathelicidin LL-37 and its derivative IG-19 regulate interleukin-32-induced inflammation. Immunology. 2014 Sep;143(1):68-80. doi: 10.1111/imm.12291. PMID: 24666281; PMCID: PMC4137957.
  30. Hayashi M, Kuroda K, Ihara K, Iwaya T, Isogai E. Suppressive effect of an analog of the antimicrobial peptide of LL‑37 on colon cancer cells via exosome‑encapsulated miRNAs. Int J Mol Med. 2018;42(6):3009-3016.
  31. Ren SX, Cheng AS, To KF, et al. Host immune defense peptide LL-37 activates caspase-independent apoptosis and suppresses colon cancer. Cancer Res. 2012;72(24):6512-23.
  32. Chen X, Zou X, Qi G, et al. Roles and Mechanisms of Human Cathelicidin LL-37 in Cancer. Cell PhysiolBiochem. 2018;47(3):1060-1073.
  33. Kuroda K, Okumura K, Isogai H, Isogai E. The Human Cathelicidin Antimicrobial Peptide LL-37 and Mimics are Potential Anticancer Drugs. Front Oncol. 2015;5:144.
  34. Tjabringa GS, Aarbiou J, Ninaber DK, Drijfhout JW, Sørensen OE, Borregaard N, Rabe KF, Hiemstra PS: The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J Immunol 2003; 171: 6690-6696.
  35. Piktel E, Niemirowicz K, Wnorowska U, Wątek M, Wollny T, Głuszek K, Góźdź S, Levental I, Bucki R: The role of cathelicidin LL-37 in cancer development. Arch ImmunolTherExp (Warsz) 2016; 64: 33-46.
  36. Choi KY, Napper S, Mookherjee N: Human cathelicidin LL-37 and its derivative IG-19 regulate interleukin-32-induced inflammation. Immunology 2014; 143: 68-80.
  37. Di Virgilio F, Falzoni S, Giuliani AL, Adinolfi E: P2 receptors in cancer progression and metastatic spreading. CurrOpinPharmacol 2016; 29: 17-25.
  38. Qiu Y, Li WH, Zhang HQ, Liu Y, Tian XX, Fang WG: P2X7 mediates ATP-driven invasiveness in prostate cancer cells. PLoS One 2014; 9:e114371.
  39. Cha HR, Lee JH, Hensel JA, Sawant AB, Davis BH, Lee CM, Deshane JS, Ponnazhagan S: Prostate cancer-derived cathelicidin-related antimicrobial peptide facilitates macrophage differentiation and polarization of immature myeloid progenitors to protumorigenic macrophages. Prostate 2016; 76: 624-636.
  40. Roger S, Jelassi B, Couillin I, Pelegrin P, Besson P, Jiang LH: Understanding the roles of the P2X7 receptor in solid tumour progression and therapeutic perspectives. BiochimBiophysActa 2015; 1848: 2584-2602.
  41. Piktel E, Niemirowicz K, Wnorowska U, Wątek M, Wollny T, Głuszek K, Góźdź S, Levental I, Bucki R: The role of cathelicidin LL-37 in cancer development. Arch ImmunolTherExp (Warsz) 2016; 64: 33-46.
  42. Tuomela JM, Sandholm JA, Kaakinen M, Hayden KL, Haapasaari KM, Jukkola-Vuorinen A, Kauppila JH, Lehenkari PP, Harris KW, Graves DE, Selander KS: Telomeric G-quadruplex-forming DNA fragments induce TLR9-mediated and LL-37-regulated invasion in breast cancer cells in vitro. Breast Cancer Res Treat 2016; 155: 261-271.
  43. Wu WK, Wang G, Coffelt SB, Betancourt AM, Lee CW, Fan D, Wu K, Yu J, Sung JJ, Cho CH: Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications. Int J Cancer 2010; 127: 1741-1747.
  44. Wu WK, Sung JJ, To KF, Yu L, Li HT, Li ZJ, Chu KM, Yu J, Cho CH: The host defense peptide LL-37 activates the tumor-suppressing bone morphogenetic protein signaling via inhibition of proteasome in gastric cancer cells. J Cell Physiol 2010; 223: 178-186.
  45. An LL, Ma XT, Yang YH, Lin YM, Song YH, Wu KF: Marked reduction of LL-37/hCAP-18, an antimicrobial peptide, in patients with acute myeloid leukemia. Int J Hematol 2005; 81: 45-7.
  46. Chen X, Qi G, Qin M, Zou Y, Zhong K, Tang Y, Guo Y, Jiang X, Liang L, Zou X: DNA methylation directly downregulates human cathelicidin antimicrobial peptide gene (CAMP) promoter activity. Oncotarget 2017; 8: 27943-27952.
  47. Piktel E, Niemirowicz K, Wnorowska U, Wątek M, Wollny T, Głuszek K, Góźdź S, Levental I, Bucki R: The role of cathelicidin LL-37 in cancer development. Arch ImmunolTherExp (Warsz) 2016; 64: 33-46.
  48. Tuomela JM, Sandholm JA, Kaakinen M, Hayden KL, Haapasaari KM, Jukkola-Vuorinen A, Kauppila JH, Lehenkari PP, Harris KW, Graves DE, Selander KS: Telomeric G-quadruplex-forming DNA fragments induce TLR9-mediated and LL-37-regulated invasion in breast cancer cells in vitro. Breast Cancer Res Treat 2016; 155: 261-271.
  49. Ren SX, Cheng AS, To KF, Tong JH, Li MS, Shen J, Wong CC, Zhang L, Chan RL, Wang XJ, Ng SS, Chiu LC, Marquez VE, Gallo RL, Chan FK, Yu J, Sung JJ, Wu WK, Cho CH: Host immune defense peptide LL-37 activates caspase-independent apoptosis and suppresses colon cancer. Cancer Res 2012; 72: 6512-6523.
  50. Niemirowicz K, Prokop I, Wilczewska AZ, Wnorowska U, Piktel E, Wątek M, Savage PB, Bucki R: Magnetic nanoparticles enhance the anti-cancer activity of cathelicidin LL-37 peptide against colon cancer cells. Int J Nanomedicine 2015; 10: 3843-3853.
  51. Niemirowicz K, Durnaś B, Tokajuk G, Piktel E, Michalak G, Gu X, Kułakowska A, Savage PB, Bucki R: Formulation and candidacidal activity of magnetic nanoparticles coated with cathelicidin LL-37 and ceragenin CSA-13. Sci Rep 2017; 7: 4610.
  52. Wu WK, Sung JJ, To KF, Yu L, Li HT, Li ZJ, Chu KM, Yu J, Cho CH: The host defense peptide LL-37 activates the tumor-suppressing bone morphogenetic protein signaling via inhibition of proteasome in gastric cancer cells. J Cell Physiol 2010; 223: 178-186.
  53. Wu WK, Cho CH, Lee CW, Wu K, Fan D, Yu J, Sung JJ: Proteasome inhibition: a new therapeutic strategy to cancer treatment. Cancer Lett 2010; 293: 15-22.
  54. Prevete N, Liotti F, Visciano C, Marone G, Melillo RM, de Paulis A: The formyl peptide receptor 1 exerts a tumor suppressor function in human gastric cancer by inhibiting angiogenesis. Oncogene 2015; 34: 3826-3838.
  55. Li L, Chen K, Xiang Y, Yoshimura T, Su S, Zhu J, Bian XW, Wang JM: New development in studies of formyl-peptide receptors: critical roles in host defense. J LeukocBiol 2016; 99: 425-435.
  56. Mader JS, Mookherjee N, Hancock RE, Bleackley RC: The human host defense peptide LL-37 induces apoptosis in a calpain- and apoptosis-inducing factor-dependent manner involving Bax activity. Mol Cancer Res 2009; 7: 689-702.
  57. Yang D, Chertov O, Oppenheim JJ: Participation of mammalian defensins and cathelicidins in antimicrobial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J LeukocBiol 2001; 69: 691-697.
  58. Okumura K, Itoh A, Isogai E, Hirose K, Hosokawa Y, Abiko Y, Shibata T, Hirata M, Isogai H: C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells. Cancer Lett 2004; 212: 185-194.
  59. Chen X, Qi G, Qin M, Zou Y, Zhong K, Tang Y, Guo Y, Jiang X, Liang L, Zou X: DNA methylation directly downregulates human cathelicidin antimicrobial peptide gene (CAMP) promoter activity. Oncotarget 2017; 8: 27943-27952.
  60. Available from https://www.promorepharma.com/en/ll-37-healing-of-chronic-wounds/.
  61. Ramos R, Silva JP, Rodrigues AC, et al. Wound healing activity of the human antimicrobial peptide LL37. Peptides. 2011;32(7):1469-76.
  62. Shaykhiev R, Beisswenger C, Kändler K, et al. Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure. Am J Physiol Lung Cell Mol Physiol. 2005;289(5):L842-8.
  63. Carretero M, Escámez MJ, García M, et al. In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37. J Invest Dermatol. 2008;128(1):223-36.
  64. Heilborn JD, Nilsson MF, Kratz G, et al. J Invest Dermatol. 2003;120:379–389.
  65. Saporito P, Vangmouritzen M, Løbner-olesen A, Jenssen H. LL-37 fragments have antimicrobial activity against Staphylococcus epidermidis biofilms and wound healing potential in HaCaT cell line. J Pept Sci. 2018;24(7):e3080.
  66. Duplantier AJ, van Hoek ML. The Human Cathelicidin Antimicrobial Peptide LL-37 as a Potential Treatment for Polymicrobial Infected Wounds. Front Immunol. 2013;4:143. Published 2013 Jul 3. doi:10.3389/fimmu.2013.00143.
  67. Grönberg A, Mahlapuu M, Ståhle M, Whately-smith C, Rollman O. Treatment with LL-37 is safe and effective in enhancing healing of hard-to-heal venous leg ulcers: a randomized, placebo-controlled clinical trial. Wound Repair Regen. 2014;22(5):613-21.
  68. Edfeldt K, Agerberth B, Rottenberg ME, Gudmundsson GH, Wang XB, Mandal K, Xu Q, Yan ZQ. Involvement of the antimicrobial peptide LL-37 in human atherosclerosis. Arterioscler Thromb Vasc Biol. 2006 Jul;26(7):1551-7. doi: 10.1161/01.ATV.0000223901.08459.57. Epub 2006 Apr 27. PMID: 16645154..
  69. Bei Y, Pan LL, Zhou Q, Zhao C, Xie Y, Wu C, Meng X, Gu H, Xu J, Zhou L, Sluijter JPG, Das S, Agerberth B, Sun J, Xiao J. Cathelicidin-related antimicrobial peptide protects against myocardial ischemia/reperfusion injury. BMC Med. 2019 Feb 20;17(1):42. doi: 10.1186/s12916-019-1268-y. PMID: 30782145; PMCID: PMC6381635.
  70. Zhou Q, Pan LL, Xue R, et al. The anti-microbial peptide LL-37/CRAMP levels are associated with acute heart failure and can attenuate cardiac dysfunction in multiple preclinical models of heart failure. Theranostics. 2020;10(14):6167-6181. Published 2020 May 15. doi:10.7150/thno.46225.
  71. Qin X, Zhu G, Huang L, Zhang W, Huang Y, Xi X. LL-37 and its analog FF/CAP18 attenuate neutrophil migration in sepsis-induced acute lung injury. J Cell Biochem. 2019 Apr;120(4):4863-4871. doi: 10.1002/jcb.27641. Epub 2018 Dec 9. PMID: 30537236.
  72. Available at https://www.jacionline.org/article/S0091-6749(06)00727-5/abstract#articleInformation.
  73. Zhang Z, Shively JE. Generation of novel bone forming cells (monoosteophils) from the cathelicidin-derived peptide LL-37 treated monocytes. PLoS One. 2010 Nov 15;5(11):e13985. doi: 10.1371/journal.pone.0013985. PMID: 21085494; PMCID: PMC2981577.
  74. Yu X, Quan J, Long W, Chen H, Wang R, Guo J, Lin X, Mai S. LL-37 inhibits LPS-induced inflammation and stimulates the osteogenic differentiation of BMSCs via P2X7 receptor and MAPK signaling pathway. Exp Cell Res. 2018 Nov 15;372(2):178-187. doi: 10.1016/j.yexcr.2018.09.024. Epub 2018 Oct 1. PMID: 30287143.
  75. Supanchart C, Thawanaphong S, Makeudom A, Bolscher JG, Nazmi K, Kornak U, Krisanaprakornkit S. The antimicrobial peptide, LL-37, inhibits in vitro osteoclastogenesis. J Dent Res. 2012 Nov;91(11):1071-7. doi: 10.1177/0022034512460402. Epub 2012 Sep 13. PMID: 22983411.
  76. Kittaka M, Shiba H, Kajiya M, Fujita T, Iwata T, Rathvisal K, Ouhara K, Takeda K, Fujita T, Komatsuzawa H, Kurihara H. The antimicrobial peptide LL37 promotes bone regeneration in a rat calvarial bone defect. Peptides. 2013 Aug;46:136-42. doi: 10.1016/j.peptides.2013.06.001. Epub 2013 Jun 12. PMID: 23770151.
  77. He Y, Mu C, Shen X, Yuan Z, Liu J, Chen W, Lin C, Tao B, Liu B, Cai K. Peptide LL-37 coating on micro-structured titanium implants to facilitate bone formation in vivo via mesenchymal stem cell recruitment. Acta Biomater. 2018 Oct 15;80:412-424. doi: 10.1016/j.actbio.2018.09.036. Epub 2018 Sep 25. PMID: 30266635.
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