The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
The Cathelicidin Anti-Microbial Peptide LL-37 is Involved in Re-Epithelialization of Human Skin Wounds and is Lacking in Chronic Ulcer Epithelium
Open accessAbstract
The human cathelicidin anti-microbial protein, hCAP18 is a component of the innate immune system and has broad anti-microbial activity conferred by its C-terminal fragment LL-37. hCAP18 is constitutively produced in leukocytes and is induced in barrier organs upon inflammation and infection. We demonstrate here a novel role for this peptide in re-epithelialization of skin wounds. We show that high levels of hCAP18 are produced in skin in vivo upon wounding. The highest hCAP18 levels are attained at 48 h post-injury, declining to pre-injury levels upon wound closure. hCAP18 is detected in the inflammatory infiltrate and in the epithelium migrating over the wound bed. In chronic ulcers, however, hCAP18 levels are low and immunoreactivity for hCAP18/LL-37 is absent in ulcer edge epithelium. Using a noninflammatory ex vivo wound healing model, composed of organ-cultured human skin, we show that hCAP18 is strongly expressed in healing skin epithelium, and that treatment with antibodies raised and affinity purified against LL-37, inhibits re-epithelialization in a concentration-dependent manner. Immunoreactivity for the proliferation marker Ki67 is absent in the epithelium of such inhibited wounds, suggesting that LL-37 may play a part in epithelial cell proliferation. Thus, we suggest that, in addition to being an anti-microbial peptide, LL-37 also plays a part in wound closure and that its reduction in chronic wounds impairs re-epithelialization and may contribute to their failure to heal.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Abnormal or dysfunctional AMP production has been associated with susceptibility to microbial infections and several other cutaneous diseases, including nonhealing wounds.29”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [29]
In the citing paper
“Wound fluids and skin wounds show elevated levels of cathelicidin expression in keratinocytes and other immune cells, reaching a maximum at 48 h.29”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [29]
In the citing paper
“Using a noninflammatory ex vivo wound healing model comprising organ-cultured human skin, it has been shown that hCAP18 is strongly expressed in healing skin epithelium and that treatment with affinity-purified antibodies raised against LL-37 inhibits reepithelialization in a concentration-dependent manner.29”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [29]
In the citing paper
“Cathelicidin is low in venous leg ulcers and absent at the margin of other nonhealing wounds.29”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [29]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids
Fields, G., & NOBLE, R. L. (1990) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1990.tb00939.x · Cited by 2,490
A peptide antibiotic from human skin
Harder, J., Bartels, J., Christophers, E., & Schröder, J. ‐. (1997) · Nature · doi:10.1038/43088 · Cited by 1,365
Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
Human β-Defensin-1 Is a Salt-Sensitive Antibiotic in Lung That Is Inactivated in Cystic Fibrosis
Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., ZASLOFF, M. A., & Wilson, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81895-4 · Cited by 1,077
Defensins: Antimicrobial and Cytotoxic Peptides of Mammalian Cells
Lehrer, R. I., Lichtenstein, A. K., & Ganz, T. (1993) · Annual Review of Immunology · doi:10.1146/annurev.iy.11.040193.000541 · Cited by 1,000
Analysis of the acute and chronic wound environments: the role of proteases and their inhibitors
Trengove, N. J., Stacey, M. C., Macauley, S., Bennett, N., Gibson, J., Burslem, F., Murphy, G., & Schultz, G. (1999) · Wound Repair and Regeneration · doi:10.1046/j.1524-475x.1999.00442.x · Cited by 908
Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N. (2001) · Blood · doi:10.1182/blood.v97.12.3951 · Cited by 894
Self-citationFrohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803
Self-citation
Cited by
Sorted by citations
Items 101–200 of 572
Developmental switch of intestinal antimicrobial peptide expression
Ménard, S., Förster, V., Lotz, M., Gütle, D., Duerr, C. U., Gallo, R. L., Henriques‐Normark, B., Pütsep, K., Andersson, M., Glocker, E. O., et al. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071022 · Cited by 151
Dendritic epidermal T cells regulate skin antimicrobial barrier function
MacLeod, A. S., Hemmers, S., Garijo, O., Chabod, M., Mowen, K., Witherden, D. A., & Havran, W. L. (2013) · Journal of Clinical Investigation · doi:10.1172/jci70064 · Cited by 152
Innate Defense Regulator Peptide 1018 in Wound Healing and Wound Infection
Steinstraesser, L., Hirsch, T., Schulte, M., Kueckelhaus, M., Jacobsen, F., Mersch, E., Stricker, I., Afacan, N. J., Jenssen, H., Hancock, R. E. W., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039373 · Cited by 151
Lau, Y. E., Rozek, A., Scott, M. G., Goosney, D. L., Davidson, D. J., & Hancock, R. E. W. (2004) · Infection and Immunity · doi:10.1128/iai.73.1.583-591.2005 · Cited by 145
Sáinz, B., Alcalá, S., García, E., Sanchez-Ripoll, Y., Azevedo, M. M., Cioffi, M., Tatari, M. N., Miranda‐Lorenzo, I., Hidalgo, M. M., Goméz-López, G., et al. (2015) · Gut · doi:10.1136/gutjnl-2014-308935 · Cited by 145
Feng, X., Sambanthamoorthy, K., Palys, T. J., & Paranavitana, C. M. (2013) · Peptides · doi:10.1016/j.peptides.2013.09.007 · Cited by 143
Niyonsaba, F., & Ogawa, H. (2005) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2005.07.009 · Cited by 144
Involvement of the Antimicrobial Peptide LL-37 in Human Atherosclerosis
Edfeldt, K., Agerberth, B., Rottenberg, M. E., Gudmundsson, G. H., Wang, X.-B., Mandal, K., Xu, Q., & Yan, Z. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000223901.08459.57 · Cited by 147
Estrogen Supports Urothelial Defense Mechanisms
Lüthje, P., Brauner, H., Ramos, N. L., Övregaard, A., Gläser, R., Hirschberg, A. L., Aspenström, P., & Brauner, A. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3005574 · Cited by 141
The role of the multifunctional peptide LL-37 in host defense
Kai-Larsen, Y. (2008) · Frontiers in bioscience · doi:10.2741/2964 · Cited by 145
Roudi, R., Syn, N. L., & Roudbary, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01320 · Cited by 139
Phenylbutyrate Induces Antimicrobial Peptide Expression
Steinmann, J., Halldórsson, S., Agerberth, B., & Gudmundsson, G. H. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00818-09 · Cited by 140
The Extracellular Matrix in Wound Healing: A Closer Look at Therapeutics for Chronic Wounds
Agren, M. S., & Werthen, M. (2007) · The International Journal of Lower Extremity Wounds · doi:10.1177/1534734607301394 · Cited by 136
Unique features of human cathelicidin LL ‐37
Bandurska, K., Berdowska, A., Barczyńska, R., & Krupa, P. (2015) · BioFactors · doi:10.1002/biof.1225 · Cited by 139
Antimicrobial peptides – Unleashing their therapeutic potential using nanotechnology
Gera, S., Kankuri, E. M., & Kogermann, K. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107990 · Cited by 137
Emerging Roles of Vitamin D-Induced Antimicrobial Peptides in Antiviral Innate Immunity
White, J. H. (2022) · Nutrients · doi:10.3390/nu14020284 · Cited by 148
Wu, W. K. K., Wang, G., Coffelt, S. B., Betancourt, A. M., Lee, C. W., Fan, D., Wu, K., Yu, J. Q., Sung, J. J. �., & Cho, C. H. (2010) · International Journal of Cancer · doi:10.1002/ijc.25489 · Cited by 136
Haisma, E. M., de Breij, A., Chan, H. L., van Dissel, J. T., Drijfhout, J. W., Hiemstra, P. S., Ghalbzouri, A. E., & Nibbering, P. H. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02554-14 · Cited by 134
The Role of Antimicrobial Peptides at the Ocular Surface
McDermott, A. M. (2008) · Ophthalmic Research · doi:10.1159/000187622 · Cited by 134
Fumakia, M., & Ho, E. A. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b00099 · Cited by 132
Heilborn, J. D., Nilsson, M. F., Chamorro, C. I., Sandstedt, B., Borregaard, N., Tham, E., Sørensen, O. E., Weber, G., & Ståhle, M. (2004) · International Journal of Cancer · doi:10.1002/ijc.20795 · Cited by 127
Self-citationThe human cathelicidin hCAP18/LL-37: A multifunctional peptide involved in mycobacterial infections
Méndez‐Samperio, P. (2010) · Peptides · doi:10.1016/j.peptides.2010.06.016 · Cited by 128
Interaction of the Microbiome with the Innate Immune Response in Chronic Wounds
Grice, E. A., & Segre, J. A. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0106-3_4 · Cited by 129
The role of cathelicidin and defensins in pulmonary inflammatory diseases
Herr, C., Shaykhiev, R., & Bals, R. (2007) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.7.9.1449 · Cited by 126
Innate antimicrobial immunity in the skin: A protective barrier against bacteria, viruses, and fungi
Coates, M., Blanchard, S., & MacLeod, A. S. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007353 · Cited by 134
Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens
LaRock, C. N., & Nizet, V. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.02.010 · Cited by 124
Zhang, Z., Cherryholmes, G. A., Chang, F., Rose, D. M., Schraufstätter, I. U., & Shively, J. E. (2009) · European Journal of Immunology · doi:10.1002/eji.200939496 · Cited by 119
Defensins and Other Antimicrobial Peptides at the Ocular Surface
McDermott, A. M. (2004) · The Ocular Surface · doi:10.1016/s1542-0124(12)70111-8 · Cited by 118
Kindrachuk, J., Jenssen, H., Elliott, M. R., Nijnik, A., Janot, L., Pasupuleti, M., Thorson, L., Ma, S., Easton, D. M., Bains, M., et al. (2012) · Innate Immunity · doi:10.1177/1753425912461456 · Cited by 119
Kovach, M. A., Ballinger, M. N., Newstead, M. W., Zeng, X., Bhan, U., Yu, F. X., Moore, B. B., Gallo, R. L., & Standiford, T. J. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103196 · Cited by 116
Antimicrobial Peptides in Human Skin
Harder, J., & Schröder, J. (2005) · KARGER eBooks · doi:10.1159/000086650 · Cited by 119
NETs: the missing link between cell death and systemic autoimmune diseases?
Darrah, E., & Andrade, F. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00428 · Cited by 120
Yu, F. X., Cornicelli, M. D., Kovach, M. A., Newstead, M. W., Zeng, X., Kumar, A., Gao, N., Yoon, S. G., Gallo, R. L., & Standiford, T. J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000509 · Cited by 112
John, J. V., Sharma, N. S., Tang, G., Luo, Z., Su, Y., Weihs, S., Shahriar, S. M. S., Wang, G., McCarthy, A. D., Dyke, J. S., et al. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202206936 · Cited by 111
Thinking Outside the Bug: Molecular Targets and Strategies to Overcome Antibiotic Resistance
Monserrat‐Martinez, A., Gambin, Y., & Sierecki, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061255 · Cited by 116
Cathelicidin Host Defense Peptides and Inflammatory Signaling: Striking a Balance
Alford, M. A., Baquir, B., Santana, F. L., Haney, E. F., & Hancock, R. E. W. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01902 · Cited by 109
Innate immune defence in the human gastrointestinal tract
Dommett, R. M., Zilbauer, M., George, J. T., & Bajaj‐Elliott, M. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2004.12.004 · Cited by 109
Mookherjee, N., Wilson, H. L., Doria, S., Popowych, Y., Falsafi, R., Yu, J., Li, Y., Veatch, S. L., Roche, F. M., Brown, K. L., et al. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0106048 · Cited by 109
Interactions between epithelial cells and leukocytes in immunity and tissue homeostasis
Shaykhiev, R., & Bals, R. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0207096 · Cited by 110
García-Orue, I., Gainza, G., Girbau, C., Alonso, R., Aguirre, J. J., Pedraz, J. L., Igartúa, M., & Hernández, R. M. (2016) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2016.04.006 · Cited by 114
Coffelt, S. B., Waterman, R. S., Flórez, L., zu Bentrup, K. H., Zwezdaryk, K. J., Tomchuck, S. L., LaMarca, H. L., Danka, E. S., Morris, C. A., & Scandurro, A. B. (2007) · International Journal of Cancer · doi:10.1002/ijc.23186 · Cited by 116
Bridle, A. R., Nosworthy, E., Polinski, M. P., & Nowak, B. F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023417 · Cited by 109
Antimicrobial peptides and the skin
Bardan, A., Nizet, V., & Gallo, R. L. (2004) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.4.4.543 · Cited by 112
Vitamin D signaling in intestinal innate immunity and homeostasis
Dimitrov, V., & White, J. H. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.04.010 · Cited by 108
Anti-LL37 Antibodies Are Present in Psoriatic Arthritis (PsA) Patients: New Biomarkers in PsA
Frasca, L., Palazzo, R., Chimenti, M. S., Alivernini, S., Tolusso, B., Bui, L., Botti, E., Giunta, A., Bianchi, L., Petricca, L., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01936 · Cited by 106
Induction of the human cathelicidin LL-37 as a novel treatment against bacterial infections
van der Does, A. M., Bergman, P., Agerberth, B., & Lindbom, L. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0412178 · Cited by 107
Mookherjee, N., Hamill, P., Gardy, J. L., Blimkie, D., Falsafi, R., Chikatamarla, A., Arenillas, D. J., Doria, S., Kollmann, T. R., & Hancock, R. E. W. (2009) · Molecular BioSystems · doi:10.1039/b813787k · Cited by 110
Species-specific regulation of innate immunity by vitamin D signaling
Dimitrov, V., & White, J. H. (2015) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2015.09.016 · Cited by 104
MicroRNA-132 with Therapeutic Potential in Chronic Wounds
Li, X., Li, D., Wang, A., Chu, T., Lohcharoenkal, W., Zheng, X., Grünler, J., Narayanan, S., Eliasson, S., Herter, E. K., et al. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.08.003 · Cited by 103
Wu, W. K. K., Sung, J. J. �., To, K. F., Yu, L., Li, H. T., Li, Z. J., Chu, K. M., Yu, J. Q., & Cho, C. H. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22026 · Cited by 102
Ron‐Doitch, S., Sawodny, B., Kühbacher, A., David, M. M. N., Samanta, A., Phopase, J., Burger‐Kentischer, A., Griffith, M., Golomb, G., & Rupp, S. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.03.025 · Cited by 100
Gunasekera, S., Muhammad, T., Strömstedt, A. A., Rosengren, K. J., & Göransson, U. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00168 · Cited by 100
Review: Human antimicrobial proteins — effectors of innate immunity
Harder, J., Gläser, R., & Schröder, J. (2007) · Journal of Endotoxin Research · doi:10.1177/0968051907088275 · Cited by 101
Diabetic Wound Repair: From Mechanism to Therapeutic Opportunities
Wang, R., Gu, S., Kim, Y. H., Lee, A., Lin, H., & Jiang, D. (2025) · MedComm · doi:10.1002/mco2.70406 · Cited by 118
Antimicrobial Activities of Chemokines: Not Just a Side-Effect?
Wolf, M., & Moser, B. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00213 · Cited by 96
Immune Response in the Barrier Epithelia: Lessons from the Fruit Fly Drosophila melanogaster
Davis, M. M., & Engström, Y. (2012) · Journal of Innate Immunity · doi:10.1159/000332947 · Cited by 97
Human antimicrobial protein hCAP18/LL-37 promotes a metastatic phenotype in breast cancer
Weber, G., Chamorro, C. I., Granath, F. N., Liljegren, A., Zreika, S., Saidak, Z., Sandstedt, B., Rotstein, S., Mentaverri, R., Sánchez, F., et al. (2009) · Breast Cancer Research · doi:10.1186/bcr2221 · Cited by 98
Self-citationMolecular mechanisms of LL-37-induced receptor activation: An overview
Verjans, E., Zels, S., Luyten, W. H. M. L., Landuyt, B., & Schoofs, L. (2016) · Peptides · doi:10.1016/j.peptides.2016.09.002 · Cited by 94
Jacobsen, F., Mittler, D., Hirsch, T., Gerhards, A., Lehnhardt, M., Voß, B., Steinau, H., & Steinstraesser, L. (2005) · Gene Therapy · doi:10.1038/sj.gt.3302568 · Cited by 94
The Human Antimicrobial Peptide LL-37 Suppresses Apoptosis in Keratinocytes
Chamorro, C. I., Weber, G., Grönberg, A., Pivarcsi, A., & Ståhle, M. (2008) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.321 · Cited by 94
Self-citationEffects of the cathelicidin LL-37 on intestinal epithelial barrier integrity
Otte, J., Zdebik, A., Brand, S., Chromik, A. M., Strauß, S., Schmitz, F., Steinstraesser, L., & Schmidt, W. E. (2009) · Regulatory Peptides · doi:10.1016/j.regpep.2009.03.009 · Cited by 94
Apoptosis of Airway Epithelial Cells
Lau, Y. E., Bowdish, D. M. E., Cosseau, C., Hancock, R. E. W., & Davidson, D. J. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0170oc · Cited by 99
Human antimicrobial peptides in ocular surface defense
Mohammed, I., Said, D. G., & Dua, H. S. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.03.004 · Cited by 94
Tjabringa, G. S., Rabe, K. F., & Hiemstra, P. S. (2005) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2005.01.001 · Cited by 93
Coffelt, S. B., & Scandurro, A. B. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0044 · Cited by 88
Pathogenesis of wound healing disorders in the elderly
Makrantonaki, E., Wlaschek, M., & Scharffetter‐Kochanek, K. (2017) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1111/ddg.13199 · Cited by 92
Bergman, P., Johansson, L., Wan, H., Jones, A., Gallo, R. L., Gudmundsson, G. H., Hökfelt, T. G. M., Jonsson, A., & Agerberth, B. (2006) · Infection and Immunity · doi:10.1128/iai.01043-06 · Cited by 87
Lynn, M. A., Kindrachuk, J., Marr, A. K., Jenssen, H., Panté, N., Elliott, M. R., Napper, S., Hancock, R. E. W., & McMaster, W. R. (2011) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0001141 · Cited by 88
A comparison of epithelial-to-mesenchymal transition and re-epithelialization
Leopold, P. L., Vincent, J., & Wang, H. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.07.003 · Cited by 93
Clinical reviews in allergy and immunology
Leung, D. Y. M., Ledford, D. K., Wechsler, M. E., Fulkerson, P. C., Bochner, B. S., Gauvreau, G. M., Gleich, G. J., Henkel, T., Kolbeck, R., Mathur, S. K., et al. (2012) · Cited by 87
Endogenous production of antimicrobial peptides in innate immunity and human disease
Gallo, R. L., & Nizet, V. (2003) · Current Allergy and Asthma Reports · doi:10.1007/s11882-003-0074-x · Cited by 89
Thakur, A., Sharma, A., Alajangi, H. K., Jaiswal, P. K., Lim, Y., Singh, G., & Barnwal, R. P. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.07.103 · Cited by 86
Girnita, A., Zheng, H., Grönberg, A., Girnita, L., & Ståhle, M. (2011) · Oncogene · doi:10.1038/onc.2011.239 · Cited by 90
RetractedAntiviral Potential of Cathelicidins
Barlow, P. G., Findlay, E. G., Currie, S. M., & Davidson, D. J. (2013) · Future Microbiology · doi:10.2217/fmb.13.135 · Cited by 89
Expression and purification of a recombinant LL-37 from Escherichia coli
Moon, J. Y., Henzler‐Wildman, K. A., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.003 · Cited by 84
Multifunctional Roles of Human Cathelicidin (LL-37) at the Ocular Surface
Huang, L. C. L., Petkova, T. D., Reins, R. Y., Proske, R. J., & McDermott, A. M. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-1649 · Cited by 85
Steinstraesser, L., Kraneburg, U. M., Hirsch, T., Kesting, M. R., Steinau, H., Jacobsen, F., & Al‐Benna, S. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10093951 · Cited by 83
Antimicrobial Peptide LL‐37 Internalized by Immature Human Dendritic Cells Alters their Phenotype
Bandholtz, L., Ekman, G. J., Vilhelmsson, M., Buentke, E., Agerberth, B., Scheynius, A., & Gudmundsson, G. H. (2006) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2006.001752.x · Cited by 86
From frog integument to human skin: dermatological perspectives from frog skin biology
Haslam, I. S., Roubos, E. W., Mangoni, M. L., Yoshizato, K., Vaudry, H., Kloepper, J. E., Pattwell, D. M., MADERSON, P. F. A., & Paus, R. (2013) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12072 · Cited by 82
Coffelt, S. B., Tomchuck, S. L., Zwezdaryk, K. J., Danka, E. S., & Scandurro, A. B. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0326 · Cited by 82
Antimicrobial peptides derived from growth factors
Malmsten, M., Davoudi, M., Walse, B., Rydengård, V., Pasupuleti, M., Mörgelin, M., & Schmidtchen, A. (2007) · Growth Factors · doi:10.1080/08977190701344120 · Cited by 83
Skin Electroporation of a Plasmid Encoding hCAP-18/LL-37 Host Defense Peptide Promotes Wound Healing
Steinstraesser, L., Lam, M. C., Jacobsen, F., Porporato, P. E., Chereddy, K. K., Becerikli, M., Stricker, I., Hancock, R. E. W., Lehnhardt, M., Sonveaux, P., et al. (2014) · Molecular Therapy · doi:10.1038/mt.2013.258 · Cited by 81
Radek, K. A., Elias, P. M., Taupenot, L., Mahata, S. K., O’Connor, D. T., & Gallo, R. L. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.03.009 · Cited by 84
Kozieł, J., Bryzek, D., Sroka, A., Maresz, K., Główczyk, I., Bielecka, E., Kantyka, T., Pyrć, K., Svoboda, P., Pohl, J., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1303062 · Cited by 82
Kindrachuk, J., Jenssen, H., Elliott, M. R., Townsend, R., Nijnik, A., Lee, S. F., Gerdts, V., Babiuk, L. A., Halperin, S. A., & Hancock, R. E. W. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.05.094 · Cited by 80
Expression of antimicrobial peptides in diabetic foot ulcer
Rivas-Santiago, B. T., Trujillo, V., Montoya, A., Gonzalez-Curiel, I. E., Castañeda‐Delgado, J. E., Cardenas, A., Rincon, K., Hernandez, M. L., & Hernández‐Pando, R. (2011) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2011.09.013 · Cited by 79
Archer, N. K., Adappa, N. D., Palmer, J. N., Cohen, N. A., Harro, J., Lee, S. K., Miller, L. S., & Shirtliff, M. E. (2016) · Infection and Immunity · doi:10.1128/iai.00596-16 · Cited by 81
Gaglione, R., Dell’Olmo, E., Bosso, A., Chino, M., Pane, K., Ascione, F., Itri, F., Caserta, S., Amoresano, A., Lombardi, A., et al. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.01.009 · Cited by 77
Yin, J., & Yu, F. X. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-3904 · Cited by 76
Coates, M., Mariottoni, P. R. C. G. B., Corcoran, D. L., Fradin, H., Jaleel, T., Brown, D. A., Brooks, S. R., Murray, J. C. S., Morasso, M. I., & MacLeod, A. S. (2019) · PLoS ONE · doi:10.1371/journal.pone.0216249 · Cited by 77
Architecture of antimicrobial skin defense
Kwiecień, K., Zegar, A., Jung, J., Brzoza, P., Kwitniewski, M., Godlewska, U., Grygier, B., Kwiecińska, P., Morytko, A., & Cichy, J. (2019) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2019.08.001 · Cited by 81
A new role for cathelicidin in ulcerative colitis in mice.
Tai, E. K. K., Wu, W. K. K., Wong, H. P. S., Lam, E. K. Y., Yu, L., & Cho, C. H. (2007) · PubMed · doi:10.3181/00379727-232-2320799 · Cited by 74
McCormick, T. S., & Weinberg, A. (2010) · Periodontology 2000 · doi:10.1111/j.1600-0757.2010.00373.x · Cited by 76
Neutrophil secondary necrosis is induced by LL-37 derived from cathelicidin
Zhang, Z., Cherryholmes, G. A., & Shively, J. E. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0208086 · Cited by 72
Enhanced expression of the antimicrobial peptide LL-37 in lesional skin of adults with atopic eczema
Ballardini, N., Johansson, C., Lilja, G., Lindh, M., Linde, Y., Scheynius, A., & Agerberth, B. (2009) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2009.09095.x · Cited by 73
Vitamin D 3 and the immune system: maintaining the balance in health and disease
Baeke, F., van Etten, E., Overbergh, L., & Mathieu, C. (2007) · Nutrition Research Reviews · doi:10.1017/s0954422407742713 · Cited by 71
Sayama, K., Komatsuzawa, H., Yamasaki, K., Shirakata, Y., Hanakawa, Y., Ouhara, K., Tokumaru, S., Dai, X., Tohyama, M., ten Dijke, P., et al. (2005) · European Journal of Immunology · doi:10.1002/eji.200425827 · Cited by 72
van der Does, A. M., Hensbergen, P. J., Bogaards, S. J. P., Cansoy, M., Deelder, A. M., van Leeuwen, H. C., Drijfhout, J. W., van Dissel, J. T., & Nibbering, P. H. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102777 · Cited by 69
Ruden, S., Rieder, A., Ster, I. C., Schwartz, T., Mikut, R., & Hilpert, K. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02740 · Cited by 68
Wang, Y., Wang, M., Shan, A., & Feng, X. (2020) · Poultry Science · doi:10.1016/j.psj.2020.09.030 · Cited by 68
Metadata
- Authors
- Heilborn, J. D., Nilsson, M. F., Sørensen, O., Ståhle-Bäckdahl, M., Kratz, G., Weber, G., & Borregaard, N.
- Affiliations
- Karolinska Institutet (SE)
- Rigshospitalet (DK)
- Venue
- Journal of Investigative Dermatology
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 120
- Issue
- 3
- Pages
- 379-389
- ISSN
- 0022-202X (ISSN-L)
- OpenAlex
- W2072432297
- Cited by
- 572
- References
- 44
- Citations by year
- 2026: 16 · 2025: 13 · 2024: 15 · 2023: 22 · 2022: 19 · 2021: 28 · 2020: 17 · 2019: 15 · 2018: 21 · 2017: 28 · 2016: 28 · 2015: 25 · 2014: 25 · 2013: 33 · 2012: 39
- FWCI
- 24.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Investigative Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- LL-37, cathelicidin, hCAP18, re-epithelialization, skin wound healing, chronic wounds, chronic ulcers, epithelial cell proliferation, Ki-67, innate immunity, antimicrobial peptides, antibody inhibition
- MeSH terms
- Antibodies, Bacillus megaterium, Chronic Disease, Dose-Response Relationship, Drug, Epithelium, Humans, Immune Sera, Leg Ulcer, Organ Culture Techniques, Skin, Wound Healing, Wounds, Penetrating, Keratinocytes, Ki-67 Antigen, Antimicrobial Cationic Peptides, Cathelicidins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review