Cathelicidins

"Cathelicidins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Antimicrobial cationic peptides with a highly conserved amino terminal cathelin-like domain and a more variable carboxy terminal domain. They are initially synthesized as preproproteins and then cleaved. They are expressed in many tissues of humans and localized to EPITHELIAL CELLS. They kill nonviral pathogens by forming pores in membranes.

Descriptor ID	D054804
MeSH Number(s)	D12.644.050.099 D12.776.543.695.054.099
Concept/Terms	Cathelicidins Cathelicidins

Below are MeSH descriptors whose meaning is more general than "Cathelicidins".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Peptides [D12.644]
Antimicrobial Cationic Peptides [D12.644.050]
Cathelicidins [D12.644.050.099]
Proteins [D12.776]
Membrane Proteins [D12.776.543]
Pore Forming Cytotoxic Proteins [D12.776.543.695]
Antimicrobial Cationic Peptides [D12.776.543.695.054]
Cathelicidins [D12.776.543.695.054.099]

Below are MeSH descriptors whose meaning is related to "Cathelicidins".

Below are MeSH descriptors whose meaning is more specific than "Cathelicidins".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Cathelicidins" by people in this website by year, and whether "Cathelicidins" was a major or minor topic of these publications.

Bar chart showing 4 publications over 4 distinct years, with a maximum of 1 publications in 2017 and 2018 and 2020 and 2025

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2017	0	1	1
2018	0	1	1
2020	1	0	1
2025	0	1	1

Below are the most recent publications written about "Cathelicidins" by people in Profiles.

Stocks B, Quesada JP, Mozzicato AM, Jacob C, Jensen S, MacGregor KA, Bangsbo J, Zierath JR, Hostrup M, Deshmukh AS. Temporal dynamics of the interstitial fluid proteome in human skeletal muscle following exhaustive exercise. Sci Adv. 2025 Jan 31; 11(5):eadp8608.

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Gulati S, Schoenhofen IC, Lindhout-Djukic T, Lewis LA, Moustafa IY, Saha S, Zheng B, Nowak N, Rice PA, Varki A, Ram S. Efficacy of Antigonococcal CMP-Nonulosonate Therapeutics Require Cathelicidins. J Infect Dis. 2020 10 13; 222(10):1641-1650.

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Wong A, Bryzek D, Dobosz E, Scavenius C, Svoboda P, Rapala-Kozik M, Lesner A, Frydrych I, Enghild J, Mydel P, Pohl J, Thompson PR, Potempa J, Koziel J. A Novel Biological Role for Peptidyl-Arginine Deiminases: Citrullination of Cathelicidin LL-37 Controls the Immunostimulatory Potential of Cell-Free DNA. J Immunol. 2018 04 01; 200(7):2327-2340.

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Kumar NP, Moideen K, Viswanathan V, Sivakumar S, Menon PA, Kornfeld H, Babu S. Heightened circulating levels of antimicrobial peptides in tuberculosis-Diabetes co-morbidity and reversal upon treatment. PLoS One. 2017; 12(9):e0184753.

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Zhang L, Wu WK, Gallo RL, Fang EF, Hu W, Ling TK, Shen J, Chan RL, Lu L, Luo XM, Li MX, Chan KM, Yu J, Wong VW, Ng SC, Wong SH, Chan FK, Sung JJ, Chan MT, Cho CH. Critical Role of Antimicrobial Peptide Cathelicidin for Controlling Helicobacter pylori Survival and Infection. J Immunol. 2016 Feb 15; 196(4):1799-809.

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Kishibe M, Griffin TM, Radek KA. Keratinocyte nicotinic acetylcholine receptor activation modulates early TLR2-mediated wound healing responses. Int Immunopharmacol. 2015 Nov; 29(1):63-70.

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Ren SX, Cheng AS, To KF, Tong JH, Li MS, Shen J, 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 Dec 15; 72(24):6512-23.

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