The only human cathelicidin antimicrobial peptide, playing key roles in innate immune defense, wound healing, and modulation of inflammatory responses.
Nature medicine|2006|Chromek M et al.|479 citations
The urinary tract functions in close proximity to the outside environment, yet must remain free of microbial colonization to avoid disease. The mechanisms for establishing an antimicrobial barrier in this area are not completely understood. Here, we…
Animal Study
PMID: 16751768
FASEB journal : official publication of the Federation of American Societies for Experimental Biology|2006|Yamasaki K et al.|353 citations
The presence of cathelicidin antimicrobial peptides provides an important mechanism for prevention of infection against a wide variety of microbial pathogens. The activity of cathelicidin is controlled by enzymatic processing of the proform (hCAP18 i…
Animal Study
PMID: 17012259
Peptides|2006|Cirioni O et al.|37 citations
An in vitro antibiotic susceptibility assay for Staphylococcus aureus biofilms developed on 96-well polystyrene tissue culture plates was performed to elucidate the activity of the 27 residues cathelicidin peptide BMAP-28, quinupristin/dalfopristin (…
Animal StudyIn Vitro
PMID: 16621147
The Journal of biological chemistry|2006|Zelezetsky I et al.|87 citations
Cathelicidin genes homologous to the human CAMP gene, coding for the host defense peptide LL-37, have been sequenced and analyzed in 20 primate species, including Great Apes, hylobatidae, cercopithecidae, callithricidae, and cebidae. The region corre…
Animal StudyIn Vitro
PMID: 16720578
Clinical and experimental immunology|2006|McDonald V et al.|37 citations
Accumulating evidence suggests that intestinal epithelial cells (IECs) constitutively express the immunoregulatory cytokine interleukin (IL)-18. IECs also serve as the host cell for the intracellular parasitic protozoan Cryptosporidium parvum. In the…
PMID: 16907926
European journal of gastroenterology & hepatology|2006|Schauber J et al.|131 citations
BACKGROUND: Inflammatory bowel diseases (IBDs) are characterized by a breakdown of colon epithelial barrier function. Antimicrobial peptides like cathelicidins are molecules of the innate immune system located at epithelial surfaces. Cathelicidins in…
In Vitro
PMID: 16702850
Investigative ophthalmology & visual science|2006|Huang L et al.|72 citations
PURPOSE: The goals of this study were to examine the expression of the antimicrobial peptide LL-37 in the corneal epithelium during wound healing and to investigate whether LL-37 stimulates human corneal epithelial cell (HCEC) migration, proliferatio…
PMID: 16723446
The Journal of biological chemistry|2006|Xiao Y et al.|183 citations
Cathelicidins comprise a family of antimicrobial peptides sharing a highly conserved cathelin domain. Here we report that the entire chicken genome encodes three cathelicidins, namely fowlicidin-1 to -3, which are densely clustered within a 7.5-kb di…
PMID: 16326712
Molecular immunology|2006|Kida Y, Shimizu T, Kuwano K|85 citations
The antimicrobial protein cathelicidin is considered to play an important role in the defense mechanisms against bacterial infection. Recent studies show that sodium butyrate induces cathelicidin gene expression in human colonic, gastric and hepatic…
In Vitro
PMID: 16423398
Immunity|2006|Howell M et al.|255 citations
Atopic dermatitis (AD) is associated with eczema vaccinatum (EV), a disseminated viral skin infection that follows inoculation with vaccinia virus (VV). This study examined whether AD skin can control VV replication, and the role of IL-4 and IL-13 in…
Animal Study
PMID: 16546102
Journal of leukocyte biology|2006|Barlow P et al.|124 citations
The human cathelicidin LL-37 is a cationic host defense peptide (antimicrobial peptide) expressed primarily by neutrophils and epithelial cells. This peptide, up-regulated under conditions of inflammation, has immunomodulatory and antimicrobial funct…
PMID: 16793910
Biophysical journal|2006|Neville F et al.|131 citations
Interaction of the human antimicrobial peptide LL-37 with lipid monolayers has been investigated by a range of complementary techniques including pressure-area isotherms, insertion assay, epifluorescence microscopy, and synchrotron x-ray scattering,…
PMID: 16299073
Biochimica et biophysica acta|2006|Yang S et al.|43 citations
The cathelicidin-derived antimicrobial tritrpticin could be classified as either Trp-rich or Pro/Arg-rich peptide. We recently found that the sequence modification of tritrpticin focused on Trp and Pro residues led to considerable change in structure…
PMID: 16859636
The Journal of pharmacology and experimental therapeutics|2006|Yang Y et al.|45 citations
Cathelicidin, a cationic host defense peptide, has been shown to promote cutaneous wound repair and reaches high levels in the gastric mucosa during infection and inflammation. Therefore, we investigated whether this peptide contributes to gastric ul…
Animal Study
PMID: 16670350
Journal of the American Chemical Society|2006|Li X et al.|238 citations
To understand the structure and activity relationship of human LL-37, a series of peptide fragments was designed. The N-terminal fragment, LL-37(1-12), was not active, while the C-terminal fragment, LL-37(13-37), killed Escherichia coli, as well as d…
PMID: 16637646
DNA sequence : the journal of DNA sequencing and mapping|2006|Das H, Sharma B, Kumar A|10 citations
Cathelicidin synthesized by bone marrow cells plays an important role in neutralizing invading pathogens. In the present study, the myeloid cathelicidin cDNA from Bubalus bubalis has been cloned and characterized. RNA from bone marrow of buffalo ribs…
Animal Study
PMID: 17381041
The Journal of antimicrobial chemotherapy|2006|López-García B, Lee P, Gallo R|47 citations
OBJECTIVES: This study was designed to characterize the role of the human cathelicidin LL-37 in fungal skin infections such as dermatophytosis and tinea versicolor. METHODS: The in vitro antimicrobial activity of synthetic antimicrobial peptides incl…
In Vitro
PMID: 16556635
Biology of reproduction|2006|Evans K et al.|168 citations
The active form of vitamin D, 1,25-dihydroxyvitamin D(3) (1,25[OH](2)D(3)) is a potent immunomodulatory seco-steroid. We have demonstrated that several components of vitamin D metabolism and signaling are strongly expressed in human uterine decidua f…
PMID: 16957024
Current topics in microbiology and immunology|2006|Bowdish D, Davidson D, Hancock R|214 citations
Host defence peptides are a conserved component of the innate immune response in all complex life forms. In humans, the major classes of host defence peptides include the alpha- and beta-defensins and the cathelicidin, hCAP-18/LL-37. These peptides a…
Review
PMID: 16909917
The Journal of antimicrobial chemotherapy|2006|Benincasa M et al.|111 citations
OBJECTIVES: To investigate the in vitro antifungal activity of the structurally different cathelicidin peptides SMAP-29, BMAP-27, BMAP-28, protegrin-1 (PG-1) and indolicidin. METHODS: The in vitro antifungal and fungicidal activities of these antimic…
In Vitro
PMID: 17023499