FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

Agerberth, Birgitta; Gunne, Hans; Odeberg, Jacob; Kogner, Per; Boman, Hans G.; Guðmundsson, Guðmundur H.

doi:10.1073/pnas.92.1.195

Cited by 458 publications

(386 citation statements)

References 31 publications

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“…To date, cathelicidins have only been described in mammals, including humans, monkeys, horses, cattle, sheep, goats, pigs, rabbits, mice and guinea pig (for review, see Ramanathan et al 2002). Each species has variable numbers of cathelicidin genes; artiodactyls in particular have high copy numbers (Scocchi et al 1997), whereas humans and mice have only one gene copy each (Agerberth et al 1995;Cowland et al 1995;Gallo et al 1997;Larrick et al 1995). Neutrophils are a particularly rich source of cathelicidins in a variety of species.…”

Section: Introductionmentioning

confidence: 99%

“…Neutrophils are a particularly rich source of cathelicidins in a variety of species. In humans, cathelicidins have also been found to be expressed in several other tissues, including the testis (Agerberth et al 1995;Malm et al 2000), squamous epithelia (Frohm Nilsson et al 1999;Nizet et al 2001), airway epithelia (Bals et al 1998), sweat glands (Murakami et al 2002b), salivary glands (Murakami et al 2002a) and colon (Hase et al 2002). Cathelicidins have a wide spectrum of antimicrobial activity and have been shown to be active against Gram-negative and Grampositive bacteria (Travis et al 2000), fungi (Shin et al 2000) and enveloped viruses (Tamamura et al 1995).…”

Section: Introductionmentioning

confidence: 99%

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Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken

et al. 2004

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Antimicrobial peptides (AMPs) are essential components of innate immunity in a range of species fromDrosophila to humans and are generally thought to act by disrupting the membrane integrity of microbes. In order to discover novel AMPs in the chicken, we have implemented a bioinformatic approach that involves the clustering of more than 420,000 chicken expressed sequence tags (ESTs). Similarity searching of proteinspredicted to be encoded by these EST clusters-for homology to known AMPs has resulted in the in silico identification of full-length sequences for seven novel gallinacins (Gal-4 to Gal-10), a novel cathelicidin and a novel liver-expressed antimicrobial peptide 2 (LEAP-2) in the chicken. Differential gene expression of these novel genes has been demonstrated across a panel of chicken tissues. An evolutionary analysis of the gallinacin family has detected sites-primarily in the mature AMP-that are under positive selection in these molecules. The functional implications of these results are discussed.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken

et al. 2004

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“…in several peptides: polypeptides Bac 5 and Bac 7 [9,10], prophenin [11] and PR-39 [12] belonging to the family of prolineand arginine-rich antibiotics, associated with the large granules of bovine neutrophils; in the cysteine-rich cyclic dodecapeptide [13] and protegrins [14]; in polypeptides CAP 18 [15] and p15 with two isoforms [16] from rabbit neutrophils; and in human polypeptide FALL-39 [17].…”

Section: Introductionmentioning

confidence: 99%

A novel murine cathelin‐like protein expressed in bone marrow

et al. 1996

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A novel cDNA encoding a putative secreted protein was isolated from murine bone marrow. The encoded protein named MCLP (.m.urine cathelin-_like protein) was found to be highly homologous to the pig cathelin, and to four neutrophil antimicrobial polypeptides: CAP 18, indolicidin, Bac 5 and FALL-39. Secondary structure prediction studies identified a highly cationic region in the C-terminal part of prepro-MCLP with a tendency to adopt an amphipathic a-helical conformation, as observed in many antimicrobial peptides. However, no antibacterial activity was observed with the synthetic peptide corresponding to this region of MCLP.

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“…Human cathelicidin antimicrobial protein hCAP18, the only known cathelicidin in humans, consists of a conserved cathelin domain and a variable C-terminus, called LL-37. 1,2 Extracellular proteolytic processing of the holoprotein releases the LL-37 peptide, which has broad antimicrobial activity 1,3 as well as effects on host cells mediated by the G-protein-coupled receptor, formyl peptide receptor-like 1 (FPRL1). 4,5 hCAP18 is present in leucocytes 6 and is expressed in skin and other epithelia, where it is upregulated in association with inflammation 7,8 and injury, 9,10 consistent with a role in innate barrier protection.…”

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confidence: 99%

Antimicrobial protein hCAP18/LL‐37 is highly expressed in breast cancer and is a putative growth factor for epithelial cells

Heilborn

Nilsson

Jimenez

et al. 2005

Intl Journal of Cancer

112

110

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Human cathelicidin antimicrobial protein hCAP18/LL-37 is an effector molecule of the nonspecific innate immune system. hCAP18/LL-37 is present in leukocytes and is expressed in skin and other epithelia, where it is upregulated in association with inflammation and injury. In addition, antimicrobial proteins including cathelicidins have been proposed to play a role in the nonspecific defense against tumors. To assess its potential role in tumor host defense, we investigated the expression of hCAP18/ LL-37 in a series of breast carcinomas. Unexpectedly, we found that hCAP18/LL-37 was strongly expressed in the tumor cells and not in the adjacent stroma. To test the hypothesis that hCAP18/ LL-37 may provide a growth advantage for the tumor cells, we treated human epithelial cell lines with synthetic biologically active LL-37 peptide and found a significant increase in cell proliferation. In addition, transgenic expression of hCAP18 in 2 different human epithelial cell lines resulted in increased proliferation of both cell types. These findings do not support the hypothesis that LL-37 has an antitumor effect, but rather suggest that hCAP18/LL-37 may promote tumor cell growth in breast cancer.

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FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

Cited by 458 publications

References 31 publications

Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken

Bioinformatic discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken

A novel murine cathelin‐like protein expressed in bone marrow

Antimicrobial protein hCAP18/LL‐37 is highly expressed in breast cancer and is a putative growth factor for epithelial cells

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