Disease relevance of CATHL1

• The MICs of all cathelicidin-derived peptides tested for Borrelia strains ranged between 307 and 449.4 mg/L [1].
• Comparative in vitro activity of five cathelicidin-derived synthetic peptides against Leptospira, Borrelia and Treponema pallidum [1].
• The cathelicidin displayed strong activity against Gram-negative bacteria, but lesser activity against Gram-positive bacteria and yeast, whilst the beta-defensin showed good activity against all three test organisms [2].
• Bactenecin interacted well with the outer membrane and its higher affinity for E. coli UB1005 lipopolysaccharide and improved ability to permeabilize the outer membrane seemed to account for its better antimicrobial activity against Gram-negative bacteria [3].
• Bactenecin was more active against the Gram-negative wild type bacteria Escherichia coli, Pseudomonas aeruginosa, and Salmonella typhimurium than its linear derivative and reduced form, while all three peptides were equally active against the outer membrane barrier-defective mutants of the first two bacteria [3].

High impact information on CATHL1

• To test this, we investigated the effects of the addition of cathelicidins by combining synthetic cathelicidin peptides in vitro, by producing human keratinocytes that overexpress cathelicidins in culture, or by producing transgenic mice that constitutively overexpress cathelicidins in vivo [4].
• Bactenecin, a 12-amino acid cationic antimicrobial peptide from bovine neutrophils, has two cysteine residues, which form one disulfide bond, making it a cyclic molecule [3].
• Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane [3].
• It was shown that the linear derivative and reduced form were able to dissipate the membrane potential at much lower concentrations than bactenecin despite the similar minimal inhibitory concentrations of all three against this barrier-defective mutant [3].
• The peptide, named bactenecin, has the amino acid sequence, Arg-Leu-Cys-Arg-Ile-Val-Val-Ile-Arg-Val-Cys-Arg, maintained in a cyclic structure by a disulfide bond between the two cysteine residues [5].

Biological context of CATHL1

• Thus, rtCATH_1 represents a novel antimicrobial peptide gene belonging to the cathelicidin family and may play an important role in the innate immunity of rainbow trout [6].
• Apoptosis of airway epithelial cells: human serum sensitive induction by the cathelicidin LL-37 [7].
• The rtCATH_1 gene comprises four exons, as seen in all known mammalian cathelicidin genes, and several transcription factor binding sites known to be of relevance to host defenses were identified in the 5' flanking region [6].
• We mapped the two-exon beta-defensin genes to sheep chromosome 26 and the four-exon cathelicidin genes to sheep chromosome 19 using sheep-hamster somatic cell hybrids in conjunction with flow-sorted sheep chromosomes [8].
• Acetylation and amidation of the amino- and carboxy-termini of bactenecin do not change its potency, while replacement of its two cysteine residues with serine decreases the potency [9].

Anatomical context of CATHL1

• Bac-X had similar characteristics to Bac-5, a previously characterised bactenecin of bovine neutrophil granules, with respect to its proline, arginine and hydrophobic amino acid content, molecular mass and antibacterial specificity [10].
• Antibacterial activity of bactenecin 5 fragments and their interaction with phospholipid membranes [11].

Associations of CATHL1 with chemical compounds

• Structure and property of model peptides of proline/arginine-rich region in bactenecin 5 [12].
• Delineation of an active fragment and poly(L-proline) II conformation for candidacidal activity of bactenecin 5 [13].
• This study examined the effect of trophic factor supplementation [TFS; bovine neutrophil peptide-1 (bactenecin), 1 mg/L; substance P, 2.5 mg/L; nerve growth factor, 20 microg/L; epidermal growth factor, 10 microg/L; insulin-like growth factor-1, 10 microg/L] during cold storage with UW lactobionate solution [14].

Other interactions of CATHL1

• OBJECTIVE: The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of five different cathelicidin-derived synthetic peptides (SMAP-29, LL-37, PG-1, CRAMP and BMAP-28) for Leptospira interrogans, Borrelia spp. and Treponema pallidum subsp. pallidum were investigated in vitro [1].
• Bac4 is a bovine cathelicidin gene contiguous to another member of this family named Bac7 [15].
• The cathelicidin peptides, human LL-37 and bovine myeloid antimicrobial peptide-27 (BMAP-27), are homologs, yet they have diverged notably in terms of sequence similarity [16].
• A putative antimicrobial peptide of 34 residues was recently deduced from a bovine cathelicidin gene sequence and named BMAP-34 [17].

Analytical, diagnostic and therapeutic context of CATHL1

• Circular dichroism spectroscopy showed that bactenecin existed as a type I beta-turn structure regardless of its environment, while the reduced form and linear bactenecin adopted different conformations according to the lipophilicity of the environment [3].
• Partial N-terminal sequence analysis further shows that it is proline rich and shares more than 60% identity in a 28-amino-acid overlap with the mature form of bactenecin 7, an antimicrobial peptide from bovine neutrophils which belongs to the cathelicidin family of mammalian peptide antibiotics [18].
• Six antimicrobial peptide genes of the cathelicidin family map to bovine chromosome 22q24 by fluorescence in situ hybridization [19].

References