A novel murine cathelin‐like protein expressed in bone marrow

Popsueva, Anna; Zinovjeva, Marina V.; Visser, J. W. M.; Zijlmans, J. M. J. M.; Fibbe, Willem E.; Belyavsky, A. V.

doi:10.1016/0014-5793(96)00692-8

Cited by 37 publications

(25 citation statements)

References 30 publications

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“…The deduced pre-propeptides of uterus cathelicidin cDNA had conserved N-terminal and diverse heterogeneous C-terminal was in agreement with other cathelicidin congeners (Popsueva et al, 1996;Wu et al, 1999). Alanine at 29 was conserved in most of the congeners and it might be the probable site of elastase mediated proteolytic cleavage to separate the signal sequence from the prosequence.…”

Section: Discussionsupporting

confidence: 72%

Characterization of cathelicidin gene from buffalo (Bubalus bubalis)

Kalita¹

2015

Afr. J. Biotechnol.

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Wide spread and indiscriminate use of antibiotics is accompanied by the emergence of microorganism that are resistant to these agents. Therefore, new approaches are required to address the problem of antimicrobial resistance. Epithelial linings of living organisms are the source of various antimicrobial peptides. Keeping this in view, the present experiment was designed to characterize one of the important natural antimicrobial peptide gene, that is, cathelicidin gene from the buffalo (Bubalus bubalis) uterine epithelium and explored its potency for use as template for synthesis of novel antimicrobial agents. Total RNA was isolated from epithelial layer of buffalo uterus and reverse transcribed using designed primers. The amplified PCR product was purified and cloned. Positive clone was sequenced and result was analysed using laser gene software (DNA Star, USA). The cDNA of uterus cathelicidin had 516 bases with complete ORF from 6-452 bp. The predicted pre-propeptide comprised of 148 amino acids. Mature active peptide had 18 amino acids and had five each of arginine and tryptophan and four proline residues. From this study, it can be concluded that the buffalo (Bubalus bubalis) uterus expressed a potent antimicrobial peptide and amino acid sequence of mature peptide can be used as template for synthesis of novel antimicrobial agents.

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Section: Discussionsupporting

confidence: 72%

Characterization of cathelicidin gene from buffalo (Bubalus bubalis)

Kalita¹

2015

Afr. J. Biotechnol.

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“…In mice 44,45 and rabbits, 46 the putative cleavage sites of the cathelicidins do not resemble those in human, porcine, or bovine cathelicidins. The specific proteases responsible for cleavage of these cathelicidins remain to be characterized.…”

Section: Discussionmentioning

confidence: 88%

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Sørensen

Follin

Johnsen

et al. 2001

Blood

778

626

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Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. The known biologic functions reside in the C-terminus, which must be cleaved from the holoprotein to become active. Bovine and porcine cathelicidins are cleaved by elastase from the azurophil granules to yield the active antimicrobial peptides. The aim of this study was to identify the physiological setting for cleavage of the only human cathelicidin, hCAP-18, to liberate the antibacterial and cytotoxic peptide LL-37 and to identify the protease responsible for this cleavage. Immunoelectron microscopy demonstrated that both hCAP-18 and azurophil granule proteins were present in the phagolysosome. Immunoblotting revealed no detectable cleavage of hCAP-18 in cells after phagocytosis. In contrast, hCAP-18 was cleaved to generate LL-37 in exocytosed material. Of the 3 known serine proteases from azurophil granules, proteinase 3 was solely responsible for cleavage of hCAP-18 after exocytosis. This is the first detailed study describing the generation of a human antimicrobial peptide from a promicrobicidal protein, and it demonstrates that the generation of active antimicrobial peptides from common proproteins occurs differently in related species. (Blood. 2001; 97:3951-3959)

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“…Antimicrobial peptides encoded by five distinct mammalian cathelicidins genes were synthesized. The peptide sequences are shown in Table 1 and include the CAP18 (20), mCRAMP (12,30), SMAP34 (16), SMAP29 (2,25), rCRAMP, and FALL39/LL37 (1,19) sequences. The rat sequence (rCRAMP) was identified by a homology search with the mouse protein (mCRAMP) sequence and corresponded to GenBank accession no.…”

Section: Resultsmentioning

confidence: 99%

“…The first cathelicidin precursor to be described was rabbit CAP18 (20), and its mature peptide was shown to have broad-spectrum bactericidal activity (19). Homologs of CAP18 have since been identified in other species including humans (FALL39/LL37) (1,19), mice (mCRAMP) (12,30), rats (rCRAMP), and sheep (SMAP29 and SMAP34) (2,16,25,34). Circular dichroism (CD) measurements indicate that these linear peptides adopt ␣-helical structure in some solvents (1,8,12,17,36).…”

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confidence: 99%

Bactericidal Activity of Mammalian Cathelicidin-Derived Peptides

Travis¹,

Anderson²,

Forsyth³

et al. 2000

Infect Immun

336

299

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Endogenous antimicrobial peptides of the cathelicidin family contribute to innate immunity. The emergence of widespread antibiotic resistance in many commonly encountered bacteria requires the search for new bactericidal agents with therapeutic potential. Solid-phase synthesis was employed to prepare linear antimicrobial peptides found in cathelicidins of five mammals: human (FALL39/LL37), rabbit (CAP18), mouse (mCRAMP), rat (rCRAMP), and sheep (SMAP29 and SMAP34). These peptides were tested at ionic strengths of 25 and 175 mM against Pseudomonas aeruginosa, Escherichia coli, Staphylococcus aureus, and methicillin-resistant Staphylococcus aureus. Each peptide manifested activity against P. aeruginosa irrespective of the NaCl concentration. CAP18 and SMAP29 were the most effective peptides of the group against all test organisms under both lowand high-salt conditions. Select peptides of 15 to 21 residues, modeled on CAP18 (37 residues), retained activity against the gram-negative bacteria and methicillin-sensitive S. aureus, although the bactericidal activity was reduced compared to that of the parent peptide. In accordance with the behavior of the parent molecule, the truncated peptides adopted an ␣-helical structure in the presence of trifluoroethanol or lipopolysaccharide. The relationship between the bactericidal activity and several physiochemical properties of the cathelicidins was examined. The activities of the full-length peptides correlated positively with a predicted gradient of hydrophobicity along the peptide backbone and with net positive charge; they correlated inversely with relative abundance of anionic residues. The salt-resistant, antimicrobial properties of CAP18 and SMAP29 suggest that these peptides or congeneric structures have potential for the treatment of bacterial infections in normal and immunocompromised persons and individuals with cystic fibrosis.The rapidly expanding prevalence of bacterial strains resistant to conventional antibiotics has prompted a search for new therapeutic agents, including various antimicrobial peptides of animal origin (15). Two broad classes of mammalian antibacterial peptides have been especially well studied: the cysteinerich ␣-and ␤-defensins and various cathelicidins (6,13,22,26,27,41,42). Both classes are produced as precursors that require proteolytic processing to generate the mature antimicrobial peptide. Cathelicidins contain an N-terminal domain called cathelin, for which no function has yet been ascribed, and a C-terminal domain that comprises an antimicrobial peptide (reviewed in references 41 and 42). While the cathelin domains are highly conserved across species, the C-terminal antimicrobial domains are structurally diverse. The first cathelicidin precursor to be described was rabbit CAP18 (20), and its mature peptide was shown to have broad-spectrum bactericidal activity (19). Homologs of CAP18 have since been identified in other species including humans (FALL39/LL37) (1, 19), mice (mCRAMP) (12, 30), rats (rCRAMP), and sheep (SMAP29 and SMAP34...

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A novel murine cathelin‐like protein expressed in bone marrow

Cited by 37 publications

References 30 publications

Characterization of cathelicidin gene from buffalo (Bubalus bubalis)

Characterization of cathelicidin gene from buffalo (Bubalus bubalis)

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Bactericidal Activity of Mammalian Cathelicidin-Derived Peptides

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