Literature DB >> 7628604

The structure of porcine protegrin genes.

C Zhao1, T Ganz, R I Lehrer.   

Abstract

We cloned the genes of three protegrins, a family of cathelin-associated antimicrobial peptides originally isolated from porcine leukocytes. Each gene comprised 4 exons and 3 introns, wherein Exon I encoded the signal sequence and the first 37 amino acids of cathelin, Exons II and III contained 36 and 24 additional cathelin residues and Exon IV contained the final two cathelin residues followed by the protegrin sequence. This quadripartite gene structure helps explain how structurally diverse antimicrobial peptides can be expressed on common, cathelin-containing precursors. Southern blot probed with an oligonucleotide specific for protegrin genes suggested that several identical or nearly identical protegrin genes were densely clustered in the pig chromosome.

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Year:  1995        PMID: 7628604     DOI: 10.1016/0014-5793(95)00633-k

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  16 in total

1.  Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity.

Authors:  D A Steinberg; M A Hurst; C A Fujii; A H Kung; J F Ho; F C Cheng; D J Loury; J C Fiddes
Journal:  Antimicrob Agents Chemother       Date:  1997-08       Impact factor: 5.191

2.  Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and atlantic salmon (Salmo salar).

Authors:  Chin-I Chang; Yong-An Zhang; Jun Zou; Pin Nie; Christopher J Secombes
Journal:  Antimicrob Agents Chemother       Date:  2006-01       Impact factor: 5.191

3.  Regulation of cathelicidin gene expression: induction by lipopolysaccharide, interleukin-6, retinoic acid, and Salmonella enterica serovar typhimurium infection.

Authors:  H Wu; G Zhang; J E Minton; C R Ross; F Blecha
Journal:  Infect Immun       Date:  2000-10       Impact factor: 3.441

4.  Cathelicidin gene expression in porcine tissues: roles in ontogeny and tissue specificity.

Authors:  H Wu; G Zhang; C R Ross; F Blecha
Journal:  Infect Immun       Date:  1999-01       Impact factor: 3.441

5.  Haemophilus ducreyi is susceptible to protegrin.

Authors:  K Fortney; P A Totten; R I Lehrer; S M Spinola
Journal:  Antimicrob Agents Chemother       Date:  1998-10       Impact factor: 5.191

6.  Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins.

Authors:  A Panyutich; J Shi; P L Boutz; C Zhao; T Ganz
Journal:  Infect Immun       Date:  1997-03       Impact factor: 3.441

7.  Activity of protegrins against yeast-phase Candida albicans.

Authors:  Y Cho; J S Turner; N N Dinh; R I Lehrer
Journal:  Infect Immun       Date:  1998-06       Impact factor: 3.441

8.  Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.

Authors:  K S Usachev; S V Efimov; O A Kolosova; E A Klochkova; A V Aganov; V V Klochkov
Journal:  J Biomol NMR       Date:  2015-03-19       Impact factor: 2.835

9.  High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles.

Authors:  K S Usachev; S V Efimov; O A Kolosova; A V Filippov; V V Klochkov
Journal:  J Biomol NMR       Date:  2014-11-28       Impact factor: 2.835

10.  Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils.

Authors:  J Turner; Y Cho; N N Dinh; A J Waring; R I Lehrer
Journal:  Antimicrob Agents Chemother       Date:  1998-09       Impact factor: 5.191

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