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Gene Review

PR39  -  peptide antibiotic PR39

Sus scrofa

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Disease relevance of PR39


High impact information on PR39

  • Here we show that a macrophage-derived peptide, PR39, inhibited the ubiquitin-proteasome-dependent degradation of hypoxia-inducible factor-1alpha protein, resulting in accelerated formation of vascular structures in vitro and increased myocardial vasculature in mice [6].
  • For the latter, coronary flow studies demonstrated that PR39-induced angiogenesis resulted in the production of functional blood vessels [6].
  • Lentiviral delivery of PR-39 enhanced killing of GAS by human keratinocytes [7].
  • PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox [8].
  • We show here that an endogenous proline-arginine (PR)-rich antibacterial peptide, PR-39, inhibits NADPH oxidase activity by blocking assembly of this enzyme through interactions with Src homology 3 domains of a cytosolic component [8].

Biological context of PR39


Anatomical context of PR39

  • In this study, we investigated the efficacy and mechanism of PR39, a gene capable of activating VEGF and fibroblast growth factor (FGF)-2-dependent pathways [1].
  • PR39 is an angiogenic peptide that improves perfusion and function of ischemic myocardium, at least in part, through collateral formation [1].
  • PR-39 was originally isolated from pig small intestine, but subsequent cDNA cloning showed that the gene is expressed in the bone marrow [2].
  • Cecropin P1 and PR-39 are two antibacterial peptides isolated from the upper part of the small intestine of the pig [3].
  • Peripheral blood neutrophils from young pigs expressed PR-39 and protegrin mRNA, which were not detectable at 42 days of age [9].

Associations of PR39 with chemical compounds

  • Its effects involve both a polybasic amino-terminal segment and a proline-rich core region of PR-39 that binds to the p47phox Src homology 3 domains and, thereby, inhibits interaction with the small subunit of cytochrome b558, p22phox [8].
  • The proline-arginine (PR) -rich antibacterial peptide, PR-39, kills bacteria by a non-pore-forming mechanism [5].
  • We report on the synthesis of a functional antibacterial domain of PR-39, the first 26 amino acid residues of the NH2 terminus [4].
  • Exon IV specified the final few cathelin residues, including its conserved C-terminal valine, followed by the mature PR-39 peptide or a PF-2 precursor [10].
  • PR-39 induced a calcein release from large unilamellar vesicles, which is dependent upon the peptide concentration and upon the presence of negatively charged lipid (glycerophosphoglycerol) in the membrane [11].

Regulatory relationships of PR39

  • In addition, PR39 also stimulates expression of the FGF receptors (FGFR)-1 and syndecan-4 [1].

Other interactions of PR39

  • The dual mechanism, i.e., stimulation of HIF-1alpha and FGF receptor expression, likely accounts for the functional benefits of PR39 [1].
  • In 10 mM sodium phosphate with 125 mM NaCl, the combinations of sublethal concentrations of PBD-1 and the porcine neutrophil peptide PG-3, PR-39, or PR-26 showed synergistic activity against E. coli or the multidrug-resistant S. typhimurium DT104 [12].
  • Chemoattractant properties of PR-39, a neutrophil antibacterial peptide [5].
  • Spleen antibacterial peptides: high levels of PR-39 and presence of two forms of NK-lysin [13].

Analytical, diagnostic and therapeutic context of PR39


  1. Adenoviral PR39 improves blood flow and myocardial function in a pig model of chronic myocardial ischemia by enhancing collateral formation. Post, M.J., Sato, K., Murakami, M., Bao, J., Tirziu, D., Pearlman, J.D., Simons, M. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2006) [Pubmed]
  2. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Gudmundsson, G.H., Magnusson, K.P., Chowdhary, B.P., Johansson, M., Andersson, L., Boman, H.G. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  3. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Boman, H.G., Agerberth, B., Boman, A. Infect. Immun. (1993) [Pubmed]
  4. Antibacterial activity of a synthetic peptide (PR-26) derived from PR-39, a proline-arginine-rich neutrophil antimicrobial peptide. Shi, J., Ross, C.R., Chengappa, M.M., Sylte, M.J., McVey, D.S., Blecha, F. Antimicrob. Agents Chemother. (1996) [Pubmed]
  5. Chemoattractant properties of PR-39, a neutrophil antibacterial peptide. Huang, H.J., Ross, C.R., Blecha, F. J. Leukoc. Biol. (1997) [Pubmed]
  6. PR39, a peptide regulator of angiogenesis. Li, J., Post, M., Volk, R., Gao, Y., Li, M., Metais, C., Sato, K., Tsai, J., Aird, W., Rosenberg, R.D., Hampton, T.G., Sellke, F., Carmeliet, P., Simons, M. Nat. Med. (2000) [Pubmed]
  7. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Lee, P.H., Ohtake, T., Zaiou, M., Murakami, M., Rudisill, J.A., Lin, K.H., Gallo, R.L. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  8. PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox. Shi, J., Ross, C.R., Leto, T.L., Blecha, F. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  9. Cathelicidin gene expression in porcine tissues: roles in ontogeny and tissue specificity. Wu, H., Zhang, G., Ross, C.R., Blecha, F. Infect. Immun. (1999) [Pubmed]
  10. Structures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39. Zhao, C., Ganz, T., Lehrer, R.I. FEBS Lett. (1995) [Pubmed]
  11. Secondary structure and membrane interaction of PR-39, a Pro+Arg-rich antibacterial peptide. Cabiaux, V., Agerberth, B., Johansson, J., Homblé, F., Goormaghtigh, E., Ruysschaert, J.M. Eur. J. Biochem. (1994) [Pubmed]
  12. Porcine epithelial beta-defensin 1 is expressed in the dorsal tongue at antimicrobial concentrations. Shi, J., Zhang, G., Wu, H., Ross, C., Blecha, F., Ganz, T. Infect. Immun. (1999) [Pubmed]
  13. Spleen antibacterial peptides: high levels of PR-39 and presence of two forms of NK-lysin. Bonetto, V., Andersson, M., Bergman, T., Sillard, R., Norberg, A., Mutt, V., Jornvall, H. Cell. Mol. Life Sci. (1999) [Pubmed]
  14. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H.G., Gudmundsson, G.H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  15. Salmonella infection increases porcine antibacterial peptide concentrations in serum. Zhang, G., Ross, C.R., Dritz, S.S., Nietfeld, J.C., Blecha, F. Clin. Diagn. Lab. Immunol. (1997) [Pubmed]
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