| Identification | Back Directory | [Name]
PR 39 (PORCINE) | [CAS]
139637-11-9 | [Synonyms]
PR 39
PR 39 (PORCINE)
PR-39, PORCINE, SYNTHETIC
M.W. 4719.64 C229H346N70O40
L-Prolinamide, L-arginyl-L-arginyl-L-prolyl-L-arginyl-L-prolyl-L-prolyl-L-tyrosyl-L-leucyl-L-prolyl-L-arginyl-L-prolyl-L-arginyl-L-prolyl-L-prolyl-L-prolyl-L-phenylalanyl-L-phenylalanyl-L-prolyl-L-prolyl-L-arginyl-L-leucyl-L-prolyl-L-prolyl-L-arginyl-L-isoleucyl-L-prolyl-L-prolylglycyl-L-phenylalanyl-L-prolyl-L-prolyl-L-arginyl-L-phenylalanyl-L-prolyl-L-prolyl-L-arginyl-L-phenylalanyl- | [Molecular Formula]
C229H345N69O41 | [MDL Number]
MFCD03458161 | [MOL File]
139637-11-9.mol | [Molecular Weight]
4720.63 |
| Hazard Information | Back Directory | [Uses]
PR-39, a natural proline- and arginine-rich antibacterial peptide, is a noncompetitive, reversible and allosteric proteasome inhibitor. PR-39 reversibly binds to the α7 subunit of the proteasome and blocks degradation of NF-κB inhibitor IκBα by the ubiquitin-proteasome pathway. PR-39 stimulates angiogenesis, inhibits inflammatory responses and significant reduces myocardial infarct size in mice[1][2]. | [Definition]
ChEBI: PR-39 is a 39 amino acid porcine cathelicidin that is rich in proline and arginine residues. It plays a pivotal role in the innate immune defence of the pig against infections and exhibits antimicrobial and immunomodulatory activities. It has a role as an antibacterial agent, an apoptosis inhibitor, an anti-inflammatory agent, a mammalian metabolite, an antifungal agent and an immunomodulator. | [in vivo]
PR-39 (10 mg/kg, intravenously; 1 hour before Caerulein of 50μg/kg, ip) blocks IκBα degradation and NF-κB-dependent transcription in the mouse pancreas after induction of acute pancreatitis[2].
PR-39 (1 μg/kg/day; 7-day intraperitoneal infusion) demonstrates significantly small infarct in C57BL/6 mice[2].
| [References]
[1] Maria Gaczynska, et al. Proline- and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry. 2003 Jul 29;42(29):8663-70. DOI:10.1021/bi034784f
[2] Y Gao, et al. Inhibition of ubiquitin-proteasome pathway-mediated I kappa B alpha degradation by a naturally occurring antibacterial peptide. J Clin Invest. 2000 Aug;106(3):439-48. DOI:10.1172/JCI9826 |
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