Beta-Endorphin 1-31 Biotransformation and cAMP Modulation in Inflammation

Asvadi, Naghmeh Hajarol, Morgan, Michael, Herath, Herath M., Hewavitharana, Amitha K., Shaw, P. Nicholas and Cabot, Peter J. (2014) Beta-Endorphin 1-31 Biotransformation and cAMP Modulation in Inflammation. PLoS One, 9 3: e90380.1-e90380.11. doi:10.1371/journal.pone.0090380

Author Asvadi, Naghmeh Hajarol
Morgan, Michael
Herath, Herath M.
Hewavitharana, Amitha K.
Shaw, P. Nicholas
Cabot, Peter J.
Title Beta-Endorphin 1-31 Biotransformation and cAMP Modulation in Inflammation
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2014-01-01
Year available 2014
Sub-type Article (original research)
DOI 10.1371/journal.pone.0090380
Open Access Status DOI
Volume 9
Issue 3
Start page e90380.1
End page e90380.11
Total pages 11
Place of publication San Francisco, CA, United States
Publisher Public Library of Science
Language eng
Subject 1300 Biochemistry, Genetics and Molecular Biology
1100 Agricultural and Biological Sciences
Abstract A large body of evidence now exists for the immune cell expression, production, and the release of beta-endorphin (BE 1-31) within inflamed tissue. The inflammatory milieu is characterised by increased acidity, temperature and metabolic activity. Within these harsh conditions BE 1-31 is even more susceptible to increased enzymatic degradation over that of plasma or other non-injured tissue. To elucidate the biotransformation pathways of BE 1-31 and provide an insight to the impact of inflamed tissue environments, BE 1-31 and three of its major N-terminal fragments (BE 1-11, BE 1-13 and BE 1-17) were incubated in inflamed tissue homogenates at pH 5.5 for 2 hrs. In addition, the potency of BE 1-31 and five main N - terminal fragments (BE 1-9, BE 1-11, BE 1-13, BE 1-17, BE 1-20) was assessed at mu-opioid receptors (MOR), delta-opioid receptors (DOR), and kappa-opioid receptors (KOR). Opioid receptor potency was investigated by examining the modulation of forskolin induced cAMP accumulation. The majority of the N-terminal fragment of BE 1-31 had similar efficacy to BE 1-31 at MOR. The shortest of the major N-terminal fragments (BE 1-9), had partial agonist activity at MOR but possessed the highest potency of all tested peptides at DOR. There was limited effect for BE 1-31 and the biotransformed peptides at KOR. Major N-terminal fragments produced within inflamed tissue have increased presence within inflamed tissue over that of the parent molecule BE 1-31 and may therefore contribute to BE 1-31 efficacy within disease states that involve inflammation.
Keyword Multidisciplinary Sciences
Science & Technology - Other Topics
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Pharmacy Publications
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Created: Tue, 01 Apr 2014, 20:01:41 EST by Charna Kovacevic on behalf of School of Pharmacy