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  3. Characterization of pepcan-23 as pro-peptide of RVD-hemopressin (pepcan-12) and stability of hemopressins in mice.
 

Characterization of pepcan-23 as pro-peptide of RVD-hemopressin (pepcan-12) and stability of hemopressins in mice.

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BORIS DOI
10.48350/161545
Date of Publication
May 2021
Publication Type
Article
Division/Institute

Institut für Biochemi...

Author
Glasmacher, Sandra Patricia
Institut für Biochemie und Molekulare Medizin (IBMM)
Gertsch, Jürg
Institut für Biochemie und Molekulare Medizin (IBMM)
Subject(s)

500 - Science::570 - ...

600 - Technology::610...

Series
Advances in biological regulation
ISSN or ISBN (if monograph)
2212-4934
Publisher
Elsevier
Language
English
Publisher DOI
10.1016/j.jbior.2021.100808
PubMed ID
33799079
Uncontrolled Keywords

Cannabinoid receptors...

Description
Hemopressins ((x)-PVNFKLLSH) or peptide endocannabinoids (pepcans) can bind to cannabinoid receptors. RVD-hemopressin (pepcan-12) was shown to act as endogenous allosteric modulator of cannabinoid receptors, with opposite effects on CB1 and CB2, respectively. Moreover, the N-terminally elongated pepcan-23 was detected in different tissues and was postulated to be the pro-peptide of RVD-hemopressin. Currently, data about the pharmacokinetics, tissue distribution and stability of hemopressin-type peptides are lacking. Here we investigated the secondary structure and physiological role of pepcan-23 as precursor of RVD-hemopressin. We assessed the metabolic stability of these peptides, including hemopressin. Using LC-ESI-MS/MS, pepcan-23 was measured in mouse tissues and human whole blood (~50 pmol/mL) and in plasma was the most stable endogenous peptide containing the hemopressin sequence. Using peptide spiked human whole blood, mouse adrenal gland and liver homogenates demonstrate that pepcan-23 acts as endogenous pro-peptide of RVD-hemopressin. Furthermore, administered pepcan-23 converted to RVD-hemopressin in mice. In circular dichroism spectroscopy, pepcan-23 showed a helix-unordered-helix structure and efficiently formed complexes with divalent metal ions, in particular Cu(II) and Ni(II). Hemopressin and RVD-hemopressin were not bioavailable to the brain and showed poor stability in plasma, in agreement with their overall poor biodistribution. Acute hemopressin administration (100 mg/kg) did not modulate endogenous RVD-hemopressin/pepcan-23 levels or influence the endocannabinoid lipidome but increased 1-stearoyl-2-arachidonoyl-sn-glycerol. Overall, we show that pepcan-23 is a biological pro-peptide of RVD-hemopressin and divalent metal ions may regulate this process. Given the lack of metabolic stability of hemopressins, administration of pepcan-23 as pro-peptide may be suitable in pharmacological experiments as it is converted to RVD-hemopressin in vivo.
Handle
https://boris-portal.unibe.ch/handle/20.500.12422/57761
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1-s2.0-S2212492621000245-main.pdftextAdobe PDF7.46 MBAttribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0)publishedOpen
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