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"Chrétien MN" Authored Publications:

Title Authors PubMed ID
1 Reduction and S-nitrosation of the neuropeptide oxytocin: implications for its biological function Roy JF; Chrétien MN; Woodside B; English AM; 17692543
CBAMS

 

Title:Reduction and S-nitrosation of the neuropeptide oxytocin: implications for its biological function
Authors:Roy JFChrétien MNWoodside BEnglish AM
Link:https://pubmed.ncbi.nlm.nih.gov/17692543/
DOI:10.1016/j.niox.2007.06.005
Publication:Nitric oxide : biology and chemistry
Keywords:
PMID:17692543 Category:Nitric Oxide Date Added:2019-06-19
Dept Affiliation: CBAMS
1 Department of Chemistry and Biochemistry, Centre for Biological Applications of Mass Spectrometry, Concordia University, 7141 Sherbrooke Street W., Montreal, Que., Canada.

Description:

Oxytocin (OT; Cys-Tyr-Ile-Gln-Asn-Cys-Pro-leu-Gly), a posterior pituitary peptide hormone, is characterized by a Cys1-Cys6 disulfide bond in its stable, isolated state. This paper describes a simple, one-step method for the production of OT in its reduced, dithiol form (OT dithiol), free of reducing agent. The effects of temperature, pH, and metal-ion chelators on the autoxidation of OT dithiol were examined to establish if this form is likely to persist under biological conditions. It was found that OT dithiol has a half-life of 1.8h with respect to reformation of OT disulfide at 37 degrees C and pH 6.9 in the presence of the copper chelators, DTPA and neocuproine. S-Nitrosation of OT dithiol by acidified nitrite at pH 3.0 was examined by absorption spectroscopy and HPLC-UV-MS, which revealed that both singly and doubly S-nitrosated OT are formed. These results suggest novel chemical aspects to OT signaling, the biological implications of which are discussed here.





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