These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Identification of endomorphin-1 and endomorphin-2 binding sites in human mu-opioid receptor by antisense oligonucleotide strategy.
    Author: Fichna J, Gach K, Perlikowska R, Poels J, Vanden Broeck J, Szemraj J, Janecka A.
    Journal: Chem Biol Drug Des; 2008 Dec; 72(6):507-12. PubMed ID: 19090917.
    Abstract:
    The effects of phosphorothioate antisense oligodeoxynucleotides against exons-1, -2, -3 and -4 of the human mu-opioid receptor were studied in the CHO-mu-opioid receptor cells using aequorin luminescence-based calcium assay. All four antisense oligodeoxynucleotides significantly decreased the level of mu-opioid receptor mRNA in comparison with the non-treated cells, used as control. However, no statistically significant differences between antisense oligodeoxynucleotides were observed. antisense oligodeoxynucleotides against exon-2 attenuated endomorphin-1-induced intracellular calcium response in a concentration-dependent manner. antisense oligodeoxynucleotides against exons-1, -2, -3 and -4 inhibited endomorphin-2-induced intracellular calcium response in a concentration-dependent manner and the effect of antisense oligodeoxynucleotides against exons-3 and -4 was most pronounced. The mismatch oligodeoxynucleotides against respective exons failed to exert any effect. The selective actions of antisense probes directed against different exons of the human mu-opioid receptor gene, that resulted, at the protein level, in attenuation of calcium responses induced by endomorphin-1 and endomorphin-2, suggest that the binding sites for endomorphins are structurally and functionally different. The presence of functionally distinct binding sites might play a crucial role in the modulation of pain and may be important clinically.
    [Abstract] [Full Text] [Related] [New Search]