Analysis of the beta-endorphin structure-related activity on human monocyte chemotaxis: importance of the N- and C-terminal.
We evaluated the chemotactic activity of beta-endorphin and beta-endorphin-related peptides on human monocytes. We tested beta-endorphin(1-31) and fragments (1-16), (1-17), (1-27) in which the N-terminal of the opioid is preserved, N-acetyl-beta-endorphin(1-31) and fragments (6-31) and (28-31) in which the C-terminal is preserved, and fragment (2-17) that lacks both the N- and C-terminal. The fragments in which the N- and C-terminal were preserved [with the exception of fragment (28-31)] showed a chemotactic effect, while the lack of both terminals deprived the peptides of any activity. Moreover, only the N-terminal-mediated effects were naloxone reversible, while the C-terminal effects were not. These results indicate that while the intact N-terminal is necessary for opioid like effects, both N- and C-terminal can mediate effects on the immune system, thus offering evidence for a nonopioid receptor-mediated effect of opioid peptides on the immune system.
Sacerdote
P
P
Department of Pharmacology, University of Milano, Italy.
Panerai
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AE
D000595:Amino Acid Sequence; D002634:Chemotaxis, Leukocyte / Q000187:drug effects*; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009000:Monocytes / Q000187:drug effects / Q000502:physiology*; D009270:Naloxone / Q000494:pharmacology; D013329:Structure-Activity Relationship; D001615:beta-Endorphin / Q000031:analogs & derivatives* / Q000494:pharmacology*
D009270:Naloxone; D001615:beta-Endorphin