Antagonistic effect of a vasoactive intestinal peptide fragment, vasoactive intestinal peptide(1-11), on guinea pig trachea smooth muscle relaxation.
The conformation of various regions of vasoactive intestinal peptide (VIP) has been analyzed by semiempirical methods, CD, and NMR spectroscopy, indicating that residues 11-21 are most likely to be helical, whereas the amino-terminal portion VIP(1-11) could exhibit two beta-turn structures. VIP(1-11) inhibits 125I-VIP binding to intact guinea pig tracheal epithelial cells and the VIP-induced smooth muscle response. However, the endecapeptide exhibits no effect on the muscle tone. All these data suggest that VIP(1-11) may be a useful tool in studying VIP receptor recognition, its regulation, and cellular functions.
Goossens
J F
JF
INSERM U 16, Lille, France.
Pommery
N
N
Lohez
M
M
Pommery
J
J
Helbecque
N
N
Cotelle
P
P
Lhermitte
M
M
Henichart
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D002478:Cells, Cultured; D004847:Epithelial Cells; D004848:Epithelium / Q000187:drug effects / Q000378:metabolism; D006168:Guinea Pigs; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D008969:Molecular Sequence Data; D009126:Muscle Relaxation / Q000187:drug effects*; D009130:Muscle, Smooth / Q000187:drug effects / Q000502:physiology; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation; D014132:Trachea / Q000187:drug effects* / Q000502:physiology; D014660:Vasoactive Intestinal Peptide / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*
D010446:Peptide Fragments; C072440:vasoactive intestinal peptide (1-11); D014660:Vasoactive Intestinal Peptide