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J. Biol. Chem., Vol. 262, Issue 29, 14010-14013, Oct, 1987
Y Yiangou, V Di Marzo, RA Spokes, M Panico, HR Morris and SR Bloom
The primary structure and biological activity of a novel prepro- vasoactive
intestinal peptide (prepro-VIP)-derived peptide has been determined from an
adrenal pheochromocytoma. The peptide was purified sufficiently for
characterization by fast atom bombardment mapping after cation-exchange and
reverse-phase fast protein liquid chromatography. The sequence of this
novel peptide corresponds exactly to prepro-VIP-81-122 and has been
designated peptide histidine valine 42 (PHV-42). Synthetic PHV-42 reduced
both the force and frequency of spontaneous contractions of isolated rat
uterus and was at least 12 times more potent than peptide histidine
methionine (prepro-VIP-81- 107), and over a hundred times more potent than
noradrenaline. PHV-42 was also more potent than peptide histidine
methionine in relaxing smooth muscle preparations of rat stomach and guinea
pig trachea, but was approximately 4-fold less potent in reducing blood
pressure than VIP. PHV-42 thus forms a separate subsystem in the VIP family
of peptides and may be the most biologically active product of prepro-VIP
in certain tissues such as the uterus and trachea.
Isolation, characterization, and pharmacological actions of peptide histidine valine 42, a novel prepro-vasoactive intestinal peptide- derived peptide
Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.
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