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HYDROXY ANALOGUES OF OXYTOCIN AND OF LYSINE‐VASOPRESSIN
Author(s) -
BISSET G.W.,
CHOWDREY H.S.,
HOPE D.B.,
NILWISES N.,
WÄLTI M.
Publication year - 1979
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1979.tb08704.x
Subject(s) - oxytocin , vasopressin , antidiuretic , endocrinology , medicine , lysine , neuropeptide , hormone , peptide hormone , chemistry , amino acid , biology , biochemistry , receptor
1 Synthetic analogues of oxytocin and of lysine‐vasopressin with an hydroxyl group in either the l or d configuration replacing the primary amino group have been tested for biological activity. 2 [1‐ l (‐2‐Hydroxy‐3‐mercaptopropanoic acid)] oxytocin ([ l ‐Hmp 1 ]oxytocin) was 1.5 to 2 times more potent than oxytocin on the rat uterus in situ , the rat mammary strip and the rat mammary gland in situ and 3 times more potent on the rat isolated uterus. 3 The pressor activity of [1‐( l ‐2‐hydroxy‐3‐mercaptopropanoic acid)‐8‐lysine]vasopressin ([ l ‐Hmp 1 , Lys 8 ] vasopressin) was 2.2 and the antidiuretic activity 2.1 times that of lysine‐vasopressin. 4 The [ d ‐Hmp 1 ] analogues of oxytocin and vasopressin were much less potent than the [ l ‐Hmp 1 ] analogues. 5 The responses to oxytocin and its hydroxy analogues in vivo were qualitatively indistinguishable but the pressor and antidiuretic responses to the hydroxy analogues of lysine‐vasopressin were prolonged compared with those to the parent hormone. 6 The hydroxy analogues of oxytocin and lysine‐vasopressin were not inactivated by pregnancy plasma oxytocinase. 7 The results are discussed in relation to the importance of the primary amino group for the biological activity and metabolism of the neurohypophysial hormones.