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¹ Department of Pharmacology and Toxicology, School of Medicine, Wright State University, Dayton, Ohio 45435, USA
² Division of Endocrinology, Metabolism and Molecular Medicine, Charles R Drew University, Los Angeles, California 90059, USA
³ Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA

(Requests for offprints should be addressed to D R Cool; Email: david.cool{at}wright.edu)

(M Furuta is now at The First Department of Medicine, Wakayama University of Medical Science, 811-1 Kimiidera, Wakayama 641-9509, Japan)

Pro-vasopressin and pro-oxytocin are prohormones processed in the neurointermediate lobe pituitary to form the biologically active peptide hormones, arginine vasopressin (AVP) and oxytocin. Neurointermediate lobe pituitaries from normal (+/+), heterozygous (+/–), PC2-Null (–/–), PC1/3-Null and oxytocin-Null mice were analyzed by SELDI-TOF mass spectroscopy for the peptide hormone products, AVP, oxytocin and neurophysin I and II. Molecular ion species with masses characteristic of oxytocin, AVP, neurophysin I and II, i.e. 1009.41, 1084.5, 9677 and 9679 daltons respectively, were identified in all but the oxytocin-Null mice by comparison with synthetic standards or by C-terminal sequence analysis. Other ion species were found specifically in PC2-Null, heterozygote or normal mice. The results indicate that, in mice, both PC1/3 or PC2 enzyme activity are capable, but not required to correctly process pro-vasopressin or pro-oxytocin to their constituent active peptide hormones.

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