1. Endocrinomic profile of neurointermediate lobe pituitary prohormone processing in PC1/3- and PC2-Null mice using SELDI-TOF mass spectrometry
- Author
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Theodore C. Friedman, William C. Grunwald Jr., Ziaorong Zhu, Machi Furuta, Donald F. Steiner, Atira Hardiman, and David R. Cool
- Subjects
endocrine system ,Pituitary gland ,Vasopressin ,medicine.medical_specialty ,Proteome ,Neurophysin I ,Molecular Sequence Data ,Prohormone ,Neurophysins ,Biology ,Peptide hormone ,Oxytocin ,Article ,Mass Spectrometry ,Mice ,Endocrinology ,Internal medicine ,medicine ,Animals ,Humans ,Amino Acid Sequence ,Protein Precursors ,Molecular Biology ,Peptide sequence ,Mice, Knockout ,Arginine Vasopressin ,Proprotein Convertase 2 ,medicine.anatomical_structure ,Proprotein Convertase 1 ,Pituitary Gland ,hormones, hormone substitutes, and hormone antagonists ,medicine.drug - Abstract
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.
- Published
- 2005
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