ArticleJournal of molecular endocrinology2005
Endocrinomic profile of neurointermediate lobe pituitary prohormone processing in PC1/3- and PC2-Null mice using SELDI-TOF mass spectrometry.
Article in Journal of molecular endocrinology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Appetite- and Weight-Regulating Neuroendocrine Circuitry in Hypothalamic Obesity.Endocrine reviews · 2024Review
- Transcription factor Creb3l1 regulates the synthesis of prohormone convertase enzyme PC1/3 in endocrine cells.Journal of neuroendocrinology · 2020Article
- Somatostatin receptor subtype 5 modifies hypothalamic-pituitary-adrenal axis stress function.JCI insight · 2018Article
- POMC: The Physiological Power of Hormone Processing.Physiological reviews · 2018Review
- Mass spectrometric evidence for neuropeptide-amidating enzymes inThe Journal of biological chemistry · 2018Article
- Peptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function.Journal of neuroscience research · 2010Review
- Components of the basal lamina and dystrophin-dystroglycan complex in the neurointermediate lobe of rat pituitary gland: different localizations of beta-dystroglycan, dystrobrevins, alpha1-syntrophin, and aquaporin-4.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
- Severe obesity and diabetes insipidus in a patient with PCSK1 deficiency.Molecular genetics and metabolismArticle
Corrections and comments
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Authors and funding
7 authors.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.