ArticleThe Biochemical journal2002
Processing of proSAAS in neuroendocrine cell lines.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- ProSAAS neuropeptides and receptors GPR171 and GPR83: Potential therapeutic applications for pain, anxiety, and body weight regulation.The Journal of pharmacology and experimental therapeutics · 2025Review
- Mice lacking proSAAS display alterations in emotion, consummatory behavior and circadian entrainment.Genes, brain, and behavior · 2022Article
- Article
- PEN Receptor GPR83 in Anxiety-Like Behaviors: Differential Regulation in Global vs Amygdalar Knockdown.Frontiers in neuroscience · 2021Article
- Secreted Chaperones in Neurodegeneration.Frontiers in aging neuroscience · 2020Review
- Neuropeptide PEN and Its Receptor GPR83: Distribution, Signaling, and Regulation.ACS chemical neuroscience · 2019Review
- Orphan neuropeptides and receptors: Novel therapeutic targets.Pharmacology & therapeutics · 2018Review
- Targeting the Recently Deorphanized Receptor GPR83 for the Treatment of Immunological, Neuroendocrine and Neuropsychiatric Disorders.Progress in molecular biology and translational science · 2018Review
- The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Chaperones in Neurodegeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Review
- Carboxypeptidases in disease: insights from peptidomic studies.Proteomics. Clinical applications · 2014Review
- A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.Journal of neurochemistry · 2014Article
- ProSAAS-derived peptides are differentially processed and sorted in mouse brain and AtT-20 cells.PloS one · 2014Article
- Effects of maternal separation and methamphetamine exposure on protein expression in the nucleus accumbens shell and core.Metabolic brain disease · 2012Article
- The hypothalamic-neurohypophyseal system: from genome to physiology.Journal of neuroendocrinology · 2012Review
- ProSAAS-derived peptides are colocalized with neuropeptide Y and function as neuropeptides in the regulation of food intake.PloS one · 2011Article
- Article
- The propeptide precursor proSAAS is involved in fetal neuropeptide processing and body weight regulation.Journal of neurochemistry · 2010Article
- Article
- Peptidomics of Cpe(fat/fat) mouse brain regions: implications for neuropeptide processing.Journal of neurochemistry · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
ProSAAS, a recently discovered granin-like protein, potently inhibits prohormone convertase (PC)1, and might also perform additional functions. In the present study, the processing of proSAAS was compared in two neuroendocrine cell lines overexpressing this protein: the AtT-20 mouse pituitary corticotrophic line and the PC12 rat adrenal phaeochromocytoma line. The processing of proSAAS was examined by pulse-chase analysis using [(3)H]leucine, by MS, and by chromatography and radioimmunoassay. Various smaller forms of proSAAS were detected, including peptides designated as little SAAS, PEN and big LEN. Because the PC-12 cells used in the present study do not express either PC1 or PC2, the finding that these cells efficiently cleave proSAAS indicates that these cleavages do not require either enzyme. Two of the peptides identified in AtT-20 media represent novel C-terminally truncated forms of PEN. In both cell lines, the secretion of the small proSAAS-derived peptides is stimulated by secretagogues. However, long-term treatment of wild-type AtT-20 cells with two different secretagogues (8-bromo-cAMP and a phorbol ester) does not affect levels of proSAAS mRNA; this treatment significantly increases PC1 mRNA by approx. 60-80%. The lack of co-regulation of proSAAS and PC1 mRNA implies that enzyme activity can be induced without an accompanying increase in the inhibitor. In addition, the finding that the peptides are secreted via the regulated pathway is consistent with the proposal that they may function as neuropeptides.
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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.