ArticleEndocrinology2008
7B2 prevents unfolding and aggregation of prohormone convertase 2.
Article in Endocrinology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
29 citing papers in PubMed, 51 citations in OpenAlex.
- SEL1L-HRD1 ER-associated degradation facilitates prohormone convertase 2 maturation and glucagon production in islet α cells.Nature communications · 2026Article
- Condensation of the β-cell secretory granule luminal cargoes pro/insulin and ICA512 RESP18 homology domain.Protein science : a publication of the Protein Society · 2023Article
- Molecular Abnormalities in BTBR Mice and Their Relevance to Schizophrenia and Autism Spectrum Disorders: An Overview of Transcriptomic and Proteomic Studies.Biomedicines · 2023Article
- Dense core vesicle markers in CSF and cortical tissues of patients with Alzheimer's disease.Translational neurodegeneration · 2021Article
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
- Mouse Models of Human Proprotein Convertase Insufficiency.Endocrine reviews · 2021Review
- Secreted Chaperones in Neurodegeneration.Frontiers in aging neuroscience · 2020Review
- Divergent kinase regulates membrane ultrastructure of theProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- 7B2 chaperone knockout in APP model mice results in reduced plaque burden.Scientific reports · 2018Article
- Secretogranin III: a diabetic retinopathy-selective angiogenic factor.Cellular and molecular life sciences : CMLS · 2018Review
- Chaperones in Neurodegeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Review
- Phosphorylation and Alternative Splicing of 7B2 Reduce Prohormone Convertase 2 Activation.Molecular endocrinology (Baltimore, Md.) · 2015Article
- A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.Journal of neurochemistry · 2014Article
- Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS.FEBS letters · 2013Article
- The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins.The Journal of biological chemistry · 2013Article
- The pituitary gland of the European eel reveals massive expression of genes involved in the melanocortin system.PloS one · 2013Article
- Parasite neuropeptide biology: Seeding rational drug target selection?International journal for parasitology. Drugs and drug resistance · 2012Review
- The neuroendocrine protein 7B2 is intrinsically disordered.Biochemistry · 2012Article
- Dynamic modulation of prohormone convertase 2 (PC2)-mediated precursor processing by 7B2 protein: preferential effect on glucagon synthesis.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Prohormone convertase 2 (PC2) requires interaction with the neuroendocrine protein 7B2 for the production of an activatable zymogen; the mechanism for this effect is unknown. 7B2 could act proactively to generate an activation-competent form of pro-PC2 during synthesis, or block spontaneous generation of activation-incompetent forms. We here demonstrate that addition of exogenous recombinant 7B2 to CHO cells expressing pro-PC2 prevented the unfolding and aggregation of secreted PC2 forms in a dose-dependent manner, as assessed by aggregation assays, activity assays, cross-linking experiments, and sucrose density gradients. Intracellular pro-PC2 was also found to exist in part as higher-order oligomers that were reduced in the presence of coexpressed 7B2. 7B2 addition did not result in the acquisition of enzymatic competence unless added before or very rapidly after pro-PC2 secretion, indicating that an activation-competent structure cannot be maintained in the absence of 7B2. Velocity sedimentation experiments showed that addition of extracellular 7B2 solubilized three different PC2 species from a precipitable aggregate: two activatable pro-PC2 species, the intact zymogen and a zymogen with a partially cleaved propeptide, and an inactive 66-kDa form. Our results suggest that 7B2 possesses chaperone activity that blocks partially unfolded pro-PC2 forms from losing catalytic competence and then aggregating. The loss of the catalytically competent conformer appears to represent the earliest indicator of pro-PC2 unfolding and is followed on a slower time scale by the appearance of aggregates. Because 7B2 expression is not confined to areas expressing pro-PC2, 7B2 may represent a general intracellular and extracellular secretory chaperone.
Indexed as
Identifiers
What OpenQuestion holds
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.