ArticleProceedings of the National Academy of Sciences of the United States of America1994
The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 143 citations in OpenAlex.
- Carboxypeptidase E and the Identification of Novel Neuropeptides as Potential Therapeutic Targets.Advances in pharmacology (San Diego, Calif.) · 2018Review
- A repertoire of protease inhibitor families in Amblyomma americanum and other tick species: inter-species comparative analyses.Parasites & vectors · 2017Article
- The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions.The Journal of biological chemistry · 2013Review
- The extended granin family: structure, function, and biomedical implications.Endocrine reviews · 2011Review
- Latent transforming growth factor beta-binding proteins-2 and -3 inhibit the proprotein convertase 5/6A.The Journal of biological chemistry · 2011Article
- Regulation of neuropeptide processing enzymes by catecholamines in endocrine cells.Molecular pharmacology · 2011Article
- ProSAAS-derived peptides are colocalized with neuropeptide Y and function as neuropeptides in the regulation of food intake.PloS one · 2011Article
- The propeptide precursor proSAAS is involved in fetal neuropeptide processing and body weight regulation.Journal of neurochemistry · 2010Article
- The zebra finch neuropeptidome: prediction, detection and expression.BMC biology · 2010Article
- Cell-surface processing of the metalloprotease pro-ADAMTS9 is influenced by the chaperone GRP94/gp96.The Journal of biological chemistry · 2010Article
- Characterization of the prohormone complement in cattle using genomic libraries and cleavage prediction approaches.BMC genomics · 2009Article
- Synthetic small-molecule prohormone convertase 2 inhibitors.Molecular pharmacology · 2009Article
- Peptidomics of Cpe(fat/fat) mouse brain regions: implications for neuropeptide processing.Journal of neurochemistry · 2008Article
- 7B2 prevents unfolding and aggregation of prohormone convertase 2.Endocrinology · 2008Article
- Potential opportunity in the development of new therapeutic agents based on endogenous and exogenous inhibitors of the proprotein convertases.Medicinal research reviews · 2007Review
- A proprotein convertase-inhibiting serpin with an endoplasmic reticulum targeting signal from Branchiostoma lanceolatum, a close relative of vertebrates.The Biochemical journal · 2006Article
- In vitro aggregation of the regulated secretory protein chromogranin A.The Biochemical journal · 2002Article
- Mortality in 7B2 null mice can be rescued by adrenalectomy: involvement of dopamine in ACTH hypersecretion.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Processing of proSAAS in neuroendocrine cell lines.The Biochemical journal · 2002Article
- Neuroendocrine secretory protein 7B2: structure, expression and functions.The Biochemical journal · 2001Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The subtilisin-like prohormone convertase PC2 and the polypeptide 7B2 (an intracellularly cleaved protein of unknown function) are both selectively present in the regulated secretory pathway of neurons and endocrine cells. Here we demonstrate that intact recombinant 7B2 is a potent inhibitor of PC2 and prevents proPC2 cleavage in vitro, whereas the 7B2 cleavage product is virtually inactive. The PC2-related proteinase PC1/PC3 is not inhibited by 7B2. Furthermore, the carboxyl-terminal half of the 7B2 protein sequence is distantly related to the so-called potato inhibitor I family (which includes subtilisin inhibitors). Our findings indicate that 7B2 is a physiological inhibitor of PC2 and may provide alternative avenues for the manipulation of peptide hormone levels.
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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.