ArticleThe Biochemical journal1996
Processing of chromogranins in chromaffin cell culture: effects of reserpine and alpha-methyl-p-tyrosine.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Chromogranin A and catestatin regulate pancreatic islet homeostasis, endocrine function, and neurotransmitter signaling.Communications biology · 2025Article
- Signaling from the sympathetic nervous system regulates hematopoietic stem cell emergence during embryogenesis.Cell stem cell · 2012Article
- The extended granin family: structure, function, and biomedical implications.Endocrine reviews · 2011Review
- Regulation of neuropeptide processing enzymes by catecholamines in endocrine cells.Molecular pharmacology · 2011Article
- Chromogranin/secretogranin proteins in murine heart: myocardial production of chromogranin A fragment catestatin (Chga(364-384)).Cell and tissue research · 2010Article
- Chromogranins A and B as regulators of vesicle cargo and exocytosis.Cellular and molecular neurobiology · 2010Review
- Esomeprazole-induced hyperchromograninemia in the absence of concomitant hypergastrinemia.Nature reviews. Gastroenterology & hepatology · 2010Article
- Measurement of secretory vesicle pH reveals intravesicular alkalinization by vesicular monoamine transporter type 2 resulting in inhibition of prohormone cleavage.The Journal of physiology · 2001Article
- Modulation of gastrin processing by vesicular monoamine transporter type 1 (VMAT1) in rat gastrin cells.The Journal of physiology · 1999Article
- Reserpine-induced reduction in norepinephrine transporter function requires catecholamine storage vesicles.Neurochemistry internationalArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bovine chromaffin cell cultures were treated with either reserpine or alpha-methyl-p-tyrosine for up to 10 days. Afterwards the cells were harvested and the degree of proteolytic processing of secretogranin II, chromogranin A and chromogranin B was determined by immunoblotting and HPLC followed by RIA. There was a significant increase in the proteolysis of all three chromogranins after 4-6 days in the presence of reserpine. The small peptides formed in the presence of reserpine in vitro are also produced in vivo. A similar effect was observed with alpha-methyl-p-tyrosine, an inhibitor of tyrosine hydroxylase, but the response took up to 10 days to develop. Both drugs decreased catecholamine levels but reserpine was more effective, reaching a high degree of depletion after 4 days. In addition, experiments in vitro indicate that low millimolar amounts of either adrenaline (IC50 5.2 mM) or noradrenaline (IC50 2.4 mM) can significantly impair the proteolytic activity of recombinant murine prohormone convertase 1 when assayed with synthetic fluorogenic and/or peptidyl substrates. We conclude that a lowering of catecholamine levels in chromaffin granules leads to a concomitant increase in proteolytic processing of all secretory peptides. Apparently within chromaffin granules the endoproteases are inhibited by catecholamines and thus their removal leads to increased proteolysis.
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Registered trials
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