ReviewDiabetes, obesity & metabolism2006
Catecholamine storage vesicles and the metabolic syndrome: The role of the chromogranin A fragment pancreastatin.
Review in Diabetes, obesity & metabolism, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Naturally occurring variants of the dysglycemic peptide pancreastatin: differential potencies for multiple cellular functions and structure-function correlation.The Journal of biological chemistry · 2014Trial
- Functional genetic variants of the catecholamine-release-inhibitory peptide catestatin in an Indian population: allele-specific effects on metabolic traits.The Journal of biological chemistry · 2012Trial
- Direct vasoactive effects of the chromogranin A (CHGA) peptide catestatin in humans in vivo.Clinical and experimental hypertension (New York, N.Y. : 1993) · 2010Trial
- Utility Evaluation of Porcine Enteroids as PDCoV Infection ModelFrontiers in microbiology · 2020Article
- Circulating chromogranin A and its fragments as diagnostic and prognostic disease markers.Pflugers Archiv : European journal of physiology · 2018Review
- Salivary alpha amylase not chromogranin A reflects sympathetic activity: exercise responses in elite male wheelchair athletes with or without cervical spinal cord injury.Sports medicine - open · 2017Article
- Profiles of secreted neuropeptides and catecholamines illustrate similarities and differences in response to stimulation by distinct secretagogues.Molecular and cellular neurosciences · 2015Article
- Molecular Mechanism for Hypertensive Renal Disease: Differential Regulation of Chromogranin A Expression at 3'-Untranslated Region Polymorphism C+87T by MicroRNA-107.Journal of the American Society of Nephrology : JASN · 2015Article
- Expression of Secretogranin III in Chicken Endocrine Cells: Its Relevance to the Secretory Granule Properties of Peptide Prohormone Processing and Bioactive Amine Content.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015Article
- MicroRNA-22 and promoter motif polymorphisms at the Chga locus in genetic hypertension: functional and therapeutic implications for gene expression and the pathogenesis of hypertension.Human molecular genetics · 2013Article
- Systematic polymorphism discovery after genome-wide identification of potential susceptibility loci in a hereditary rodent model of human hypertension.Blood pressure · 2011Article
- Catecholamine storage vesicles: role of core protein genetic polymorphisms in hypertension.Current hypertension reports · 2011Article
- Chromogranin A and the tumor microenvironment.Cellular and molecular neurobiology · 2010Review
- Secretory granules in inositol 1,4,5-trisphosphate-dependent Ca2+ signaling in the cytoplasm of neuroendocrine cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Review
- Global metabolic consequences of the chromogranin A-null model of hypertension: transcriptomic detection, pathway identification, and experimental verification.Physiological genomics · 2010Article
- Article
Corrections and comments
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Authors and funding
15 authors at 1 institution in 1 country.
Funding
Abstract
Chromogranins or secretogranins (granins), present in secretory granules of virtually all neuroendocrine cells and neurones, are structurally related proteins encoded by different genetic loci: chromogranins A and B, and secretogranins II through VI. Compelling evidence supports both intracellular and extracellular functions for this protein family. Within the cells of origin, a granulogenic or sorting role in the regulated pathway of hormone or neurotransmitter secretion has been documented, especially for chromogranin A (CHGA). Granins also function as pro-hormones, giving rise by proteolytic processing to an array of peptide fragments for which diverse autocrine, paracrine, and endocrine activities have been demonstrated. CHGA measurements yield insight into the pathogenesis of such human diseases as essential hypertension, in which deficiency of the catecholamine release-inhibitory CHGA fragment catestatin may trigger sympathoadrenal overactivity as an aetiologic culprit in the syndrome. The CHGA dysglycaemic fragment pancreastatin is functional in humans in vivo, affecting both carbohydrate (glucose) and lipid (fatty acid) metabolism. Pancreastatin is cleaved from CHGA in hormone storage granules in vivo, and its plasma concentration varies in human disease. The pancreastatin region of CHGA gives rise to three naturally occurring human variants, one of which (Gly297Ser) occurs in the functionally important carboxy-terminus of the peptide, and substantially increases the peptide's potency to inhibit cellular glucose uptake. These observations establish a role for pancreastatin in human intermediary metabolism and disease, and suggest that qualitative hereditary alterations in pancreastatin's primary structure may give rise to interindividual differences in glucose disposition.
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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.