ArticleBiochemistry2009
Proteolytic fragments of chromogranins A and B represent major soluble components of chromaffin granules, illustrated by two-dimensional proteomics with NH(2)-terminal Edman peptide sequencing and MALDI-TOF MS.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Endometriosis Is Associated with Increased Serum and Peritoneal Fluid Concentrations of Chromogranin A and Its Derivatives.Journal of clinical medicine · 2026Article
- Peptidomic Analysis Reveals Seasonal Neuropeptide and Peptide Hormone Changes in the Hypothalamus and Pituitary of a Hibernating Mammal.ACS chemical neuroscience · 2023Article
- Forty years of the adrenal chromaffin cell through ISCCB meetings around the world.Pflugers Archiv : European journal of physiology · 2023Review
- Chromogranin A and its fragments as regulators of small intestinal neuroendocrine neoplasm proliferation.PloS one · 2013Article
- The functional role of chromogranins in exocytosis.Journal of molecular neuroscience : MN · 2012Article
- The extended granin family: structure, function, and biomedical implications.Endocrine reviews · 2011Review
- Neuropeptidomic components generated by proteomic functions in secretory vesicles for cell-cell communication.The AAPS journal · 2010Review
- Reprint of: Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis.Regulatory peptides · 2010Article
- Chromogranins A and B as regulators of vesicle cargo and exocytosis.Cellular and molecular neurobiology · 2010Review
- Proteomics of dense core secretory vesicles reveal distinct protein categories for secretion of neuroeffectors for cell-cell communication.Journal of proteome research · 2010Article
- Chromogranin A: a new proposal for trafficking, processing and induction of granule biogenesis.Regulatory peptides · 2010Review
- Chromogranin B gene ablation reduces the catecholamine cargo and decelerates exocytosis in chromaffin secretory vesicles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Neuroendocrine chromaffin granules of adrenal medulla represent regulated secretory vesicles that secrete neuropeptides and catecholamines which mediate cell-cell communication for physiological functions. This study addressed the identification of the major proteins in these secretory vesicles that provide dynamic storage and secretion of bioactive molecules. Proteins of the soluble compartment of the vesicles were separated by two-dimensional gels and subjected to NH(2)-terminal Edman sequencing for identification and determination of NH(2)-termini. Results showed that proteolytic fragments of chromogranin A (CgA) and chromogranin B (CgB) represent the major proteins of these secretory vesicles. These fragments resulted from cleavage of their respective precursor proteins at dibasic and monobasic sites, which is consistent with the known cleavage specificities of prohormone processing enzymes. MALDI-TOF MS analyses of protein spots similar in molecular weight that possessed a range of pI values were represented by molecular forms of CgA and CgB proteins. These findings indicate the high prevalence of endogenous CgA and CgB proteolytic fragments that function in chromaffin secretory vesicles for release of bioactive molecules for cell-cell communication.
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Registered trials
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