ArticleEndocrinology2009
Cathepsin L colocalizes with chromogranin a in chromaffin vesicles to generate active peptides.
Article in Endocrinology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 71 citations in OpenAlex.
- Endometriosis Is Associated with Increased Serum and Peritoneal Fluid Concentrations of Chromogranin A and Its Derivatives.Journal of clinical medicine · 2026Article
- Inflammation Promotes Proteolytic Processing of the Prohormone Chromogranin A by Macrophages.Journal of the Endocrine Society · 2025Article
- A complex role of chromogranin A and its peptides in inflammation, autoimmunity, and infections.Frontiers in immunology · 2025Review
- The Role of Catestatin in Preeclampsia.International journal of molecular sciences · 2024Review
- Catestatin: Antimicrobial Functions and Potential Therapeutics.Pharmaceutics · 2023Review
- Serum Catestatin Level as a Stratification Assessment Tool in Non-Critical COVID-19 Patients.International journal of environmental research and public health · 2023Article
- Review
- Putative regulation of macrophage-mediated inflammation by catestatin.Trends in immunology · 2022Review
- Assessment of plasma Catestatin in COVID-19 reveals a hitherto unknown inflammatory activity with impact on morbidity-mortality.Frontiers in immunology · 2022Article
- Review
- Efficient intracellular delivery of proteins by a multifunctional chimaeric peptide in vitro and in vivo.Nature communications · 2021Article
- Chromogranin A regulates gut permeability via the antagonistic actions of its proteolytic peptides.Acta physiologica (Oxford, England) · 2021Article
- Chromogranin A and its fragments in cardiovascular, immunometabolic, and cancer regulation.Annals of the New York Academy of Sciences · 2019Review
- Catestatin as a Target for Treatment of Inflammatory Diseases.Frontiers in immunology · 2018Review
- Circulating chromogranin A and its fragments as diagnostic and prognostic disease markers.Pflugers Archiv : European journal of physiology · 2018Review
- Glycosylated Chromogranin A: Potential Role in the Pathogenesis of Heart Failure.Current heart failure reports · 2017Review
- Identification of novel loci affecting circulating chromogranins and related peptides.Human molecular genetics · 2017Article
- Chromogranin A Regulation of Obesity and Peripheral Insulin Sensitivity.Frontiers in endocrinology · 2017Review
- Polymorphisms at the F12 and KLKB1 loci have significant trait association with activation of the renin-angiotensin system.BMC medical genetics · 2016Article
- Cateslytin, a chromogranin A derived peptide is active against Staphylococcus aureus and resistant to degradation by its proteases.PloS one · 2013Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Chromogranin A (CgA), the major soluble protein in chromaffin granules, is proteolytically processed to generate biologically active peptides including the catecholamine release inhibitory peptide catestatin. Here we sought to determine whether cysteine protease cathepsin L (CTSL), a novel enzyme for proteolytic processing of neuropeptides, acts like the well-established serine proteases [prohormone convertase (PC)1/3 or PC2] to generate catestatin by proteolytic processing of CgA. We found that endogenous CTSL colocalizes with CgA in the secretory vesicles of primary rat chromaffin cells. Transfection of PC12 cells with an expression plasmid encoding CTSL directed expression of CTSL toward secretory vesicles. Deconvolution fluorescence microscopy suggested greater colocalization of CTSL with CgA than the lysosomal marker LGP110. The overexpression of CTSL in PC12 cells caused cleavage of full-length CgA. CTSL also cleaved CgA in vitro, in time- and dose-dependent fashion, and specificity of the process was documented through E64 (thiol reagent) inhibition. Mass spectrometry on CTSL-digested recombinant CgA identified a catestatin-region peptide, corresponding to CgA(360-373). The pool of peptides generated from the CTSL cleavage of CgA inhibited nicotine-induced catecholamine secretion from PC12 cells. CTSL processing in the catestatin region was diminished by naturally occurring catestatin variants, especially Pro370Leu and Gly364Ser. Among the CTSL-generated peptides, a subset matched those found in the catestatin region in vivo. These findings indicate that CgA can be a substrate for the cysteine protease CTSL both in vitro and in cella, and their colocalization within chromaffin granules in cella suggests the likelihood of an enzyme/substrate relationship in vivo.
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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.