Background: Little is known of the importance of chromogranins (Cg) and secretogranins (Sg) in ulcerative colitis (UC). We therefore investigated fecal levels of CgA, CgB, SgII and SgIII, and their association with inflammatory activity, disease duration and medical therapy in UC.
Methods: Analyses of CgA, CgB, SgII, SgIII and calprotectin in stool samples from 41 UC patients and 29 healthy controls were performed. Two stool samples, during relapse and remission, respectively, were obtained from each UC patient.
Results: The levels of fecal CgA and SgII were higher in UC patients with active disease as compared to healthy controls. CgB and SgII were positively correlated with disease duration, but none of the granins were positively correlated with calprotectin, Mayo score, CRP or serum concentrations of TNF in UC patients with active disease. Also UC patients in remission had higher levels of CgA, CgB, SgII, and SgIII as compared to healthy controls. However, levels of fecal CgA, CgB, SgII and SgIII were lower during active disease relative to remission. Moreover, fecal levels of CgA and SgII were higher in UC patients in remission treated with thiopurines than in thiopurine-naïve patients in remission.
Conclusion: Fecal chromogranins and secretogranins are increased in UC but are not associated with disease activity, but seem to increase with duration of the disease. Thus, fecal granins might reflect structural changes associated with chronicity of disease, or medical therapy.
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http://dx.doi.org/10.1016/j.crohns.2013.04.019 | DOI Listing |
Kaohsiung J Med Sci
March 2019
Department of Neurology, Dongyang People's Hospital, Zhejiang, China.
Little is known about the relevance of chromogranins (Cgs) and secretogranins (Sgs) in Parkinson's disease (PD). In this study, we determined serum levels of CgA, CgB, and SgII in PD patients and assessed their association with disease severity. PD patients were recruited, identified, and classified as having early (n = 14), intermediate (n = 18), or late (n = 4) stage disease according to Hoehn-Yahr scores.
View Article and Find Full Text PDFCell Tissue Res
April 2019
Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0732, USA.
We have previously shown that the chromogranin A (CgA)-derived peptide catestatin (CST: hCgA) inhibits nicotine-induced secretion of catecholamines from the adrenal medulla and chromaffin cells. In the present study, we seek to determine whether CST regulates dense core (DC) vesicle (DCV) quanta (catecholamine and chromogranin/secretogranin proteins) during acute (0.5-h treatment) or chronic (24-h treatment) cholinergic (nicotine) or peptidergic (PACAP, pituitary adenylyl cyclase activating polypeptide) stimulation of PC12 cells.
View Article and Find Full Text PDFSci Rep
November 2018
Institute of Medicine, University of Gothenburg, Gothenburg, Sweden.
Altered fecal levels of chromogranins (Cg) and secretogranins (Sg) are demonstrated in irritable bowel syndrome (IBS), but their role in IBS pathophysiology remains unknown. This study aimed to determine if granins are associated with bacterial composition, immune activation and IBS symptoms. Protein levels of fecal granins (CgA, CgB, SgII and SgIII) were analysed with immunoassays.
View Article and Find Full Text PDFNeurogastroenterol Motil
January 2019
University of Washington, Seattle, Washington.
Background: Granins have been implicated in the pathophysiology of irritable bowel syndrome (IBS) in adults. We sought to determine whether fecal granins are altered in children with IBS and associated with symptoms.
Methods: Children (7-12 years of age) with IBS and healthy controls (HC) kept daily pain and stool diaries for 2 weeks.
Prog Neurobiol
July 2017
Department of Biomedicine, University of Bergen, Norway.
The granin family comprises altogether 7 different proteins originating from the diffuse neuroendocrine system and elements of the central and peripheral nervous systems. The family is dominated by three uniquely acidic members, namely chromogranin A (CgA), chromogranin B (CgB) and secretogranin II (SgII). Since the late 1980s it has become evident that these proteins are proteolytically processed, intragranularly and/or extracellularly into a range of biologically active peptides; a number of them with regulatory properties of physiological and/or pathophysiological significance.
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