Chromogranin B
Chromogranin A
Chromogranins
Secretogranin II
Adrenal Medulla
PC12 Cells
Inositol 1,4,5-Trisphosphate Receptors
Pancreatic Hormones
Golgi Apparatus
The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. (1/53)
The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules. Here we show that this loop, when fused to the constitutively secreted protein alpha1-antitrypsin (AT), is sufficient to direct the fusion protein to secretory granules. Importantly, the sorting efficiency of the AT reporter protein bearing two loops (E2/3-AT-E2/3) is much higher compared with that of AT with a single disulfide-bonded loop. In contrast to endogenous CgB, E2/3-AT-E2/3 does not undergo Ca2+/pH-dependent aggregation in the TGN. Furthermore, the disulfide-bonded loop of CgB mediates membrane binding in the TGN and does so with 5-fold higher efficiency if two loops are present on the reporter protein. The latter finding supports the concept that under physiological conditions, aggregates of CgB are the sorted units of cargo which have multiple loops on their surface leading to high membrane binding and sorting efficiency of CgB in the TGN. (+info)Characterisation of N-terminal chromogranin A and chromogranin B in mammals by region-specific radioimmunoassays and chromatographic separation methods. (2/53)
Chromogranin A (CgA) and chromogranin B (CgB) are acidic proteins stored in and released from hormone granules in endocrine and neuroendocrine tissue. The chromogranins are postulated to serve as pro-hormones to generate biologically active peptides, which may influence hormonal release and vascular functions or have antibacterial functions. Although N-terminal and C-terminal regions show some species amino acid homology, the chromogranins as a whole display considerable interspecies differences, which prevents their use in comparative studies of biological functions. We present four new radioimmunoassays for the measurement of defined N-terminal regions of CgA and CgB. A new radioimmunoassay for measurement of intact bovine CgA has also been developed. With these assays and two previously published ones, we have compared the cross-reactivity of chromogranins from man, cattle, sheep, goat, pig and horse and compared adrenomedullar content and serum levels of CgA from these species. We have also studied the influence of peptide concentrations and the ionic strength of the mobile phase on molecular weight estimations. Assays with antibodies directed against the N-terminal parts of CgA and CgB showed sufficient interspecies cross-reactivity to allow comparative quantification of the circulating levels in man, cattle, sheep, goat, pig and horse. Assays measuring the intact human or bovine CgA were not suitable for comparative purposes in samples from sheep, goat, pig and horse. Molecular interactions between vasostatin immunoreactive material and intact bovine CgA were demonstrated in gel permeation studies, suggesting that conclusions about the degree of N-terminal processing from elution profiles should be made with caution. Reliable interspecies comparison of chromogranins is difficult, but measurements with region-specific assays may be helpful to study concentrations of chromogranins and chromogranin-related peptides. (+info)Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS. (3/53)
Chromogranin B (CgB) is a regulated secretory protein that is stored in endocrine and neuroendocrine cells. It can be processed proteolytically to small peptide fragments. In the present study three proteolytic products of porcine CgB were obtained after size-exclusion, immunoaffinity, and reversed-phase chromatography, and then identified by electrospray tandem MS. One novel peptide was identified as S586-R602 (SR-17) and is phosphorylated at one or two serine residues. Another novel peptide H603-Q636 (HQ-34), with molecular mass 3815.56 Da, was found to be oxidized at the methionine residue. In addition, a secretolytin-like peptide fragment (KR-11), which is two amino acids shorter than the bovine secretolytin, was found. This is the first report that the C-terminal region of CgB, the homologue of human CCB, is proteolytically processed further into three small peptide fragments. (+info)Molecular characterization of frog chromogranin B reveals conservation of selective sequences encoding potential novel regulatory peptides. (4/53)
Chromogranin B (CgB) is a member of the granin family of neuroendocrine secretory proteins, which has been proposed to play a role in secretory granule biogenesis and as a precursor to bioactive peptides. The cloning of CgB in a phylogenetically distant vertebrate, the frog Rana ridibunda, reveals a modest overall homology (35-40%) with mammalian CgB. However, the sequences of the N- and C-terminal regions are more highly conserved (57-65% amino acid identity) and may give rise to novel regulatory peptides. In frog, intense expression of CgB mRNA was observed in particular structures of the brain and in the distal lobe of the pituitary. (+info)Localization of the secretory granule marker protein chromogranin B in the nucleus. Potential role in transcription control. (5/53)
Chromogranins A (CGA) and B (CGB) are two major Ca(2+) storage proteins of the secretory granules of neuroendocrine cells. Nevertheless, we found in the present study that CGB was also localized in the nucleus. In immunogold electron microscopy using bovine adrenal medullary chromaffin cells, it was found that the number of CGB-labeled gold particles localized per microm(2) of the nucleus was equivalent to 20% that of CGB-labeled gold particles localized per microm(2) of the secretory granules. Considering that CGB is estimated to exist in the 0.1-0.2-mm range in the secretory granules of bovine chromaffin cells, 20% of these amounts to 20-40 microm. In addition, transfection of CGA and CGB into nonneuroendocrine COS-7 and NIH3T3 cells repeatedly indicated the nuclear localization of CGB in addition to its usual localization in the cytoplasm. Moreover, immunoblot and immunogold electron microscopy analyses of neuroendocrine PC12 cells also showed the existence of endogenous CGB in both the cytosol and the nucleus. Nuclear routing of CGB did not appear to depend entirely upon the nuclear localization signal as some of the nuclear localization signal mutant CGB were still targeted to the nucleus. In gene array assay, CGB was shown to either induce or suppress transcription of many genes including those of transcription factors. Of these we have analyzed eight genes, four induced (zinc finger protein, MEF2C, hCRP2, abLIM) and four suppressed (hcKrox, T3-receptor, troponin C, integrin) using the quantitative reverse transcription-PCR method and spectrophotometry to determine the transcription levels of each mRNA. CGB was shown to increase the transcription of zinc finger protein, MEF2C, hCRP2, and abLIM by 2.5-5-fold while suppressing that of hcKrox, T3-receptor, troponin C, and integrin by 60-75%. Given that MEF2C and hcKrox genes are transcription factors, these results pointed to the transcription control role of CGB in the nucleus. (+info)Presence of chromogranin-derived antimicrobial peptides in plasma during coronary artery bypass surgery and evidence of an immune origin of these peptides. (6/53)
Chromogranin A (CGA) and chromogranin B (CGB) are acidic proteins stored in secretory organelles of endocrine cells and neurons. In addition to their roles as helper proteins in the packaging of peptides, they may serve as prohormones to generate biologically active peptides such as vasostatin-1 and secretolytin. These molecules derived from CGA and CGB, respectively, possess antimicrobial properties. The present study demonstrates that plasmatic levels of both vasostatin-1 and secretolytin increase during surgery in patients undergoing cardiopulmonary bypass (CPB). Vasostatin-1 and secretolytin, initially present in plasma at low levels, are released just after skin incision. Consequently, they can be added to enkelytin, an antibacterial peptide derived from proenkephalin A, for the panoply of components acting as a first protective barrier against hypothetical invasion of pathogens, which may occur during surgery. CGA and CGB, more commonly viewed as markers for endocrine and neuronal cells, were also found to have an immune origin. RNA messengers coding for CGB were amplified by reverse transcription-polymerase chain reaction in human monocytes, and immunocytochemical analysis by confocal microscopy revealed the presence of CGA or CGB or both in monocytes and neutrophils. A combination of techniques including confocal microscopic analysis, mass spectrometry measurement, and antibacterial tests allowed for the identification of the positive role of interleukin 6 (IL-6) in the secretolytin release from monocytes in vitro. Because IL-6 release is known to be strongly enhanced during CPB, we suggest a possible relationship between IL-6 and the increased level of secretolytin in patients undergoing CPB. (+info)Chromogranin B-induced secretory granule biogenesis: comparison with the similar role of chromogranin A. (7/53)
The two major proteins of secretory granules of secretory cells, chromogranins A (CGA) and B (CGB), have previously been proposed to play key roles in secretory granule biogenesis. Recently, CGA was reported to play an on/off switch role for secretory granule biogenesis. In the present study we found CGB being more effective than CGA in inducing secretory granule formation in non-neuroendocrine NIH3T3 and COS-7 cells. The mean number of dense core granules formed/cell of CGA-transfected NIH3T3 cells was 2.51, whereas that of CGB-transfected cells was 4.02, indicating the formation of 60% more granules in the CGB-transfected cells. Similarly, there were 55% more dense core granules formed in the CGB-transfected COS-7 cells than in the CGA-transfected cells. Moreover, transfection of CGA- and CGB-short interfering RNA (siRNA) into neuroendocrine PC12 cells not only decreased the amount of CGA and CGB expressed but also reduced the number of secretory granules by 41 and 78%, respectively, further suggesting the importance of CGB expression in secretory granule formation. (+info)A functional interaction between chromogranin B and the inositol 1,4,5-trisphosphate receptor/Ca2+ channel. (8/53)
Chromogranins A and B (CGA and CGB) are high capacity, low affinity calcium (Ca2+) storage proteins found in many cell types most often associated with secretory granules of secretory cells but also with the endoplasmic reticulum (ER) lumen of these cells. Both CGA and CGB associate with inositol 1,4,5-trisphosphate receptor (InsP3R) in a pH-dependent manner. At an intraluminal pH of 5.5, as found in secretory vesicles, both CGA and CGB bind to the InsP3R. When the intraluminal pH is 7.5, as found in the ER, CGA totally dissociates from InsP3R, whereas CGB only partially dissociates. To investigate the functional consequences of the interaction between the InsP3R and CGB monomers or CGA/CGB heteromers, purified mouse InsP3R type I were fused to planar lipid bilayers and activated by 2 microM InsP3. In the presence of luminal CGB monomers or CGA/CGB heteromers the InsP3R/Ca2+ channel open probability and mean open time increased significantly. The channel activity remained elevated when the pH was changed to 7.5, a reflection of CGB binding to the InsP3R even at pH 7.5. These results suggest that CGB may play an important modulatory role in the control of Ca2+ release from the ER. Furthermore, the difference in the ability of CGA and CGB to regulate the InsP3R/Ca2+ channel and the variability of CGA/CGB ratios could influence the pattern of InsP3-mediated Ca2+ release. (+info)Chromogranin B is a protein that is synthesized and stored in the secretory granules of various endocrine cells, including neurons, chromaffin cells of the adrenal medulla, and endocrine cells of the pancreas, gut, and lung. It is a member of the chromogranin family of proteins, which are characterized by their high molecular weight and their ability to bind to calcium ions. In the medical field, chromogranin B is often used as a diagnostic marker for various diseases, particularly neuroendocrine tumors (NETs). NETs are a type of cancer that arises from neuroendocrine cells and can occur in various parts of the body, including the pancreas, lung, and gastrointestinal tract. Chromogranin B is often overexpressed in NETs, and its levels in the blood can be used to monitor the progression of the disease and to assess the response to treatment. Chromogranin B is also used as a marker for other conditions, such as pheochromocytoma (a tumor of the adrenal gland), carcinoid syndrome (a condition caused by the release of excessive amounts of hormones by NETs), and multiple endocrine neoplasia type 1 (a genetic disorder that increases the risk of developing NETs).
Chromogranin A (CgA) is a protein that is synthesized and stored in the secretory granules of various endocrine and neuroendocrine cells, including neurons, chromaffin cells of the adrenal medulla, and endocrine cells of the pancreas, gastrointestinal tract, and lungs. In the medical field, CgA is often used as a diagnostic marker for various diseases, including neuroendocrine tumors (NETs), pheochromocytoma, and carcinoid syndrome. It is also used as a marker for the functional status of endocrine cells, as well as a predictor of tumor recurrence and survival in patients with NETs. CgA is a large protein that is cleaved into smaller peptides, some of which have specific functions. For example, the chromogranin A 72-160 fragment (CgA 72-160) is a potent vasoconstrictor that is released from chromaffin cells in response to stress or injury. Other CgA fragments have been shown to have anti-inflammatory and anti-apoptotic effects.
Chromogranins are a family of proteins that are synthesized and stored in secretory granules of endocrine and neuroendocrine cells. They are composed of multiple tandem repeats of a basic amino acid-rich domain, and are involved in various cellular processes such as exocytosis, cell signaling, and regulation of enzyme activity. In the medical field, chromogranins are often used as markers for neuroendocrine tumors, as they are overexpressed in many of these tumors. They are also used as diagnostic tools for various conditions, including pheochromocytoma, carcinoid syndrome, and pancreatic neuroendocrine tumors. Additionally, chromogranins have been studied for their potential therapeutic applications, such as in the treatment of Alzheimer's disease and other neurodegenerative disorders.
Secretogranin II (also known as chromogranin B) is a protein that is synthesized and stored in secretory granules of endocrine cells, such as chromaffin cells in the adrenal medulla and neurons in the central nervous system. It is a member of the secretogranin family of proteins, which are involved in the regulation of neurotransmitter release and hormone secretion. Secretogranin II is synthesized as a precursor protein that is cleaved into smaller peptides and proteins by proteolytic enzymes. One of the cleavage products of secretogranin II is vasopressin, a hormone that regulates blood pressure and water balance in the body. Other cleavage products of secretogranin II include chromogranin A, which is involved in the regulation of neurotransmitter release, and catestatin, which inhibits the release of catecholamines (such as adrenaline and noradrenaline) from the adrenal medulla. In addition to its role in hormone and neurotransmitter regulation, secretogranin II has also been implicated in the pathogenesis of certain diseases, including neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, as well as certain types of cancer.
The adrenal medulla is the inner part of the adrenal gland, located adjacent to the outer adrenal cortex. It is responsible for producing and secreting hormones that regulate the body's response to stress, including adrenaline (epinephrine) and noradrenaline (norepinephrine). These hormones are released into the bloodstream in response to stressors such as physical exertion, fear, or injury, and help to increase heart rate, blood pressure, and blood sugar levels, preparing the body for a fight or flight response. The adrenal medulla is innervated by the sympathetic nervous system, which controls the body's response to stress.
In the medical field, cytoplasmic granules refer to small, dense structures found within the cytoplasm of certain cells. These granules are often involved in various cellular processes, such as protein synthesis, metabolism, and signaling. There are many different types of cytoplasmic granules, each with its own unique function and composition. Some examples of cytoplasmic granules include: - Lysosomes: These are organelles that contain digestive enzymes and are involved in breaking down and recycling cellular waste. - Peroxisomes: These are organelles that contain enzymes involved in the breakdown of fatty acids and other molecules. - Endosomes: These are organelles that are involved in the internalization and processing of extracellular molecules. - Ribosomes: These are small structures that are involved in protein synthesis. Cytoplasmic granules can be visualized using various microscopy techniques, such as light microscopy, electron microscopy, and immunofluorescence microscopy. The presence and distribution of cytoplasmic granules can provide important information about the function and health of a cell.
Inositol 1,4,5-trisphosphate receptors (IP3Rs) are a family of intracellular calcium channels that are activated by the binding of inositol 1,4,5-trisphosphate (IP3), a second messenger molecule. These receptors are found in the endoplasmic reticulum (ER) of most eukaryotic cells and play a critical role in regulating intracellular calcium levels. When IP3 binds to an IP3R, it causes a conformational change in the receptor that opens a channel in the ER membrane, allowing calcium ions to flow out of the ER and into the cytosol. This increase in cytosolic calcium levels can trigger a wide range of cellular responses, including muscle contraction, neurotransmitter release, and gene expression. IP3Rs are important for many physiological processes, including fertilization, neurotransmission, and the regulation of the immune response. They are also involved in a number of pathological conditions, including neurodegenerative diseases, cardiovascular disease, and cancer. As such, they are an important target for the development of new drugs and therapies.
Pancreatic hormones are hormones produced by the pancreas that play important roles in regulating various bodily functions. The pancreas is a glandular organ located in the abdomen, behind the stomach, and it produces both digestive enzymes and hormones. The main pancreatic hormones are: 1. Insulin: This hormone regulates blood sugar levels by promoting the uptake of glucose by cells and the storage of glucose in the liver and muscles. 2. Glucagon: This hormone raises blood sugar levels by stimulating the liver to release stored glucose into the bloodstream. 3. Somatostatin: This hormone inhibits the release of insulin and glucagon, as well as the production of digestive enzymes. 4. Pancreatic polypeptide: This hormone regulates appetite and digestion. 5. VIP (Vasoactive Intestinal Peptide): This hormone regulates the contraction and relaxation of smooth muscles in the digestive tract. Pancreatic hormones play a crucial role in maintaining normal blood sugar levels, regulating digestion, and controlling appetite. Imbalances in these hormones can lead to various medical conditions, such as diabetes, pancreatitis, and pancreatic cancer.
Dithiothreitol (DTT) is a reducing agent used in various medical and scientific applications. It is a small molecule that contains two sulfur atoms and is commonly used to break disulfide bonds in proteins, which can help to unfold or denature them. This property makes DTT useful in protein purification and analysis, as well as in the study of protein structure and function. In addition to its use in protein chemistry, DTT is also used in the treatment of certain medical conditions. For example, it has been shown to have anti-inflammatory and antioxidant effects, and it has been used to treat conditions such as cystic fibrosis and multiple sclerosis. However, more research is needed to fully understand the potential therapeutic applications of DTT in medicine.
Chromogranin A
SCG5
SCG3
Granin
SCG2
Pheochromocytoma
Solid pseudopapillary tumour
Ceruminous adenoma
Carcinoid syndrome
Saliva testing
Thyroid neoplasm
Lung cancer
Peptide YY
Secretoneurin
Homeostasis
Neuroendocrine tumor
Insulinoma
Secretogranin-1
Synaptophysin
B3GAT1
MIA PaCa-2
Mepartricin
Pancreatic neuroendocrine tumor
Molecular diagnostics
Zollinger-Ellison syndrome
Neuroendocrine differentiation
Paraganglioma
Atrial fibrillation
Neuroendocrine cell
Xenin
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Positive for chromogranin4
- A wide variety of neuroendocrine tumors stain positive for chromogranin A. (medscape.com)
- Adrenal system tumors that stain positive for chromogranin A include pheochromocytoma. (medscape.com)
- In contrast, conventional carcinoids are often diffusely positive for chromogranin and synaptophysin, with abundant electron-dense granules on electron microscopy [ 4 ]. (gastrores.org)
- 1C: Immunohistochemical stain showing tumor cells with neuroendocrine pattern was positive for chromogranin (Immunoperoxidase X400). (nepjol.info)
Synaptophysin8
- Adenocarcinoma ex-goblet cell carcinoid (AdexGCC) was considered a neuroendocrine adenocarcinoma, despite majority of tumor cells being negative for conventional neuroendocrine markers such as chromogranin and synaptophysin. (gastrores.org)
- Recently, insulinoma-associated protein 1 (INSM1) has been identified as a novel neuroendocrine marker that is more sensitive than chromogranin, synaptophysin, and CD56 in pulmonary neuroendocrine tumors. (gastrores.org)
- We studied this marker in conjunction with chromogranin, synaptophysin, and CD56 in 36 appendiceal AdexGCCs (21 primaries, 15 metastatic). (gastrores.org)
- Primary and metastatic AdexGCCs showed no difference in INSM1, chromogranin, synaptophysin, or CD56 staining. (gastrores.org)
- INSM1 exhibits low expression in AdexGCCs and is expressed by a lower proportion of tumor cells compared to chromogranin and synaptophysin. (gastrores.org)
- Conventional neuroendocrine markers, such as chromogranin and synaptophysin, however, are often negative or focally positive in these tumors [ 2 , 3 ]. (gastrores.org)
- Hristov et al previously demonstrated that chromogranin and synaptophysin were only expressed in 37% and 30% of AdexGCCs, respectively [ 2 ]. (gastrores.org)
- Tumor cells are immunoreactive for chromogranin, synaptophysin, neuron-specific enolase or other neuroendocrine markers. (pathologyoutlines.com)
Secretory protein3
- Chromogranin A or parathyroid secretory protein 1 (gene name CHGA) is a member of the granin family of neuroendocrine secretory proteins. (wikipedia.org)
- Chromogranin A is a secretory protein, composed of 439 amino acids, found in the large dense-core vesicles of the neuroendocrine cells. (medscape.com)
- Chromogranin A (CgA) is a secretory protein, composed of 439 amino acids, found in the large dense-core vesicles of the neuroendocrine cells. (medscape.com)
Pancreatic2
- Chromogranin A induces and promotes the generation of secretory granules such as those containing insulin in pancreatic islet beta cells. (wikipedia.org)
- Chromogranin A is a reliable serum diagnostic biomarker for pancreatic neuroendocrine tumors but not for insulinomas. (medscape.com)
Carcinoid1
- Chromogranin A (a marker of neuroendocrine tumors) is one of the most important indicators in the diagnosis of carcinoid tumors. (rezus.lt)
Granins1
- It belongs to the family of granins that includes chromogranin B, chromogranin C, and secretogranin II. (medscape.com)
Serum3
- Chromogranin A can be either measured in the serum or detected by immunohistochemistry in a tissue specimen. (medscape.com)
- Serum chromogranin A can be elevated in other situations and conditions, including chronic proton-pump inhibitors use, renal failure, liver failure, heart failure, rheumatoid arthritis, inflammatory bowel disease, and hypertension. (medscape.com)
- Clearance of an automated immunoassay allows practices to measure chromogranin A concentration in human serum, thereby tracking disease progression in those with gastroenteropancreatic neuroendocrine tumors. (cancernetwork.com)
Protein2
- In humans, chromogranin A protein is encoded by the CHGA gene. (wikipedia.org)
- Generation of NOD mice lacking the chromogranin A protein (NOD.ChgA−/−) completely nullified the autoreactivity of the BDC2.5 T cell and conferred protection from diabetes onset. (wustl.edu)
ChgA2
- Examples of cells producing chromogranin A (ChgA) are chromaffin cells of the adrenal medulla, paraganglia, enterochromaffin-like cells and beta cells of the pancreas. (wikipedia.org)
- Here we revisited the NOD.ChgA−/− mice and found that their lack of diabetes development may not be solely explained by the absence of chromogranin A reactivity. (wustl.edu)
Antigen1
- Therefore, the global deficiency of chromogranin A impairs recognition of the major diabetogenic antigen insulin, leading to broadly impaired autoimmune responses controlled by multiple regulatory mechanisms. (wustl.edu)
Peptides2
- Chromogranin A is the precursor to several functional peptides including vasostatin-1, vasostatin-2, pancreastatin, catestatin and parastatin. (wikipedia.org)
- Chromogranin A contains multiple cleavage sites, which undergo a tissue-specific proteolytic process, leading to the production of many biologically active peptides including vasostatin I, vasostatin II, pancreastatin, catestatin, parastatin, and serpinin. (medscape.com)
Biomarker1
- Chromogranin A: a useful biomarker in castration-resistant prostate cancer. (bvsalud.org)
Marker2
Prostate1
- Further data were obtained from PubMed and Embase databases by searches using keywords , including chromogranin A and prostate cancer . (bvsalud.org)
Conjunction1
- Chromogranin A can be used, in conjunction with other testing modalities, as a diagnostic tool, but caution is advised since it is elevated in many other conditions. (medscape.com)
Amino1
- There are considerable differences in the amino acid composition between different species' chromogranin A . Commercial assays for measuring human CGA can usually not be used for measuring CGA in samples from other animals. (wikipedia.org)
Patients1
- Chromogranin A, Ki-67 index and IGF-related genes in patients with neuroendocrine tumors. (medscape.com)
Produce1
- Chromogranin A is cleaved by an endogenous prohormone convertase to produce several peptide fragments. (wikipedia.org)
Chromaffin cells2
- Examples of cells producing chromogranin A (ChgA) are chromaffin cells of the adrenal medulla, paraganglia, enterochromaffin-like cells and beta cells of the pancreas. (wikipedia.org)
- Adrenocortical and adrenomedullary cells were characterized by double-immunohistochemistry with anti-17 alpha hydroxylase (cortical cells) and anti-chromogranin A (chromaffin cells). (biopsychiatry.com)
Serum chromogranin7
- However, the reference ranges for serum chromogranin A vary widely with the techniques used. (medscape.com)
- Serum chromogranin A can be elevated in other situations and conditions, including chronic proton-pump inhibitors use, renal failure, liver failure, heart failure, rheumatoid arthritis, inflammatory bowel disease, and hypertension. (medscape.com)
- The goal of this study is to explore constituents that influence serum chromogranin A levels in autoimmune gastritis patients. (turkjgastroenterol.org)
- One hundred and eighty-eight autoimmune gastritis patients and 20 patients with type I gastric carcinoid tumors were analyzed retrospectively and compared to 110 functional dyspepsia patients in terms of factors that might affect serum chromogranin A levels. (turkjgastroenterol.org)
- The presence of corpus atrophy (p=0.026, OR: 5.03, CI 95%: 1.21-20.88, β=1.61) and presence of enterochromaffin-like cell hyperplasia (p=0.017, OR: 6.59, CI 95%: 1.4-31.08, β=1.88) were found as risk factors associated with serum chromogranin A level. (turkjgastroenterol.org)
- Factors influencing raised serum chromogranin A levels in autoimmune gastritis were the presence of ECL cell hyperplasia and serum gastrin levels. (turkjgastroenterol.org)
- Serum chromogranin A levels maybe helpful in distinguishing autoimmune gastritis patients and gastric carcinoid type I from the control group, but not useful in the differentiation of individuals with autoimmune gastritis from patients with gastric carcinoids. (turkjgastroenterol.org)
Enzyme Immunoassay1
- We used enzyme immunoassay based on Chromogranin A NEOLISA (Euro Diagnostica) and Serotonin ELISA (IBL International GmbH) test systems. (almclinmed.ru)
Serotonin1
- However, there are still no clear criteria for the assessment of clinically significant abnormalities of the main NET biomarkers chromogranin A (CgA) and serotonin. (almclinmed.ru)
Adrenal medulla1
- Double immunostained cross-section of a human adrenal gland for 17-α-Hydroxylase and chromogranin A. zM = adrenal medulla, zR = zona reticularis, zF = zona fasciculata, zG = zona glomerulosa, Caps = adrenal capsule. (endotext.org)
Assays1
- There are considerable differences in the amino acid composition between different species' chromogranin A . Commercial assays for measuring human CGA can usually not be used for measuring CGA in samples from other animals. (wikipedia.org)
Gastrin1
- The GI ordered the chromogranin and gastrin prior to these tests based on my symptoms and family history. (cancer.org)
Diagnostic5
- Context Chromogranin A (Cg A) is the best available diagnostic marker for neuroendocrine neoplasms (NENs). (medscape.com)
- Chromogranin A can be used, in conjunction with other testing modalities, as a diagnostic tool, but caution is advised since it is elevated in many other conditions. (medscape.com)
- Chromogranin A is a reliable serum diagnostic biomarker for pancreatic neuroendocrine tumors but not for insulinomas. (medscape.com)
- This study was designed to assess diagnostic utility of chromogranin A (CgA) alone or in combination with NMN in patients with PHEO/PGL related to mutations in SDHB and SDHD. (nih.gov)
- Increased chromogranin A (CgA) levels may interfere with diagnostic investigations for neuroendocrine tumors, temporarily stop esomeprazole magnesium delayed-release capsules at least 14 days before assessing CgA levels. (nih.gov)
Neuroendocrine cells2
- chromogranin-A (CgA)+ Pulmonary neuroendocrine cells account for 0.41% of all epithelial cells in the conducting airway, but are absent from the alveoli. (wikipedia.org)
- Chromogranin A is a protein released by neuroendocrine cells. (citylab.bg)
CHGB3
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Chromogranin B (CHGB) in serum, plasma, tissue homogenates and other biological fluids. (thescientistconnect.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rat Chromogranin B (CHGB) in samples from Serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species. (thescientistconnect.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Human Chromogranin B (CHGB) in samples from serum, plasma, tissue homogenates or other biological fluids. (thescientistconnect.com)
Molecular1
- mRNA expression and protein localization for molecular markers of neuroendocrine differentiation, including chromogranin A and neuropilin-1, were elevated in prostate tumors compared to tumor-free ventral prostates, regardless of Ahr genotype or age. (nih.gov)
Gene2
Immunohistochemistry1
- Chromogranin A can be either measured in the serum or detected by immunohistochemistry in a tissue specimen. (medscape.com)
Urine1
- I hope my GI orders more blood/urine now that the chromogranin is slightly high, did you have other tests done? (cancer.org)
Granules1
- Immunohistochemically, the tumor cells were positive for cytokeratin (CK) 7 and CD56 and were negative for CK20, synaptophysin, and chromogranin A. Membrane-bound dense-core granules were detected on ultrastructural study. (karger.com)
Measurement3
- Calcitonin and chromogranin A were stable (within the measurement uncertainty) for at least 7 days when stored at -20°C. Thyroglobulin and anti-thyroglobulin antibody concentrations were stable for at least 7 days at all three temperatures (room temperature, 4°C, -20°C) investigated. (nih.gov)
- Stable levels was defined as remaining within the measurement uncertainty of the assay, which was 8.2% for calcitonin, 6.9% for chromogranin A, 6.9% for thyroglobulin and 16.4% for anti-thyroglobulin antibodies. (nih.gov)
- Description: A competitive ELISA for quantitative measurement of Monkey Chromogranin A in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (cd1234567890.com)
Levels2
- This paper compared levels of calcitonin, chromogranin A, thyroglobulin and anti-thyroglobulin antibodies in serum before and after storage at room temperature, 4°C and -20°C for 1, 3 5 and 7 days. (nih.gov)
- Levels of calcitonin, thyroglobulin and anti-thyroglobulin antibodies were quantified using a Siemens Immulite 2000 analyzer and chromogranin A levels were assayed using a Thermo-Fisher Scientific Kryptor Compact analyzer. (nih.gov)
Tissue1
- Description: Enzyme-linked immunosorbent assay kit for quantification of Rat Chromogranin-A in samples from serum, plasma, tissue homogenates and other biological fluids. (cd1234567890.com)
Blood1
- Glinicki P, Jeske W. Chromogranin A (CgA)--the influence of various factors in vivo and in vitro, and existing disorders on its concentration in blood. (medscape.com)
References1
- See chromogranin A GeneRIFs for references. (wikipedia.org)
Level1
- Chromogranin A is also elevated in autoimmune gastritis patients with a different level of increase in each patient. (turkjgastroenterol.org)