scholarly journals Promising immunohistochemical and circulating markers of insulinoma

2020 ◽  
Vol 14 (1) ◽  
pp. 14-21
Author(s):  
Marina Yu. Yukina ◽  
Liliya S. Selivanova ◽  
Nurana F. Nuralieva ◽  
Ekaterina A. Troshina ◽  
Natalya S. Izmailova ◽  
...  
Keyword(s):  
Pancreatic Neuroendocrine Tumor ◽  
Predictive Biomarker ◽  
Secretory Protein ◽  
Melatonin Receptors ◽  
Chromogranin B ◽  
Primary Methods ◽  
Circulating Markers ◽  
Glucagon Like Peptide 1 ◽  
Secretory Products

Insulinoma is the most common functioning pancreatic neuroendocrine tumor. The review examines the currently used immunohistochemical and circulating markers for its diagnosis, and discusses the sensitivity and specificity of these parameters. At the same time, the relevance of searching for new biochemical indicators of the presence of insulinoma and its characteristics, as well as studying the mechanisms of tumor growth and hormonal hypersecretion is emphasized. One of the primary methods for solving these problems is immunohistochemical testing with the determination of circulating markers. The results of recent studies of alternative secretory products, in particular, cocaine - and amphetamine - regulated transcript (CART), chromogranin B, and neuroendocrine secretory protein 55 (NESP55) are presented. In addition, the question of expression of various receptors in the insulinoma tissue is considered, including in the context of determining molecular targets for its visualization or radiotherapy. In particular, the expression of receptors for glucagon-like peptide 1 in the tumor tissue is characterized. The possible role of melatonin receptors MT1 (MTNR1a) and MT2 (MTNR1b) in the pathogenesis of insulinoma is clarified. The article also discusses the possible use of tumor protein D52 (TPD52) as a new predictive biomarker for the differential diagnosis of benign and malignant insulinoma.

Interaction of calcium with porcine adrenal chromogranin A (secretory protein-I) and chromogranin B (secretogranin I)

1989 ◽  
Vol 257 (2) ◽  
pp. E247-E254 ◽  
Author(s):  
S. U. Gorr ◽  
J. Shioi ◽  
D. V. Cohn
Keyword(s):  
Chromogranin A ◽  
Secretory Granules ◽  
Extracellular Fluid ◽  
Secretory Protein ◽  
Secretory Proteins ◽  
Chromogranin B ◽  
Secretory Products ◽  
Adrenal Chromaffin ◽  
Secretogranin I

Secretory granules of endocrine cells contain one or more of the acidic secretory proteins chromogranin A (secretory protein-I), chromogranin B (secretogranin I), and secretogranin II (chromogranin C). It has been proposed that these proteins play a role in the packaging of secretory products. In the present study, lysates of purified porcine adrenal chromaffin granules containing chromogranins A and B and a putative chromogranin B fragment bound calcium and formed aggregates in the presence of 10–20 mM calcium at pH 5–6 and at 100 mM or less KCl, NaCl, or norepinephrine. The precipitates contained virtually all of the chromogranin B and the chromogranin B fragment and about one-third of the chromogranin A. The aggregates did not form or were dissociated at the pH and salt concentration of the extracellular fluid. Calcium precipitated purified chromogranin A and chromogranin B from pure solution to the same extent as from the granule lysates. Parathormone, added to the lysates, was incorporated in the precipitates, whereas the acidic secretory protein ovalbumin and norepinephrine were not. These findings suggest that secretory protein-I and secretogranin can exist in situ as aggregates that may include selected secretory products.

Characterization of excretory–secretory products from protoscoleces of Echinococcus granulosus and evaluation of their potential for immunodiagnosis of human cystic echinococcosis

Parasitology ◽  
2004 ◽  
Vol 129 (3) ◽  
pp. 371-378 ◽  
Author(s):  
D. CARMENA ◽  
J. MARTÍNEZ ◽  
A. BENITO ◽  
J. A. GUISANTES
Keyword(s):  
Echinococcus Granulosus ◽  
Cystic Echinococcosis ◽  
Secretory Protein ◽  
Major Protein ◽  
Healthy Donors ◽  
Secretory Products ◽  
Protein Components ◽  
Human Cystic Echinococcosis

This study describes, for the first time, the characterization of excretory–secretory antigens (ES-Ag) from Echinococcus granulosus protoscoleces, evaluating their usefulness in the immunodiagnosis of human cystic echinococcosis. ES-Ag were obtained from the first 50 h maintenance of protoscoleces in vitro. This preparation contained over 20 major protein components which could be distinguished by 1-dimensional SDS–PAGE with apparent masses between 9 and 300 kDa. The culture of of protoscoleces from liver produced a greater variety of excretory–secretory protein components than those from lung. Determination of enzymatic activities of secreted proteins revealed the presence of phosphatases, lipases and glucosidases, but no proteases. These findings were compared to those obtained from somatic extracts of protoscoleces and hydatid cyst fluid products. Immunochemical characterization was performed by immunoblotting with sera from individuals infected by cystic echinococcosis (n=15), non-hydatidic parasitoses (n=19), various liver diseases (n=24), lung neoplasia (n=16), and healthy donors (n=18). Antigens with apparent masses of 89, 74, 47/50, 32, and 20 kDa showed specificity for immunodiagnosis of human hydatidosis. The 89 and 74 kDa components corresponded to antigens not yet described in E. granulosus, whereas proteins of 41–43 kDa and 91–95 kDa were recognized by the majority of the non-hydatid sera studied.

scholarly journals An antibody against secretogranin I (chromogranin B) is packaged into secretory granules.

1989 ◽  
Vol 109 (1) ◽  
pp. 17-34 ◽  
Author(s):  
P Rosa ◽  
U Weiss ◽  
R Pepperkok ◽  
W Ansorge ◽  
C Niehrs ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Secretory Granules ◽  
Intracellular Localization ◽  
Secretory Protein ◽  
Secretory Proteins ◽  
Chromogranin B ◽  
Double Labeling ◽  
Protein Protein Interaction ◽  
And Function ◽  
Secretogranin I

We have investigated the sorting and packaging of secretory proteins into secretory granules by an immunological approach. An mAb against secretogranin I (chromogranin B), a secretory protein costored with various peptide hormones and neuropeptides in secretory granules of many endocrine cells and neurons, was expressed by microinjection of its mRNA into the secretogranin I-producing cell line PC12. An mAb against the G protein of vesicular stomatitis virus--i.e., against an antigen not present in PC12 cells--was expressed as a control. The intracellular localization and the secretion of the antibodies was studied by double-labeling immunofluorescence using the conventional and the confocal microscope, as well as by pulse-chase experiments. The secretogranin I antibody, like the control antibody, was transported along the secretory pathway to the Golgi complex. However, in contrast to the control antibody, which was secreted via the constitutive pathway, the secretogranin I antibody formed an immunocomplex with secretogranin I, was packaged into secretory granules, and was released by regulated exocytosis. Our results show that a constitutive secretory protein, unaltered by genetic engineering, can be diverted to the regulated pathway of secretion by its protein-protein interaction with a regulated secretory protein. The data also provide the basis for immunologically studying the role of luminally exposed protein domains in the biogenesis and function of regulated secretory vesicles.

scholarly journals Genome-Wide Analysis of Sterol-Lipid Storage and Trafficking in Saccharomyces cerevisiae

2007 ◽  
Vol 7 (2) ◽  
pp. 401-414 ◽  
Author(s):  
Weihua Fei ◽  
Gabriel Alfaro ◽  
Baby-Periyanayaki Muthusamy ◽  
Zachary Klaassen ◽  
Todd R. Graham ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Neutral Lipid ◽  
Lipid Synthesis ◽  
Secretory Protein ◽  
Lipid Storage ◽  
Protein Glycosylation ◽  
Particle Assembly ◽  
Genome Wide ◽  
And Storage

ABSTRACT The pandemic of lipid-related disease necessitates a determination of how cholesterol and other lipids are transported and stored within cells. The first step in this determination is the identification of the genes involved in these transport and storage processes. Using genome-wide screens, we identified 56 yeast (Saccharomyces cerevisiae) genes involved in sterol-lipid biosynthesis, intracellular trafficking, and/or neutral-lipid storage. Direct biochemical and cytological examination of mutant cells revealed an unanticipated link between secretory protein glycosylation and triacylglycerol (TAG)/steryl ester (SE) synthesis for the storage of lipids. Together with the analysis of other deletion mutants, these results suggested at least two distinct events for the biogenesis of lipid storage particles: a step affecting neutral-lipid synthesis, generating the lipid core of storage particles, and another step for particle assembly. In addition to the lipid storage mutants, we identified mutations that affect the localization of unesterified sterols, which are normally concentrated in the plasma membrane. These findings implicated phospholipase C and the protein phosphatase Ptc1p in the regulation of sterol distribution within cells. This study identified novel sterol-related genes that define several distinct processes maintaining sterol homeostasis.

scholarly journals Characterization of the rat salivary-gland B1-immunoreactive proteins

1998 ◽  
Vol 330 (1) ◽  
pp. 437-444 ◽  
Author(s):  
Lily MIRELS ◽  
J. Abigail MIRANDA ◽  
D. William BALL
Keyword(s):  
Submandibular Gland ◽  
Protein A ◽  
Secretory Protein ◽  
Cdna Clones ◽  
Parotid Glands ◽  
Gene Encoding ◽  
Adult Rat ◽  
Related Clone ◽  
Secretory Products

The B1-immunoreactive proteins (B1-IPs) are major secretory products of rat submandibular gland acinar-cell progenitors, and are also produced by neonatal and adult rat sublingual and parotid glands. In order to characterize the B1-IPs, we have previously isolated cDNA clones encoding rat parotid secretory protein (PSP; the predominant parotid B1-IP) and the related clone ZZ3, which is developmentally regulated in the neonatal submandibular gland. The remainder of the B1-IPs were uncharacterized. This report demonstrates that all of the B1-IPs are derived from the PSP and ZZ3 transcripts. Molecular cloning and Western-blot analyses using PSP- and ZZ3-specific antisera show that, of the B1-IPs, only PSP and neonatal submandibular gland protein A (SMGA) are products of the Psp gene. This finding corrects our previous assertion that SMGA is derived from ZZ3. Neonatal submandibular gland proteins B1 and B2, as well as apparent Mr 26000-28000 and Mr 18000-20000 forms in submandibular, sublingual and parotid glands, are derived from the gene encoding ZZ3 by differential N-glycosylation and by proteolytic cleavage. The apparent Mr 18000-20000 proteolytic products are significant in secretion product collected in vitro, but rare in gland homogenate and submandibular/sublingual saliva. The gene encoding ZZ3 has been named Smgb. Psp and Smgb are regulated similarly in the developing submandibular gland, but differently in the sublingual and parotid glands. The expression pattern of Psp is conserved between rat and mouse. However, no evidence for proteins derived from an Smgb-like gene was observed in neonatal mouse submandibular or sublingual glands.

scholarly journals Red Cell Distribution Width: a Novel Predictive Biomarker for Stroke Risk After Transient Ischemic Attack

2021 ◽  
Author(s):  
Ke-Hang Xie ◽  
Ling-Ling Liu ◽  
Yun-Ru Liang ◽  
Chu-Yin Su ◽  
Run-Ni Liu ◽  
...  
Keyword(s):  
Transient Ischemic Attack ◽  
Complete Blood Count ◽  
Predictive Biomarker ◽  
Cell Distribution ◽  
Distribution Width ◽  
The Mean ◽  
Stroke Center ◽  
Ischemic Attack ◽  
New Onset

Abstract Objective: Predicting the prognosis of transient ischemic attack (TIA) is difficult for many frontline clinicians. The purpose of this study was to determine whether subsequent stroke in TIA patients can be predicted via the red blood cell distribution width(RDW).Material and methods: A total of 309 consecutive age- and sex-matched patients with new onset TIA, in our stroke center, were enrolled over the period studied. The patients were divided into two groups :103 TIA patients and 206 patients who had a stroke within 7 days after TIA. Complete blood count, biochemical parameters and brain imaging were performed in all patients. Results: The mean RDW values of patients with stroke after TIA were significantly higher than patients with TIA (12.84 ±1.19, 13.35 ±1.59, p= 0.001). In a multivariate model, RDW was independently associated with stroke after TIA (OR=2.52, 95% CI 1.46 to 3.35, P= 0.002). We also found that the higher levels of RDW, the earlier the stroke onset (p=0.024). Compared to ABCD2 score, the diagnostic power of RDW in the differentiation of patients with stroke after TIA is better (AUCs:0.613vs0.731, p= 0.015). When an RDW cut-off value of 13.95% is accepted for differentiating patients with stroke after TIA from TIA, the sensitivity and specificity were 73.7% and 74.3%, respectively.Conclusions: The early determination of RDW is a promising, rapid, easy and inexpensive biomarker to predict the subsequent stroke in TIA patients.

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