Atypical presentations of intracranial dysgerminoma mimicking central nervous system inflammatory or demyelinating disease
CANADIAN JOURNAL OF OPHTHALMOLOGY-JOURNAL CANADIEN D OPHTALMOLOGIE
Authors: Zhou, You; Vickers, Aroucha; Chan, Noel C. Y.; Chan, Carmen K. M.; Urias, Elizabeth; Lee, Andrew G.; Lo, Sherman S. M.; Trivedi, Darshan
Abstract
Objectives: The aim of this study is to report a case series of atypical presentations of intracranial dysgerminoma in which the diagnosis was delayed due to clinical and radiographic findings initially suggestive of CNS inflammatory or demyelinating diseases, such as MS. Methods: This study is a case series detailing the history, clinical presentations, radiographic and laboratory results, and management of three patients with biopsy-proven intracranial dysgerminoma. Results: All three patients demonstrated hyperintense lesions on MRI that were more suggestive of demyelinating or inflammatory diseases, including lesions involving the midbrain and corpus callosum. All three patients were serum positive for oligoclonal bands and negative for both AFP and beta-hCG (these two markers are commonly seen in dysgerminoma cases). One case involved a steroid-responsive tumor whereas the other two cases either did not respond to steroids or steroids were withheld due to uncertainty of etiology. Following biopsy, all three results were consistent with dysgerminoma. Natural food-derived hypoglycemic molecules hold potential for decreasing the postprandial increase in blood glucose and preventing type 2 diabetes along with its associated comorbidities. This study investigated the inhibitory effects of Lonicera caerulea berry polyphenols (LCBP) on the activity of a-amylase and the involved mechanisms. We used an enzyme inhibition assay, enzyme kinetics analysis, fluorescence quenching, and molecular docking to assess the effects of LCBP and its primary constituents. LCBP significantly inhibited the activity of a-amylase (IC50 301.5 pg/mL) and exhibited a higher inhibitory effect than acarbose, a positive control for carbohydrate digestion. The enzyme kinetics and Lineweaver - Burk plot analyses revealed a reversible competitive inhibition of a-amylase activity by LCBP and its main constituent components cyanidin-3-glucoside (C-3-G), catechins, and chlorogenic acid (CA). Fluorescence quenching experiments revealed that LCBP exerted a dose-dependent quenching effect on a-amylase and produced an emission wavelength redshift due to static quenching. The computer simulation-assisted molecular docking study showed that the binding of C-3-G, catechins, and CA disrupts enzyme conformation, while the formation of the polyphenol-enzyme complex inhibits enzyme activity. Together, these results suggest that LCBP effectively reduces postprandial hyperglycemia and type 2 diabetes and thus, exhibits potential for application as a functional food additive.
On the Electrochemical Detection of Alpha-Fetoprotein Using Aptamers: DNA Isothermal Amplification Strategies to Improve the Performance of Weak Aptamers
BIOSENSORS-BASEL
Authors: Lorenzo-Gomez, Ramon; Gonzalez-Robles, Daniel; Miranda-Castro, Rebeca; de-los-Santos-alvarez, Noemi; Lobo-Castanon, Maria Jesus
Abstract
Affinity characterization is essential to develop reliable aptamers for tumor biomarker detection. For alpha-fetoprotein (AFP), a biomarker of hepatocellular carcinoma (HCC), two DNA aptamers were described with very different affinity. In this work, we estimate the dissociation constant of both of them by means of a direct assay on magnetic beads modified with AFP and electrochemical detection on carbon screen-printed electrodes (SPCE). Unlike previous works, both aptamers showed similar dissociation constant (K-d) values, in the sub mu M range. In order to improve the performance of these aptamers, we proposed the isothermal amplification of the aptamers by both terminal deoxynucleotidyl transferase (TdT) and rolling circle amplification (RCA). Both DNA amplifications improved the sensitivity and also the apparent binding constants from 713 nM to 189 nM for the short aptamer and from 526 nM to 32 nM for the long aptamer. This improvement depends on the true affinity of the binding pair, which ultimately limits the analytical usefulness.