Plummer-Vinson Syndrome

A 37-year-old African American woman with no past medical history presented to the Emergency Department with a chief complaint of abdominal pain. She also reported associated fatigue and dysphagia. Over the past two months, she reported 40 Lbs. unintentional weight loss and decrease appetite. Her dysphagia primarily to solids, which also had been worsening over the past few weeks. She had no history of similar symptoms in the past. She was not on any medications. On admission, vital signs were stable. In the Emergency Department,. Hemoglobin on admission was 3.3 g/dL [11.9–15.1 g/dL] with a mean corpuscular volume of 61.1. Her serum iron on admission was 10 ug/dL [60–140 ug/dL], iron saturation was 2% [15–50%], and ferritin was 1.0 ng/mL [11.0–307 ng/mL]. Upon further questioning, the patient stated that she did not describe menorrhagia. She denied hematemesis, hematochezia, or melena. She was transfused with 3 units of packed red blood cells and was started on 1000 mg of IV iron dextran complex infusions. Gastroenterology was consulted, and the patient underwent esophagogastroduodenoscopy (EGD) and colonoscopy. Colonoscopy showed erythematous and edematous mucosa in the terminal ileum which was Biopsied. The EGD revealed a few intrinsic stenoses in the upper esophagus which were successfully dilated with savary. A pathology exam of the terminal ileum showed well differentiated neuroendocrine tumor. Given the clinical, laboratory, and endoscopic (as shown below) Esophageal web located in the upper esophagus. a diagnosis of Plummer-Vinson syndrome was made. Her dysphagia improved over the three days in the hospital after iron infusions and blood transfusions, and she was able to tolerate a regular diet. Approximately 2 months after her discharge, a follow-up phone call was made to the patient. She stated that she had been compliant with all her medications and her dysphagia had resolved. At the time of the phone call, she was tolerating a regular diet without any dietary restrictions.https://scholarlycommons.henryford.com/merf2020caserpt/1132/thumbnail.jp

The <em>MUC2 </em>Gene Product: Polymerisation and Post-Secretory Organisation—Current Models

\ua9 2024 by the authors.MUC2 mucin, the primary gel-forming component of intestinal mucus, is well researched and a model of polymerisation and post-secretory organisation has been published previously. Recently, several significant developments have been made which either introduce new ideas or challenge previous theories. New ideas include an overhaul of the MUC2 C-terminal globular structure which is proposed to harbour several previously unobserved domains, and include a site for an extra intermolecular disulphide bridge dimer between the cysteine 4379 of adjacent MUC2 C-termini. MUC2 polymers are also now thought to be secreted attached to the epithelial surface of goblet cells in the small intestine and removed following secretion via a metalloprotease meprin β-mediated cleavage of the von Willebrand D2 domain of the N-terminus. It remains unclear whether MUC2 forms intermolecular dimers, trimers, or both, at the N-termini during polymerisation, with several articles supporting either trimer or dimer formation. The presence of a firm inner mucus layer in the small intestine is similarly unclear. Considering this recent research, this review proposes an update to the previous model of MUC2 polymerisation and secretion, considers conflicting theories and data, and highlights the importance of this research to the understanding of MUC2 mucus layers in health and disease

TCT-126 Outcomes of Chronic Total Occlusion Percutaneous Coronary Intervention of the Left Anterior Descending Artery

Background: Improvement of left ventricular ejection fraction (LVEF) after chronic total occlusion (CTO) percutaneous coronary intervention (PCI) has been modest in prior studies. Methods: Our cohort included patients who underwent LAD CTO PCI at a single center (Henry Ford Hospital) from 2014 to 2021. We evaluate the change in LVEF after LAD CTO PCI using the paired t test in all patients, those with ischemic cardiomyopathy (CM), and those who underwent a viability test. Results: From December 2014 to February 2022, a total of 237 LAD CTO PCI procedures were performed at Henry Ford Hospital (proximal LAD: 56.6%). In-hospital MACE occurred in 13 patients (5.5%; death: 1.3%). Landmark analysis after discharge showed an overall survival of the cohort was 92.7% and MACE-free survival of 85.0% over a median follow-up of 2 years. The median baseline EF was 50% (IQR 35%-55%). Only 51 patients had reduced baseline LVEF (40% or less). After a median follow-up of 9.2 months (IQR 3-28.6 months), there was a significant improvement in LVEF after LAD CTO PCI (mean 10.9%, 95% CI 7.1%-14.8%, P \u3c 0.001). When limiting the analysis to patients who had ischemic cardiomyopathy, proximal LAD CTO PCI, and were on optimal medical therapy (n = 29), LVEF was significantly improved (mean increase of 14%, 95% CI 9.5-18.5%, P \u3c 0.001) after a median follow-up period of 6.2 months (3-29.5 months). Conclusion: LAD CTO PCI was associated with a significant 10% improvement in LVEF in ICM patients and was more pronounced (14% improvement) in those who had proximal LAD treated and were on optimal medical therapy. Categories: CORONARY: Complex and Higher Risk Procedures for Indicated Patients (CHIP

Carbohydrate-active enzymes from <em>Akkermansia</em> <em>muciniphila</em> break down mucin <em>O</em>-glycans to completion

\ua9 The Author(s) 2025. Akkermansia muciniphila is a human microbial symbiont residing in the mucosal layer of the large intestine. Its main carbon source is the highly heterogeneous mucin glycoprotein, and it uses an array of carbohydrate-active enzymes and sulfatases to access this complex energy source. Here we describe the biochemical characterization of 54 glycoside hydrolases, 11 sulfatases and 1 polysaccharide lyase from A. muciniphila to provide a holistic understanding of their carbohydrate-degrading activities. This was achieved using a variety of liquid chromatography techniques, mass spectrometry, enzyme kinetics and thin-layer chromatography. These results are supported with A. muciniphila growth and whole-cell assays. We find that these enzymes can act synergistically to degrade the O-glycans on the mucin polypeptide to completion, down to the core N-acetylgalactosaime. In addition, these enzymes can break down human breast milk oligosaccharide, ganglioside and globoside glycan structures, showing their capacity to target a variety of host glycans. These data provide a resource to understand the full degradative capability of the gut microbiome member A. muciniphila

Cyclin E as a potential therapeutic target in high grade serous ovarian cancer.

Cyclin E1 (CCNE1) gene amplification occurs in approximately 20% of ovarian high grade serous carcinoma (HGSC) and is associated with chemotherapy resistance and, in some studies, overall poor prognosis. The role of cyclin E1 in inducing S phase entry relies upon its interactions with cyclin dependent kinases (CDK), specifically CDK2. Therapies to target cyclin E1-related functions have centered on CDK inhibitors and proteasome inhibitors. While many studies have helped elucidate the functions and regulatory mechanisms of cyclin E1, further research utilizing cyclin E1 as a therapeutic target in ovarian cancer is warranted. This review serves to present the scientific background describing the role and function of cyclin E1 in cancer development and progression, to distinguish cyclin E1-amplified HGSC as a unique subset of ovarian cancer deserving of further therapeutic investigation, and to provide an updated overview on the studies which have utilized cyclin E1 as a target for therapy in ovarian cancer

Cyclin E as a potential therapeutic target in high grade serous ovarian cancer.

Cyclin E1 (CCNE1) gene amplification occurs in approximately 20% of ovarian high grade serous carcinoma (HGSC) and is associated with chemotherapy resistance and, in some studies, overall poor prognosis. The role of cyclin E1 in inducing S phase entry relies upon its interactions with cyclin dependent kinases (CDK), specifically CDK2. Therapies to target cyclin E1-related functions have centered on CDK inhibitors and proteasome inhibitors. While many studies have helped elucidate the functions and regulatory mechanisms of cyclin E1, further research utilizing cyclin E1 as a therapeutic target in ovarian cancer is warranted. This review serves to present the scientific background describing the role and function of cyclin E1 in cancer development and progression, to distinguish cyclin E1-amplified HGSC as a unique subset of ovarian cancer deserving of further therapeutic investigation, and to provide an updated overview on the studies which have utilized cyclin E1 as a target for therapy in ovarian cancer