12 research outputs found
Amiodarone-induced Loculated Pleural Effusion Without Pulmonary Parenchymal Involvement: a Case Report and Literature Review
Amiodarone is an extremely effective antiarrhythmic drug that is known to cause many adverse effects such as pulmonary, thyroid, and liver toxicities. Of these, pulmonary toxicity is most serious. Pulmonary toxicity can present as interstitial pneumonitis, organizing pneumonia, pulmonary nodules and masses, and very rarely pleural effusions. We present a case of a 73-year-old male who presented with progressive exertional dyspnea, nonproductive cough, generalized fatigue, and weakness. He was found to have multiorgan toxicity secondary to long-term treatment with high doses of amiodarone. This case illustrates that amiodarone may cause toxicity involving multiple organs simultaneously in patients receiving long-term therapy and represents the first reported case of amiodarone-induced loculated pleural effusion without associated lung parenchymal involvement
BluePort: A Platform to Study the Eosinophilic Response of Mice to the Bite of a Vector of Leishmania Parasites, Lutzomyia longipalpis Sand Flies
transmission in residents of endemic areas has been attributed to the acquisition of immunity to sand fly salivary proteins. One theoretical way to accelerate the acquisition of this immunity is to increase the density of antigen-presenting cells at the sand fly bite site. Here we describe a novel tissue platform that can be used for this purpose. sand flies. Results presented indicate that a shift in the inflammatory response, from neutrophilic to eosinophilic, is the main histopathological feature associated with the immunity acquired through repeated exposure to the bite of sand flies, and that the BluePort tissue compartment could be used to accelerate this process. In addition, changes observed inside the BluePort parenchyma indicate that it could be used to study complex immunobiological processes, and to develop ectopic secondary lymphoid structures.Understanding the characteristics of the dermal response to the bite of sand flies is a critical element of strategies to control leishmaniasis using vaccines that target salivary proteins. Finding that dermal eosinophilia is such a prominent component of the anti-salivary immunity induced by repeated exposure to sand fly bites raises one important consideration: how to avoid the immunological conflict derived from a protective Th2-driven immunity directed to sand fly saliva with a protective Th1-driven immunity directed to the parasite. The BluePort platform is an ideal tool to address experimentally this conundrum
Fast and Efficient Online Release of N‑Glycans from Glycoproteins Facilitating Liquid Chromatography–Tandem Mass Spectrometry Glycomic Profiling
A novel online enzyme reactor incorporating peptide-N-glycosidase
F (PNGase F) on a monolithic polymer support has been developed to
allow the rapid simultaneous release of both neutral and acidic N-linked
glycans from glycoproteins. The PNGase F monolithic reactor was fabricated
in a fused silica using glycidyl methacrylate-<i>co</i>-ethylene
dimethacrylate polymer. The reactor was coupled to a C8 trap and a
porous graphitic carbon (PGC) HPLC-chip. This arrangement was interfaced
to an ion trap mass spectrometer for liquid chromatography–mass
spectrometry (LC–MS) and liquid chromatography–tandem
mass spectrometry (LC–MS/MS) analyses. The performance of the
PNGase F reactor was optimized using the MS signal for the disialylated
biantennary N-glycan derived from fetuin. Optimum conditions for glycan
release were attained at room temperature using a loading flow rate
of 2 ÎĽL/min and a reaction time of 6 min. The loading capacity
of the reactor was determined to be around 2 pmol of glycoprotein.
The online digestion and MS characterization experiments resulted
in sensitivities as high as 100 fmol of glycoprotein and 0.1 ÎĽL
of human blood serum. The enzyme reactor activity was also shown to
remain stable after 1 month of continuous use. Both small and large
glycoproteins as well as glycoproteins containing high-mannose glycans,
fucolsylated glycans, sialylated glycans, and hybrid structures were
studied. The model glycoproteins included ribonuclease B, fetuin,
α<sub>1</sub>-acid glycoprotein, immunoglobulin, and thyroglobulin.
All N-glycans associated with these model glycoproteins were detected
using the online PNGase F reactor setup