Recognizing thyrotoxicosis in a patient with bipolar mania: a case report

<p>Abstract</p> <p>Background</p> <p>A thyroid stimulating hormone level is commonly measured in patients presenting with symptoms of mania in order to rule out an underlying general medical condition such as hyperthyroidism or thyrotoxicosis. Indeed, many cases have been reported in which a patient is initially treated for bipolar mania, but is later found to have a thyroid condition. Several case reports have noted the development of a thyroid condition in bipolar patients either on lithium maintenance treatment or recently on lithium treatment.</p> <p>Case presentation</p> <p>We review a case in which a patient with a long history of bipolar disorder presents with comorbid hyperthyroidism and bipolar mania after recent discontinuation of lithium treatment.</p> <p>Conclusion</p> <p>Physicians should consider a comorbid hyperthyroidism in bipolar manic patients only partially responsive to standard care treatment with a mood stabilizer and antipsychotic.</p

A portable reverse transcription recombinase polymerase amplification assay for rapid detection of foot-and-mouth disease virus

Foot-and-mouth disease (FMD) is a trans-boundary viral disease of livestock, which causes huge economic losses and constitutes a serious infectious threat for livestock farming worldwide. Early diagnosis of FMD helps to diminish its impact by adequate outbreak management. In this study, we describe the development of a real-time reverse transcription recombinase polymerase amplification (RT-RPA) assay for the detection of FMD virus (FMDV). The FMDV RT-RPA design targeted the 3D gene of FMDV and a 260 nt molecular RNA standard was used for assay validation. The RT-RPA assay was fast (4-10 minutes) and the analytical sensitivity was determined at 1436 RNA molecules detected by probit regression analysis. The FMDV RT-RPA assay detected RNA prepared from all seven FMDV serotypes but did not detect classical swine fever virus or swine vesicular disease virus. The FMDV RT-RPA assay was used in the field during the recent FMD outbreak in Egypt. In clinical samples, reverse transcription polymerase chain reaction (RT-PCR) and RT-RPA showed a diagnostic sensitivity of 100% and 98%, respectively. In conclusion, FMDV RT-RPA was quicker and much easier to handle in the field than real-time RT-PCR. Thus RT-RPA could be easily implemented to perform diagnostics at quarantine stations or farms for rapid spot-of-infection detection

Chymase-Dependent Generation of Angiotensin II from Angiotensin-(1-12) in Human Atrial Tissue

Since angiotensin-(1-12) [Ang-(1-12)] is a non-renin dependent alternate precursor for the generation of cardiac Ang peptides in rat tissue, we investigated the metabolism of Ang-(1-12) by plasma membranes (PM) isolated from human atrial appendage tissue from nine patients undergoing cardiac surgery for primary control of atrial fibrillation (MAZE surgical procedure). PM was incubated with highly purified 125I-Ang-(1-12) at 37°C for 1 h with or without renin-angiotensin system (RAS) inhibitors [lisinopril for angiotensin converting enzyme (ACE), SCH39370 for neprilysin (NEP), MLN-4760 for ACE2 and chymostatin for chymase; 50 µM each]. 125I-Ang peptide fractions were identified by HPLC coupled to an inline γ-detector. In the absence of all RAS inhibitor, 125I-Ang-(1-12) was converted into Ang I (2±2%), Ang II (69±21%), Ang-(1-7) (5±2%), and Ang-(1-4) (2±1%). In the absence of all RAS inhibitor, only 22±10% of 125I-Ang-(1-12) was unmetabolized, whereas, in the presence of the all RAS inhibitors, 98±7% of 125I-Ang-(1-12) remained intact. The relative contribution of selective inhibition of ACE and chymase enzyme showed that 125I-Ang-(1-12) was primarily converted into Ang II (65±18%) by chymase while its hydrolysis into Ang II by ACE was significantly lower or undetectable. The activity of individual enzyme was calculated based on the amount of Ang II formation. These results showed very high chymase-mediated Ang II formation (28±3.1 fmol×min−1×mg−1, n = 9) from 125I-Ang-(1-12) and very low or undetectable Ang II formation by ACE (1.1±0.2 fmol×min−1×mg−1). Paralleling these findings, these tissues showed significant content of chymase protein that by immunocytochemistry were primarily localized in atrial cardiac myocytes. In conclusion, we demonstrate for the first time in human cardiac tissue a dominant role of cardiac chymase in the formation of Ang II from Ang-(1-12)

Experimental foot-and-mouth disease virus infection in white tailed deer

White tailed deer (Odocoileus virginianus) were inoculated with foot-and-mouth disease virus (FMDV) O UKG 11/2001 and monitored for the development of clinical signs, histopathological changes and levels of virus replication. All FMDV-infected deer developed clinical signs starting at 2 days post inoculation and characterized by an increase in body temperature, increased salivation and lesions in the mouth and on the feet. Virus spread to various tissues was determined by quantifying the amount of FMDV RNA using quantitative reverse transcriptase polymerase chain reaction. Virus or viral antigen was also detected in tissues using traditional isolation techniques, enzyme linked immunosorbent assay and immunohistochemistry. Deer-to-cattle transmission of the virus was observed in this experimental setting; however, inoculated deer were not found to become carriers of FMDV

Comparative Effects of Selective Enzyme Inhibition on ¹²⁵I-Ang-(1-12) Metabolism by plasma membrane isolated from human atrial appendage tissues.

<p>HPLC of human ¹²⁵I-Ang-(1-12) metabolic products generated by plasma membrane (50 µg) isolated from human atrial appendage incubated with or without the presence of RAS inhibitors at 37°C for 60 min. Values are expressed as % (Mean ± SEM) of Ang peptides generated from ¹²⁵I-Ang-(1-12). <i>No RAS inhibitors group</i>: Only aminopeptidases inhibitors (amastatin & bestatin), carboxypeptidases inhibitor (benzyl succinate) and PCMB; <i>All RAS inhibitors group</i>: Above inhibitors+RAS inhibitors (lisinopril, SCH39370, MLN-4760 & chymostatin); <i>Minus RAS inhibitor group</i>: One of the RAS inhibitor (lisinopril or chymostatin) omitted at a time form the <i>All RAS inhibitors group</i>.. Results are the average of nine human samples (n = 9).</p><p>*Percent of ¹²⁵I-Ang-(1-12) parent control remained unmetabolized after 60 min incubated with plasma membrane (50 µg) at 37°C. ND = Not detected;</p>a<p>Significantly different (<i>P</i><0.05) vs. corresponding group of <i>All RAS inhibitors</i>.</p

Immunohistochemistry of human atrial tissue for chymase.

<p>Immunostaining of human atrial tissue using an Anti-Mast Cell chymase antibody (Abcam Inc., Cambridge, MA; Cat# ab2377) revealed high expression of chymase within atrial cardiac myocytes (A). Negative control without primary antibody shows no staining for chymase (B). <i>(Magnification 400; scale bar is 50 µm)</i>.</p

Diagnosis, drug treatment and clinical statement of human heart patients.

<p>Abbreviation: MV, mitral valve; AF, atrial fibrillation; CAD, Coronary artery disease; ASD, Atrial septal defect; CBS, Cardiac bypass surgery; ACE, angiotensin converting enzyme, and ARB, angiotensin receptor blocker.</p

Localization of Ang-(1-12) in human atrial tissue.

<p>Comparative adjacent sections of Ang-(1-12) immunoreactivity obtained from human atrial tissue with protein A purified polyclonal antibody produced by AnaSpec. A) Antibody (1∶2,000 dilution) blocked with 100 µmol/L of human Ang-(1-12) peptide, and B) Unblocked antibody (1∶2,000 dilution). <i>(Magnification 400; scale bar is 50 µm)</i>.</p