Puffer fish poisoning in Bangladesh: clinical and toxicological results from large outbreaks in 2008.

Poisoning after eating puffer fish containing highly lethal tetrodotoxin (TTX) is widespread in Asia. In 2008, naïve inland populations in Bangladesh were exposed to cheap puffer fish sold on markets. In three outbreaks, 141 patients with history of puffer fish consumption were hospitalized. Symptoms of poisoning included perioral paraesthesia, tingling over the entire body, nausea and vomiting, dizziness, headache, abdominal pain and muscular paralysis of the limbs. Seventeen patients (12%) died from rapidly developing respiratory arrest. Blood and urine samples from 38 patients were analyzed using a TTX-specific enzyme-linked immunoassay (ELISA). Medium to high TTX levels were detected (1.7-13.7 ng/ml) in the blood of 27 patients. TTX was below detection level (< 1.6 ng/ml) in 11 blood samples but the toxin was detected in urine. Ten patients had blood levels above 9 ng/ml and developed paralysis; seven of these died. The remaining patients recovered with supportive treatment. High concentrations of TTX and its analogues 4-epiTTX and 4,9-anhydroTTX were also found in cooked puffer fish by post-column liquid chromatography-fluorescence detection. To prevent future instances of puffer fish poisoning of this magnitude, measures should be implemented to increase awareness, to control markets and to establish toxicological testing. To improve the management of this and other poisoning in Bangladesh, facilities for life-saving assisted ventilation and related training of healthcare personnel are urgently needed at all levels of the health system.

Two brothers with X linked adrenoleukodystrophy.

In patients with Addison's disease, diagnosis of Adrenoleukodystrophy (ALD) is suggested by the abrupt development of neuropsychiatric symptoms, associated with Magnetic resonance imaging (MRI) confirmation of extensive, usually symmetric, white matter demyelinating lesion. In these two cases, diagnosis of ALD was strongly supported by symptoms, disease progression, MRI findings. The emergence of neuropsychiatric symptoms in a patient with a prior history of Addison's disease should prompt evaluation for this disorder. Early diagnosis of the disease is required for delaying the progression of the disease. Genetic counseling, carrier detection and antenatal diagnosis can reduce the incidence of this disease, which prognosis is grave in most of the cases.

Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analyzed using extended X-ray absorption fine structure (EXAFS).

The iron core of proteins in the ferritin family displays structural variations that include phosphate content as well as the number and the degree of ordering of the iron atoms. Earlier studies had shown that ferritin iron cores naturally high in phosphate, e.g., Azotobacter vinelandii (AV) ferritin (Fe:P ratio = 1:1.7), had decreased long-range order. Here, the influence of phosphate on the local structure around iron in ferritin cores is reported, comparing the EXAFS of AV ferritin, reconstituted ferritin [the protein coats of horse spleen ferritin mixed with Fe(II) with and without phosphate at pH 7] (Fe:P ratio = 1:0.25), and native horse spleen ferritin (Fe:P ratio = 1:0.125); reconstituted horse spleen ferritin without phosphate was indistinguishable from native horse spleen ferritin (HSF) in the analysis. In contrast, when the phosphate content was high in AV ferritin and horse spleen ferritin reconstituted with phosphate, the average iron atom had five to six phosphorus neighbors at 3.17 A. Moreover, the number of detectable iron neighbors was lower when phosphate was high or present during reconstitution (2-3 vs 5-6), and the interatomic distance was longer (3.50 vs 3.03 A), indicating that some phosphate bridges neighboring iron atoms. However, the decrease in the number of detectable iron-iron neighbors compared to HSF and the higher number of Fe-P interactions relative to Fe-Fe interactions suggest that some phosphate ligands were chain termini, or blocked crystal growth, and/or introduced defects which contributed both to the long-range disorder and to altered redox properties previously observed in AV ferritin.

A comparison of an undecairon(III) complex with the ferritin iron core.

The iron core of ferritin is comprised of up to 4,500 Fe(III) atoms as Fe2O3.nH2O, which is maintained in solution by a surrounding, spherical coat of protein. Organisms as diverse as bacteria and man use the ferritin iron-protein complex as a reservoir of stored iron for other essential proteins. To extend studies of the steps in polynuclear iron core formation, a recently characterized undecairon(III) oxo-hydroxo aggregate [Fe11 complex] (Gorun et al., J. Am. Chem. Soc. 109, 3337 [1987]) was examined by x-ray absorption spectroscopy as a model for an intermediate. The results, which are comparable to the previous x-ray diffraction studies, show near neighbors (Fe-O) at 1.90 A that are distinct from those in ferritin and a longer distance of 2.02 A. However, contributions from neighbors (Fe-C) known to exist at ca. 2.7 A were obscured by a highly ordered Fe-Fe interaction and were not detectable in the Fe11 complex in contrast to a previously characterized Fe(III) cluster bound to the protein coat. Of the two Fe-Fe interactions detectable in the Fe11 complex, the shortest, at 3.0 A is particularly interesting, occurring at the same distance as a full shell (CN = 6) in ferritin, but having fewer Fe neighbors (CN = 2-3) characteristic of an intermediate in core formation. The incomplete Fe-Fe shell is much more ordered than in ferritin, suggesting that the disorder in ferritin cores may be associated with the later steps of the core growth. Differences between the Fe11 complex and the full core of ferritin indicate the possibility of intermediates in ferritin iron formation that might be like Fe11.