Comparative accuracy of two veterinary-calibrated point-of-care glucometres for measurement of blood glucose concentration in dogs.

OBJECTIVES: To investigate and compare the accuracy of two veterinary portable blood glucose metres (AccuTell; AccubioTech; and AlphaTrak2; Abbott Laboratories). MATERIALS AND METHODS: One hundred twenty venous blood samples were obtained for immediate whole blood glucose concentration measurement using two portable blood glucose metres designed for use in dogs. Plasma glucose concentration was measured by a laboratory analyser using a hexokinase reaction method. Packed cell volume was measured for each sample. Linear regression analysis was performed and Bland-Altman plots constructed with International Standards Organisation 15197:2013 standards applied to assess relationship and agreement between results of portable blood glucose metres and laboratory analyser methods, respectively. Clarke's error grid analysis was used to assess clinical accuracy and usefulness. RESULTS: The AccuTell and the AlphaTrak2 had mean differences of -0.69 ± 0.70 mmol/L (bias ±sd) and -1.09 ± 1.22 mmol/L (bias ± sd) with the reference analyser, respectively. Eighty-eight of 120 (73.3%) samples for the AccuTell, and 73 of 120 (60.8%) samples for the AlphaTrak2 were plotted in the zone of the error grid analysis that indicated less clinical risk of misdiagnosis of glucose status. Neither device fulfilled the International Standards Organisation 15197:2013 standards for system accuracy. A statistically significant effect of packed cell volume was identified on the difference between blood glucose concentration obtained by the AlphaTrak2 and the hexokinase reaction method, but not for the AccuTell. CLINICAL SIGNIFICANCE: Both devices do not meet International Standards Organisation 15197:2013 standards. Users should expect 95% of the samples measured with the AccuTell to be between -0.7 and +2.1 mmol/L higher than actual values, and 95% of the samples measured with the AlphaTrak2 to be between -1.3 and +3.5 mmol/L higher than actual values.

The solution structure of the C-terminal domain of the Mu B transposition protein.

Mu B is one of four proteins required for the strand transfer step of bacteriophage Mu DNA transposition and the only one where no high resolution structural data is available. Structural work on Mu B has been hampered primarily by solubility problems and its tendency to aggregate. We have overcome this problem by determination of the three-dimensional structure of the C-terminal domain of Mu B (B(223-312)) in 1.5 M NaCl using NMR spectroscopic methods. The structure of Mu B(223-312) comprises four helices (backbone r.m.s.d. 0.46 A) arranged in a loosely packed bundle and resembles that of the N-terminal region of the replication helicase, DnaB. This structural motif is likely to be involved in the inter-domainal regulation of ATPase activity for both Mu A and DnaB. The approach described here for structural determination in high salt may be generally applicable for proteins that do not crystallize and that are plagued by solubility problems at low ionic strength.

A phosphorylation site in the ftz homeodomain is required for activity.

The Drosophila homeodomain-containing protein Fushi tarazu (Ftz) is expressed sequentially in the embryo, first in alternate segments, then in specific neuroblasts and neurons in the central nervous system, and finally in parts of the gut. During these different developmental stages, the protein is heavily phosphorylated on different subsets of Ser and Thr residues. This stage-specific phosphorylation suggests possible roles for signal transduction pathways in directing tissue-specific Ftz activities. Here we show that one of the Ftz phosphorylation sites, T263 in the N-terminus of the Ftz homeodomain, is phosphorylated in vitro by Drosophila embryo extracts and protein kinase A. In the embryo, mutagenesis of this site to the non-phosphorylatable residue Ala resulted in loss of ftz-dependent segments. Conversely, substitution of T263 with Asp, which is also non-phosphorylatable, but which successfully mimics phosphorylated residues in a number of proteins, rescued the mutant phenotype. This suggests that T263 is in the phosphorylated state when functioning normally in vivo. We also demonstrate that the T263 substitutions of Ala and Asp do not affect Ftz DNA-binding activity in vitro, nor do they affect stability or transcriptional activity in transfected S2 cells. This suggests that T263 phosphorylation is most likely required for a homeodomain-mediated interaction with an embryonically expressed protein.

Osteomyelitis due to Pseudallescheria boydii.

This report describes an unusual opportunistic fungal infection in an immunocompetent young man who had no cutaneous involvement and whose infection was diagnosed 6 years after an accident. The unusual clinical presentation and difficulties in making a correct diagnosis are discussed and prophylactic antifungal chemotherapy is suggested.

Hodgkin's disease of the endometrium.

We report a case of Hodgkin's disease of the endometrium. The endometrial stroma is replaced by a polymorphic cellular infiltrate in which Reed-Sternberg cells are seen. The patient also has a history of stage IV-B Hodgkin's disease that was diagnosed and treated three years earlier. To our knowledge, Hodgkin's disease of the endometrium has not been described.