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Objectives The objective of this study was to compare the effects of ketamine and alfaxalone on the application of a validated feline-specific multidimensional composite pain scale (UNESP-Botucatu MCPS). Methods In a prospective, randomized, blinded, crossover trial, 11 adult cats (weight 4.4 ± 0.6 kg) were given dexmedetomidine (15 μg/kg) and hydromorphone (0.05 mg/kg) with either alfaxalone (2 mg/kg) or ketamine (5 mg/kg) as a single intramuscular injection for the induction of general anesthesia. After orotracheal intubation, general anesthesia (without surgery) was maintained for 32 mins with isoflurane, followed by atipamezole. The following parameters were recorded at baseline, 1–8 h and 24 h post-extubation: pain (pain expression and psychomotor subscales) and sedation scale scores. Alfaxalone treatment injection sites were examined for inflammation at baseline, postinjection, and 8 h and 24 h post-extubation. Results Psychomotor scores were higher with ketamine at hours 1 (3.5 [0–5.0], P 0.05); one cat from each group crossed the analgesic intervention threshold. Sedation was greater with ketamine (1 [0–3], P = 0.02) than alfaxalone (0 [0–1]) 1 h post-extubation. No cats had visible inflammation at the injection sites at any time. Conclusions and relevance Ketamine has a confounding effect on the psychomotor subscale of the pain scale studied, which may lead to erroneous administration of rescue analgesia. In contrast, alfaxalone was not associated with significant increases in either pain subscale. These effects of ketamine should be considered when evaluating acute postoperative pain in cats.

Background Catheter-associated urinary tract infection (CAUTI) is the most common hospital-acquired infection. Key factors influencing the development of CAUTI are indwelling urinary catheter (IUC) insertion duration and nursing management for the prevention of this complication. There is very little evidence describing practice patterns associated with IUC management. The aim of this study was to determine the prevalence of IUC use within a major metropolitan tertiary-referral teaching hospital and to explore nurse-sensitive indicators for the prevention of CAUTI in this context. Methods We conducted a point prevalence survey of IUC use by reviewing every inpatient bed (n = 696) across two sites over a 2-day period in January 2013. Site 1 comprised (n = 520, 74.7%) acute inpatient beds and Site 2 (n = 176, 25.3%) aged care and rehabilitation beds within a single organisation. Results At the time of the survey 555 (79.7%) beds were occupied. Few patients (n = 69, 12.4%) had an IUC in situ and a standard Foley's catheter was used for the majority of patients (62, 92.5%). IUC insertion was more prevalent in women over 70 (20, 71.4%) when compared with men (18, 46.2%; χ2 4.24, P = 0.04). Fourteen nurse-sensitive indicators were assessed and although all indictors were not present for any single patient, drainage system management appeared to be in accordancewith recommended guidelines.Of the patients with an IUC12 (17.4%) had a urine sample sent in the 24 h preceding the survey and 5 (41.6%) of these samples were positive for bacterial colonisation. Conclusion The prevalence of IUC use in this tertiary teaching hospital was less than that in other centres despite a comparatively older inpatient population in the context of acute care needs. Nurses appear to be proficient in the management of IUC and associated drainage equipment and there is room for interdisciplinary improvement in documentation practices. Future research should test interventions to target appropriate insertion, ongoing need and timely removal of IUC.

Membranes of mammalian cells contain lysophosphatidic acid acyltransferase (LPAAT) activities that catalyze the acylation of sn-1-acyl lysophosphatidic acid (lysoPA) to form phosphatidic acid. As the biological roles and biochemical properties of the six known LPAAT isoforms have yet to be fully elucidated, we have characterized human LPAAT-beta activity using two different assays. In a membrane-based assay, LPAAT-beta used lysoPA and lysophosphatidylmethanol (lysoPM) but not other lysophosphoglycerides as an acyl acceptor, and it preferentially transferred 18:1, 18:0, and 16:0 acyl groups over 12:0, 14:0, 20:0, and 20:4 acyl groups. The fact that lysoPM could traverse cell membranes permitted additional characterization of LPAAT-beta activity in cells: PC-3 and DU145 cells converted exogenously added lysoPM and (14)C-labeled 18:1 into (14)C-labeled phosphatidylmethanol (PM). The rate of PM formation was higher in cells that overexpressed LPAAT-beta and was inhibited by the LPAAT-beta inhibitor CT-32501. In contrast, if lysoPM and (14)C-labeled 20:4 were added to PC-3 or DU145 cells, (14)C-labeled PM was also formed, but the rate was neither higher in cells that overexpressed LPAAT-beta nor inhibited by CT-32501. We propose that LPAAT-beta catalyzes the intracellular transfer of 18:1, 18:0, and 16:0 acyl groups but not 20:4 groups to lysoPA.

B. henselae is the etiological agent responsible for cat scratch fever (bartonellosis). The crystal structure of the smaller of the two Nudix hydrolases encoded in the genome of B. henselae, Bh-MutT, was determined to 2.1 Å resolution., Cat scratch fever (also known as cat scratch disease and bartonellosis) is an infectious disease caused by the proteobacterium Bartonella henselae following a cat scratch. Although the infection usually resolves spontaneously without treatment in healthy adults, bartonellosis may lead to severe complications in young children and immunocompromised patients, and there is new evidence suggesting that B. henselae may be associated with a broader range of clinical symptoms then previously believed. The genome of B. henselae contains genes for two putative Nudix hydrolases, BH02020 and BH01640 (KEGG). Nudix proteins play an important role in regulating the intracellular concentration of nucleotide cofactors and signaling molecules. The amino-acid sequence of BH02020 is similar to that of the prototypical member of the Nudix superfamily, Escherichia coli MutT, a protein that is best known for its ability to neutralize the promutagenic compound 7,8-dihydro-8-oxoguanosine triphos­phate. Here, the crystal structure of BH02020 (Bh-MutT) in the Mg2+-bound state was determined at 2.1 Å resolution (PDB entry 3hhj). As observed in all Nudix hydrolase structures, the α-helix of the highly conserved ‘Nudix box’ in Bh-­MutT is one of two helices that sandwich a four-stranded mixed β-sheet with the central two β-strands parallel to each other. The catalytically essential divalent cation observed in the Bh-MutT structure, Mg2+, is coordinated to the side chains of Glu57 and Glu61. The structure is not especially robust; a temperature melt obtained using circular dichroism spectroscopy shows that Bh-­MutT irreversibly unfolds and precipitates out of solution upon heating, with a T m of 333 K.