Running a mentalization-based treatment (MBT) programme within a public community adult mental health service setting: a feasibility study.

OBJECTIVES: This article aimed to address the feasibility of mentalization-based treatment (MBT) for patients with personality disorder in a non-specialist setting. The development and implementation of an MBT Programme is described. METHODS: A multidisciplinary Consult Group met to plan the implementation of the programme. Participants attended a psychoeducation group (MBT Introductory Group), then weekly individual and group therapy. Fourteen participants started the full programme with eight completing at least 9 months, complete data are available for five participants who completed 27 months (first cohort) and 21 months (second cohort). Data include quantitative measures and qualitative questionnaires/interviews. All had a diagnosis of personality dysfunction with co-morbid disorder including anxiety/depressive disorder, post-traumatic stress disorder and eating disorder. RESULTS: Data on five participants revealed reductions in global level of distress, improvements in psychological well-being, less interpersonal difficulties and better work and social functioning. Qualitative data from feedback questionnaires (n = 18) and in-depth interview (n = 2) are discussed under the themes of mentalizing, treatment feedback/outcomes and group factors. Therapist reflections on the process identify the challenges involved in implementing a specialist psychotherapy programme within a general service and learning points from this are discussed. CONCLUSIONS: MBT is an acceptable treatment for patients with personality dysfunction. Prior to the implementation of a programme, factors at the therapist, team and organizational level, as well as the wider context, need to be examined. This is to ensure that conditions are in place for proper adherence to the model to achieve the positive outcomes demonstrated in the RCT studies.

In situ ATR FTIR studies of SO4 adsorption on goethite in the presence of copper ions.

Despite the existence of many single ion sorption studies on iron and aluminum oxides, fewer studies have been reported that describe cosorption reactions. In this work, we present an in situ ATR FTIR study of synergistic adsorption of sulfate (SO4) and copper (Cu) on goethite, which is representative of the minerals and ions present in mine wastes, acid sulfate soils, and other industrial and agricultural settings. Sulfate adsorption was studied as a function of varying pH, and as a function of increasing concentration in the absence and presence of Cu. The presence of Cu ions in solution had a complex effect on the ability of SO4 ions to be retained on the goethite surface with increasing pH, with complete desorption occurring near pH 7 and 9 in the absence and presence of Cu, respectively. In addition, Cu ions altered the balance of inner vs outer sphere adsorbed SO4. The solid phase partitioning of SO4 at pH 3 and pH 5 was elevated by the presence of Cu; in both cases Cu increased the affinity of SO4 for the goethite surface. Complementary ex situ sorption edge studies of Cu on goethite in the absence and presence of SO4 revealed that the Cu adsorption edge shifted to lower pH (6.3 --> 5.6) in the presence of SO4, consistent with a decrease of the electrostatic repulsion between the goethite surface and adsorbing Cu. Based on the ATR FTIR and bulk sorption data we surmise that the cosorption products of SO4 and Cu at the goethite-water interface were not in the nature of ternary complexes under the conditions studied here. This information is critical for the evaluation of the onset of surface precipitates of copper-hydroxy sulfates as a function of pH and solution concentration.

Time and concentration dependence of the dicyclohexylcarbodiimide inhibition of proton movements in the cytochrome bc1 complex from yeast mitochondria reconstituted into proteoliposomes.

The cytochrome bc1 complex was isolated from yeast mitochondria solubilized with the detergent dodecyl maltoside and reconstituted into proteoliposomes to measure electrogenic proton pumping. Optimal respiratory control ratios of 4.0, obtained after addition of the uncoupler CCCP, and H+/e- ratios of 1.6 were obtained when the proteoliposomes were prepared with egg yolk phosphatidylcholine supplemented with cardiolipin. Moreover, it was critical to remove excess dodecyl maltoside in the final concentrated preparation prior to reconstitution to prevent loss of enzymatic activity. The rate of electrogenic proton pumping, the respiratory control ratios, and the H+/e- ratios were decreased by incubation of the cytochrome bc1 complex with dicyclohexylcarbodiimide (DCCD) in a time and concentration dependent manner. Maximum inhibitions were observed when 50 nmol DCCD per nmol of cytochrome b were incubated for 30 min at 12 degrees C with the intact cytochrome bc1 complex. Under these same conditions maximum labeling of cytochrome b with [14C] DCCD was reported in a previous study [Beattie et al. (1984). J. Biol. Chem. 259, 10562-10532] consistent with a role for cytochrome b in electrogenic proton movements.

Synthesis and antidiarrheal activity of N-(aminoiminomethyl)-1H-pyrrole-1-acetamides related to guanfacine.

A series of N-(aminoiminomethyl)-1H-pyrrole-1-acetamides, related to guanfacine, were prepared and tested for antidiarrheal activity in castor oil dosed rats. trans-N-(Aminoiminomethyl)-2,5-dihydro-2,5-dimethyl-1H-pyrrole-1-acetami de (2), in which the dichlorophenyl ring of guanfacine is replaced by 2,5-dimethyl-2,5-dihydropyrrole, showed potent antidiarrheal activity but possessed only minimal cardiovascular activity in rats.

The stimulation of yeast mitochondrial protein synthesis by low molecular weight cytoplasmic factors: requirement for intact mitochondria and lack of effect by folate derivatives.

Protein synthesis by GTP-supplemented yeast mitochondria is stimulated by a fraction of molecular weight less than 2,000 isolated from yeast high-speed supernatant (S-150). The low molecular weight fraction works independently of the respiratory chain as the stimulation effect is not cyanide-sensitive. Stimulation of mitochondrial protein synthesis by cytoplasmic factors is dependent upon the method of mitochondrial isolation. The low molecular weight stimulatory factor(s) are not reduced folate derivatives which supply formyl groups required for initiation of mitochondrial protein synthesis.