Effect of BMI on Prolonged Abstinence after Smoking Cessation Treatment: A Retrospective Cohort Study.

BACKGROUND: Despite the well-documented relationship between weight gain and poorer cessation outcomes among smokers, the role of the former (baseline) weight in smoking cessation is insufficiently investigated. We hypothesized that patients with higher baseline body mass index( BMI) have a worse prognosis in tobacco cessation. OBJECTIVES: This retrospective clinical cohort study aimed to investigate the role of the baseline BMI on abstinence over 12 months after participation in smoking cessation treatment conducted in a middle-income country (n = 664). METHODS: Data from a 6-week smoking cessation protocol performed in a Psychosocial Care Unit (CAPS) were used. The protocol included four medical consultations and six Cognitive-Behavioral Therapy (CBT) group sessions. Initially, 1,213 participants were evaluated for the study, but only the participants whose telephone contact was successful were included in the outcome analyses. The attrition rate was 45.3%. Continuous and categorical (normal, overweight, and obesity) BMI values were computed. Survival regression models were used to test the associations between BMI and the 12-month abstinence outcome. Self-report 4-week abstinence at the end of treatment was also investigated using logistic regression models. RESULTS: Baseline BMI had no significant effect on both short (4-week-point abstinence) and long (12-month prolonged abstinence) treatment outcomes. CONCLUSION: The possible influence of the baseline BMI on smoking cessation outcomes, especially considering prolonged abstinence, was not corroborated by our results. Regardless of our results, the detrimental health outcomes due to the combination of obesity/overweight and smoking justify that these subgroups of individuals be continuously targeted for adequate smoking prevention and treatment.

Adaptive Immune Response Impairs the Efficacy of Autologous Transplantation of Engineered Stem Cells in Dystrophic Dogs.

Duchenne muscular dystrophy is the most common genetic muscular dystrophy. It is caused by mutations in the dystrophin gene, leading to absence of muscular dystrophin and to progressive degeneration of skeletal muscle. We have demonstrated that the exon skipping method safely and efficiently brings to the expression of a functional dystrophin in dystrophic CD133+ cells injected scid/mdx mice. Golden Retriever muscular dystrophic (GRMD) dogs represent the best preclinical model of Duchenne muscular dystrophy, mimicking the human pathology in genotypic and phenotypic aspects. Here, we assess the capacity of intra-arterial delivered autologous engineered canine CD133+ cells of restoring dystrophin expression in Golden Retriever muscular dystrophy. This is the first demonstration of five-year follow up study, showing initial clinical amelioration followed by stabilization in mild and severe affected Golden Retriever muscular dystrophy dogs. The occurrence of T-cell response in three Golden Retriever muscular dystrophy dogs, consistent with a memory response boosted by the exon skipped-dystrophin protein, suggests an adaptive immune response against dystrophin.

Expression of constructs of the neuronal isoform of myosin-Va interferes with the distribution of melanosomes and other vesicles in melanoma cells.

Myosin-Va has been implicated in melanosome translocation, but the exact molecular mechanisms underlying this function are not known. In the dilute, S91 melanoma cells, melanosomes move to the cell periphery but do not accumulate in the tips of dendrites as occurs in wild-type B16 melanocytes; rather, they return and accumulate primarily at the pericentrosomal region in a microtubule-dependent manner. Expression of the full-length neuronal isoform of myosin-Va in S91 cells causes melanosomes to disperse, occupying a cellular area approximately twice that observed in non-transfected cells, suggesting a partial rescue of the dilute phenotype. Overexpression of the full tail domain in S91 cells is not sufficient to induce melanosome dispersion, rather it causes melanosomal clumping. Overexpression of the head and head-neck domains of myosin-Va in B16 cells does not alter the melanosome distribution. However, overexpression of the full tail domain in these cells induces melanosome aggregation and the appearance of tail-associated, aggregated particles or vesicular structures that exhibit variable degrees of staining for melanosomal and Golgi beta-COP markers, as well as colocalization with the endogenous myosin-Va. Altogether, the present data suggest that myosin-Va plays a role in regulating the direction of microtubule-dependent melanosome translocation, in addition to promoting the capture of melanosomes at the cell periphery as suggested by previous studies. These studies also reinforce the notion that myosin-V has a broader function in melanocytes by acting on vesicular targeting or intracellular protein trafficking.