RESUMO
BACKGROUND: The genus Ternstroemia is associated with the vulnerable tropical montane cloud forest in Mexico and with other relevant vegetation types worldwide. It contains threatened and pharmacologically important species and has taxonomic issues regarding its species limits. This study describes 38 microsatellite markers generated using a genomic-based approach. METHODS AND RESULTS: We tested 23 of these markers in a natural population of Ternstroemia lineata. These markers are highly polymorphic (all loci polymorphic with 3-14 alleles per locus and expected heterozygosity between 0.202 and 0.908), most of them (19 out of 23) are in Hardy-Weinberg Equilibrium and free of null alleles (18 out of 23). Also we found no evidence of linkage among them. Finally, we tested the transferability to six other American species of Ternstroemia, two other Pentaphylacaceae species, and four species from different families within the order Ericales. CONCLUSIONS: These molecular resources are promising tools to investigate genetic diversity loss and as barcodes for ethnopharmacological applications and species delimitation in the family Pentaphylacaceae and some Ericales, among other applications.
Assuntos
Ericales , Humanos , Ericales/genética , Genoma , Genômica , Heterozigoto , Repetições de Microssatélites/genética , Alelos , Sequenciamento de Nucleotídeos em Larga Escala , Loci Gênicos/genéticaRESUMO
Mercury and selenium were assessed in Mustelus henlei, which is a carnivorous predatory shark that is important for the coastal communities of the northern Mexican Pacific (NMP). Sixty-two individuals were sampled; muscle and liver were isolated and analyzed by atomic absorption spectrophotometry. The mean Hg concentrations (wet weight) obtained for muscle (0.08 ± 0.10 µg g-1) and liver (0.09 ± 0.26 µg g-1) were below the allowed limits (< 1.0 µg g-1 Hg). The average Se concentration was 0.03 ± 0.01 µg g-1 in muscle and 0.13 ± 0.05 µg g-1 in liver. The Se/Hg molar ratio of muscle was 1.83; however, the selenium health benefit value (HBVSe) was of 0.08. We calculated that an adult man (70 kg), an adult woman (60 kg), and a child (16 kg) could consume 1595, 838, and 223 g/week of M. henlei muscle, respectively, without risks to health. In conclusion, the concentrations and molar ratio of Hg and Se in M. henlei muscle mean that consumption of this shark's meat does not represent neither a benefit nor a public health risk.
Assuntos
Mercúrio/análise , Selênio/análise , Tubarões , Poluentes Químicos da Água/análise , Animais , Criança , Monitoramento Ambiental , Feminino , Humanos , Masculino , MéxicoRESUMO
Conformational diseases include heterogeneous disorders sharing a similar pathological mechanism, leading to intracellular aggregation of proteins with toxic effects. Serpins are commonly involved in these diseases. These are structurally sensitive molecules that modify their folding under even minor genetic or environmental variations. Indeed, under normal conditions, the rate of misfolding of serpins is high and unfolded serpins must be degraded by the proteasome system. Our aim was to study the effects of bortezomib, a proteasome inhibitor, on conformationally sensitive serpins. The effects of bortezomib were analysed in patients with multiple myeloma, HepG2 cells, and Swiss mice, as well as in vitro. Levels, anti-FXa activity, heparin affinity, and conformational features of antithrombin, a relevant anticoagulant serpin, were analysed. Histological, ultrastructural features and immunohistological distribution of antithrombin and alpha1-antitrypsin (another hepatic serpin) were evaluated. We also studied the intracellular accumulation of conformationally sensitive (fibrinogen) or non-sensitive (prothrombin) hepatic proteins. The inhibition of the proteasome caused intracellular accumulation and aggregation of serpins within the endoplasmic reticulum that was associated with confronting cisternae and Mallory body formation. These effects were accompanied by a heat stress response. Bortezomib also increased the levels of intracellular fibrinogen, but has no significant effect on prothrombin. Finally, bortezomib had only minor effects on the mature circulating antithrombin, with increased amounts of latent antithrombin in plasma. These results suggest that the impairment of proteasomal activities leads to an intracellular accumulation of conformationally sensitive proteins and might facilitate the release of misfolded serpins into circulation where they adopt more stable conformations.