Here, we present a comprehensive morphological and molecular phylogenetic analysis of sp. (Digenea: Clinostomidae) metacercariae parasitizing two freshwater fish species from Southeast Brazil: (piranha) and (tambuatá). The morphological examination revealed distinct characteristics of metacercariae in each host.
View Article and Find Full Text PDFThe present study determined the presence of heavy metals in green sea turtles with and without fibropapillomatosis in Itapirubá and Cassino beaches, southern Brazil. The weight, curved length of the carapace and body index were determined and blood was collected to quantify the concentrations of cadmium, lead and mercury. A total of 51 blood samples were analyzed, being 46 positives for at least one of the metals.
View Article and Find Full Text PDFThe choroid plexus (CP), located in each of the four ventricles of the brain, is formed by a monolayer of epithelial cells that surrounds a highly vascularized connective tissue with permeable capillaries. These cells are joined by tight junctions forming the blood-cerebrospinal fluid barrier (BCSFB), which strictly regulates the exchange of substances between the blood and cerebrospinal fluid (CSF). The primary purpose of the CP is to secrete CSF, but it also plays a role in the immune surveillance of the central nervous system (CNS) and in the removal of neurotoxic compounds from the CSF.
View Article and Find Full Text PDFBackground: While still controversial, it has been demonstrated that vascular defects can precede the onset of other AD hallmarks features, making it an important therapeutic target. Given that the protein transthyretin (TTR) has been established as neuroprotective in AD, here we investigated the influence of TTR in the vasculature.
Methods: We evaluated the thickness of the basement membrane and the length of brain microvessels, by immunohistochemistry, in AβPPswe/PS1A246E (AD) transgenic mice and non-transgenic mice (NT) bearing one (TTR+/-) or two (TTR+/+) copies of the TTR gene.
Background: Transthyretin (TTR) is a tetrameric, amyloid-β (Aβ)-binding protein, which reduces Aβ toxicity. The TTR/Aβ interaction can be enhanced by a series of small molecules that stabilize its tetrameric form. Hence, TTR stabilizers might act as disease-modifying drugs in Alzheimer's disease.
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