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1.
Pregnancy Hypertens ; 6(1): 30-7, 2016 Jan.
Article in English | MEDLINE | ID: mdl-26955769

ABSTRACT

The bradykinin type 2 receptor (B2R), main effector of the pleiotropic kallikrein-kinin system (KKS), has been localized in the key sites related to placentation in human, rat and guinea pig utero-placental units. The present study was directed to characterize the content, the cellular and subcellular localization of B2R in the villi and basal plate of placentas from normal and preeclamptic pregnancies by means of western blotting, immunohistochemistry and immunoelectron microscopy. The protein content of B2R was demonstrated in both placental zones. The villous placenta of normal and preeclamptic pregnancies expressed B2R in syncytiotrophoblast and fetal endothelium; the basal plate displayed B2R in extravillous trophoblasts and decidual cells. Lastly, immunogold electron microscopy revealed B2R in fetal endothelium, syncytiotrophoblast, extravillous cytotrophoblasts and decidual cells; in all cell types the receptor was mainly located in the cytosol and nucleus. The protein content of placental homogenates and the immunoreactivity in the different cells types did not differ between both study groups; however the abundance of nuclear immunogold B2R positive beads in extravillous trophoblasts was greater in the normal than in the preeclamptic placentas. The purpose of describing nuclear B2R in the utero-placental unit, and its increment in normal extravillous trophoblasts, is to stimulate the study of the functional pathways that may be relevant to understand the local role of the B2R in normal and preeclamptic gestation.


Subject(s)
Cell Nucleus/chemistry , Placenta/chemistry , Pre-Eclampsia/metabolism , Receptor, Bradykinin B2/analysis , Uterus/chemistry , Adult , Biomarkers/analysis , Blotting, Western , Case-Control Studies , Cell Nucleus/ultrastructure , Chorionic Villi/chemistry , Decidua/chemistry , Endothelial Cells/chemistry , Female , Humans , Immunohistochemistry , Microscopy, Electron , Placenta/ultrastructure , Pre-Eclampsia/diagnosis , Pregnancy , Trophoblasts/chemistry , Uterus/ultrastructure , Young Adult
2.
J Sci Food Agric ; 95(6): 1199-206, 2015 Apr.
Article in English | MEDLINE | ID: mdl-25043293

ABSTRACT

BACKGROUND: Great attention has been paid to the antioxidants present in farmed fish feeds, with the replacement of synthetic antioxidants by natural ones being a main objective. In the present study, Coho salmon (Oncorhynchus kisutch) was fed a conventional diet that was enriched with different kinds of antioxidants: synthetic antioxidants (butylated-hydroxy toluene and ethoxyquin; diet I), a tocopherols-rich mixture (diet II) and a tocopherols-rosemary extract mixture (diet III). A comparative study of the sensory and physical changes observed in the corresponding frozen products was undertaken. RESULTS: After 18 months at -18 °C, fish previously fed on diet I showed higher putrid and rancid odours and rancid taste scores, while lower mean typical odour and taste values were attained. Dripping and expressible moisture values obtained for diet II-fish were lower when compared with their counterparts belonging to the diet I; additionally, microstructure analysis revealed that Z-lines integration was better preserved in fish corresponding to diets II and III. CONCLUSION: Diet II has been recognised as being the most profitable to be employed to maintain the sensory and physical properties of the frozen product when long-term storage is considered. Further research is to be continued to optimise the natural antioxidants profile.


Subject(s)
Antioxidants/pharmacology , Diet , Food Preservation/methods , Oncorhynchus kisutch , Rosmarinus , Seafood/analysis , Tocopherols/pharmacology , Animal Feed , Animals , Female , Fish Oils/metabolism , Freezing , Humans , Lipid Peroxidation/drug effects , Male , Muscles/drug effects , Odorants , Plant Extracts/pharmacology , Taste
3.
Biol. Res ; 27(1): 29-38, 1994. ilus
Article in English | LILACS | ID: lil-225967

ABSTRACT

The association of myosin and a filamin-like protein to the F-actin cytoskeleton of parietal cells was studied in the rat gastric mucosa. Myosin and the filamin-like protein were localized by indirect immunofluorescence microscopy while the distribution of actin was established by using FITC-phalloidin. These cytoskeletal proteins, concentrated in the parietal cells, changed their distribution in correlation with the hydrochloric acid (HCl) secretory state of the cells and the appearance of a developed intracellular canaliculus. Thus,in resting parietal cells, actin showed a patchy distribution, delimiting the poorly developed secretory canaliculi, while myosin and the filamin-like protein distributed diffusely over the cytoplasm. In secreting cells, F-actin was concentrated in the cytoplasmic projections filling the canalicular lumen, while myosin and the filamin-like protein were excluded from this region, concentrating in the adjoining cytoplasm. The present results show that myosin and the filamin-like protein change their association with the secretory membranes in relation to the development of the secretory canaliculus of parietal cells. In resting cells, both proteins associate with the endocellular secretory membranes. In secreting cells, the microvillar projections of the canalicular surface formed by these membranes bind F-actin, but exclude myosin and the filamin-like protein


Subject(s)
Animals , Rats , Actins/metabolism , Contractile Proteins/metabolism , Gastric Mucosa/ultrastructure , Microfilament Proteins/metabolism , Myosins/metabolism , Parietal Cells, Gastric/ultrastructure , Cell Membrane/metabolism , Cell Membrane/ultrastructure , Contractile Proteins/ultrastructure , Cytoskeleton/metabolism , Cytoskeleton/ultrastructure , Fluorescent Antibody Technique , Gastric Acid/metabolism , Gastric Mucosa/ultrastructure , Microfilament Proteins/ultrastructure , Microscopy, Fluorescence , Myosins/ultrastructure , Parietal Cells, Gastric/metabolism , Rats, Sprague-Dawley
4.
Biol. Res ; 27(3/4): 177-92, 1994. ilus, graf
Article in English | LILACS | ID: lil-228577

ABSTRACT

The relation between the expression of the oxyntic cell phenotype and the modifications of the extracellular matrix during development of the gastric glands, was studied in 10 to 21 day-old chick embryos. Cytodifferentiation of the oxyntic cells was established by ultrastructural methods, while the expression of pepsinogen, mitochondrial enzyme markers and apical secretory membranes was determined by histochemical and biochemical procedures. Results show that the morphogenesis of the glandular lobules occurs between days 8 and 15 of gestation. Later on, the lobules enlarge but maintain their basic morphology. Until day 13, the developing glands consist of primary tubes lined by a stratified columnar epithelium. The apical poles of the cells that contact the lumen show cytoplasmic processes, and Mg-ATPase activity and F-actin are concentrated at the apical cell borders. From day 13 on, the cells of the simple epithelium that lines secondary tubules budding from the primary tube, show all the features that define differentiated oxyntic cells. The synthesis of glycosaminoglycans during glandular morphogenesis was studied measuring the incorporation of radioactive sulfate into developing chick embryo proventriculi. An important increase in isotope incorporation was found between days 13 and 18 of development. Histochemical localization of these macromolecules shows that glycosaminoglycans are closely associated with the developing glandular lobules. Variations in the structure of epithelial cells undergoing morphogenesis and in the composition of the extracellular matrix are synchronous, suggesting that interactions between them may be significant in terms of the establishment and maintenance of the adult gastric gland phenotype


Subject(s)
Animals , Chick Embryo , Extracellular Matrix , Gastric Mucosa/embryology , Parietal Cells, Gastric/cytology , Actins/analysis , Ca(2+) Mg(2+)-ATPase/analysis , Cell Differentiation , Electron Transport Complex IV/analysis , Gastric Mucosa/ultrastructure , Glycosaminoglycans/analysis , Morphogenesis
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