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Biomedical subjects

H Pinheiro

Publications and source records attributed to H Pinheiro.

9 recordsLinked to original sources

Electrochemical degradation applied to the metabolites of Acid Orange 7 anaerobic biotreatment.

The electrochemical oxidation of the biotic degradation products of the textile dye C.I. Acid Orange 7 (AO7) was achieved using a boron doped diamond electrode (BDD). Tests were performed with model solutions of the biotic degradation products, sulphanilic acid (SA) and 1-amino-2-naphthol (AN), and also with real effluents obtained in experiments carried out in an up-flow anaerobic sludge blanket (UASB) reactor, fed with a simulated textile effluent containing AO7, working in mesophilic or thermophilic conditions. Bulk electrolysis was studied using two different supporting electrolytes - NaCl and Na(2)SO(4). The influence of initial metabolite concentration and current density on the electrodegradation rates of the biotic products was investigated. For the UASB effluents, oxidation tests were carried out for different electrolytes and at different current densities. Samples were collected at pre-selected intervals and absorbance measurements, chemical oxygen demand (COD) and total organic carbon (TOC) tests and high performance liquid chromatography (HPLC) analysis were performed. Results have shown an almost complete elimination of the persistent pollutants and a COD removal higher than 70% for both AN and SA. For the UASB effluents, COD removals between 45% and 90% and TOC removals varying from 19% to 41% were obtained.

Algorithms↗

A comparison of AT1 angiotensin II antagonists at pre- and postjunctional angiotensin II receptors of the rat tail artery.

A comparison was made of the influence of candesartan, ZD7155, losartan and eprosartan on angiotensin II effects at pre- and postjunctional AT(1) receptors of the rat tail artery. To study the anti-angiotensin II effect at prejunctional receptors, the tissues were preincubated with [(3)H]noradrenaline and then superfused and electrically stimulated (1 Hz, 2 ms, 50 mA, during 5 min); to study the angiotensin II effect at postjunctional receptors, non-cumulative concentration-response curves to angiotensin II were determined in the absence and in the presence of the antagonist. p A(2) values were calculated for competitive antagonists and p D'(2) values for insurmountable antagonists. At the prejunctional level, losartan and eprosartan displayed competitive antagonism with p A(2) values of 6.50 and 8.08, respectively, whereas candesartan and ZD7155 displayed non-competitive antagonism with p D'(2) values of 8.71 and 7.98, respectively. At the postjunctional level, the four antagonists displayed the same kind of antagonism as prejunctionally with p A(2) values for losartan and eprosartan of 8.52 and 8.22, respectively, and p D'(2) values of 10.62 and 9.01, for candesartan and ZD7155, respectively. The ratios between post- and prejunctional potencies were: losartan 101, candesartan 81, ZD7155 11, and eprosartan 1.4. We conclude that, at least functionally, pre- and postjunctional angiotensin II AT(1) receptors are different and propose that the prejunctional receptors in this tissue belong to the AT(1B)-subtype.

Angiotensin II↗

Modulation of insulin transport in rat brain microvessel endothelial cells by an ecto-phosphatase activity.

The physiological function of alkaline phosphatase (ALP) remains controversial. It was recently suggested that this membrane-bound enzyme has a role in the modulation of transmembranar transport systems into hepatocytes and Caco-2 cells. ALP activity expressed on the apical surface of blood-brain barrier cells, and its relationship with (125)I-insulin internalization were investigated under physiological conditions using p-nitrophenylphosphate (p-NPP) as substrate. For this, an immortalized cell line of rat capillary cerebral endothelial cells (RBE4 cells) was used. ALP activity and (125)I-insulin internalization were evaluated in these cells. The results showed that RBE4 cells expressed ALP, characterized by an ecto-oriented active site which was functional at physiological pH. Orthovanadate (100 microM), an inhibitor of phosphatase activities, decreased both RBE4-ALP activity and (125)I-insulin internalization. In the presence of L-arginine (1 mM) or adenosine (100 microM) RBE4-ALP activity and (125)I-insulin, internalization were significantly reduced. However, D-arginine (1 mM) had no significant effect. Additionally, RBE4-ALP activity and (125)I-insulin internalization significantly increased in the presence of the bioflavonoid kaempferol (100 microM), of the phorbol ester PMA (80 nM), IBMX (1 mM), progesterone (200 microM and 100 microM), beta-estradiol (100 microM), iron (100 microM) or in the presence of all-trans retinoic acid (RA) (10 microM). The ALP inhibitor levamisole (500 microM) was able to reduce (125)I-insulin internalization to 69.1 +/- 7.1% of control. Our data showed a positive correlation between ecto-ALP activity and (125)I-insulin incorporation (r = 0.82; P < 0.0001) in cultured rat brain endothelial cells, suggesting that insulin entry into the blood-brain barrier may be modulated through ALP.

Animals↗

Differential effects of eprosartan and losartan at prejunctional angiotensin II receptors.

A comparison was made of the influence of losartan and eprosartan on angiotensin II effects at pre- and postjunctional receptors of the canine pulmonary artery and at prejunctional receptors of the rat left ventricle. To study postjunctional contractile responses to angiotensin II, non-cumulative concentration-response curves were determined; to study prejunctional effects of angiotensin II, the tissues were preincubated with [3H]noradrenaline and then superfused and electrically stimulated (1 Hz, 2 ms, 50 mA, 5 min). Postjunctionally, both losartan and eprosartan caused a parallel shift of the concentration-response curve of angiotensin II to the right (pKd of 8.15 and 8.28, respectively). At the prejunctional level, while eprosartan, in concentrations similar to those which were effective postjunctionally (30-100 nM), antagonized the facilitatory effect on noradrenaline release in both the dog pulmonary artery and the rat ventricle, losartan was ineffective in concentrations up to 1 microM. It is concluded that pre-junctional receptors for angiotensin II in the canine pulmonary artery and in the rat left ventricle are different from postjunctional receptors of the canine pulmonary artery. It is proposed that the prejunctional receptors of these tissues are atypical AT1 or "AT1B-like" receptors.

Acrylates↗

Prejunctional effects of angiotensin II and bradykinin in the heart and blood vessels.

1. Angiotensin and bradykinin facilitate the release of noradrenaline from sympathetic nerve terminals and cause positive inotropy in rat isolated atria and ventricles. The effect of bradykinin was enhanced by the ACE inhibitor, ramiprilat. 2. The facilitated release of noradrenaline in rat ventricle by bradykinin was blocked by the beta2-receptor antagonist HOE-140. This response is also reduced by removing the endocardium, suggesting the release of a mediator from the endocardium. 3. The facilitated noradrenaline release by angiotensin II and bradykinin was blocked by the angiotensin receptor antagonist saralasin to the same extent. In contrast, losartan caused only minor blockade in a range of vascular and cardiac tissues. This suggests that angiotensin and bradykinin exert these responses by interacting with a prejunctional receptor different from the established AT1 subtype. 4. These results suggest that bradykinin mediates facilitation of noradrenaline release via the local release of angiotensin onto an atypical AT1 receptor.

Angiotensin II↗

Biotransformation in organic media by enzymes and whole cells.

Biotransformation of poorly water soluble compounds in organic media by immobilized enzyme and whole cells is illustrated in this paper taking the following examples from the author's laboratory: (1) controlled hydrolysis of triglycerides and synthesis reactions by a recombinant lipolytic enzyme (cutinase); (2) enzymatic synthesis of dipeptides; (3) continuous production of isovaleraldehyde by Gluconobacter oxydans in isooctane; and (4) sitosterol side chain cleavage by Mycobacterium sp. The role of water and organic solvent are evaluated, namely the increase in the volumetric productivity of the reaction system and the shift of the reaction equilibrium in favour of product synthesis. High product yields have been obtained due to the reduction of substrate/product inhibition. Biocatalyst stability in the presence of the organic phase was also performed.

Adsorption↗

Identifying genetic markers to assess the presence of gene-environment interactions.

We analyzed a randomly chosen replicate with the goals of locating the closest markers to the genes involved in the discrete trait and utilizing these as surrogates for the genes in assessing the presence of gene-environment interactions. We screened the markers with an association test prior to using the transmission-disequilibrium test. We performed a segregation analysis, with regressive models and including the selected markers, to understand the underlying genetic mechanism and the role of the environmental factor. We were unsuccessful in locating the relevant markers due to the absence of linkage disequilibrium. Nevertheless, some insights were gained from the methods used.

Chromosome Mapping↗