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1.
Environ Toxicol Pharmacol ; 102: 104253, 2023 Sep.
Article in English | MEDLINE | ID: mdl-37604358

ABSTRACT

Microplastics are present in the environment, in drinking water, in human blood and there is evidence of nanoplastics in tap water. The objective of this work was to analyze the possibility of hemodialysis patients being contaminated by micro and nanoplastics (MNPs) during dialysis treatment. The motivation for this investigation is the fact that hemodialysis patients use about 300-600 L of drinking water per week, which may be contaminated by MNPs. A literature review, a field investigation in a London hospital and an estimation of MNPs intake in patients were carried out. The results showed potential points of risk of contamination of patients by MNPs in hemodialysis. It was also estimated that for a filtration efficiency of 99 % for MNPs, the amount of microplastics that can penetrate the kidneys of patients is 0.0021-3768 particles/week. The assessment concludes that hemodialysis patients are at high risk of MNP contamination.


Subject(s)
Drinking Water , Microplastics , Humans , Radar , Plastics , Renal Dialysis
2.
Work ; 62(3): 393-410, 2019.
Article in English | MEDLINE | ID: mdl-30856146

ABSTRACT

BACKGROUND: Considering that, environments with information and communication technology innovations, including educational institutions, are providing more interaction among individuals anywhere in the world and contributing to higher learning flexibility, it is necessary to pay extra attention to the radiation dissipated by technological equipment in these environments. OBJECTIVE: Investigate whether the behavior of the globe temperature (tg) in relation to the air temperature (ta) could affect the performance of students in information technology laboratories (ITLs). METHODS: The methodological procedures adopted consisted of the following analyses in six institutions: thermal variables - mean radiant temperature (trm) and (tg-ta); students' performance and architectural elements. RESULTS: ITL G was the ITL with the highest incidence of thermal radiation, thus a mathematical model was proposed for this sample to determine whether (tg - ta) and trm are related to overall student performance (Dt). For each increase of one degree in the difference between the globe temperature and the air temperature (tg-ta), the students' performance in the institution G decreased by approximately 29%. CONCLUSION: As well as productivity can be altered due to changes in air temperature in air-conditioned teaching environments, in this specific case, if tg> >ta, possibly the thermal radiation may interfere with the performance of the people present in the environment technological innovations of communication and information.


Subject(s)
Academic Performance/standards , Cognition/physiology , Environment , Information Technology/statistics & numerical data , Temperature , Academic Performance/statistics & numerical data , Educational Measurement/methods , Humans , Laboratories/standards , Laboratories/statistics & numerical data , Models, Theoretical
3.
Vascul Pharmacol ; 53(1-2): 22-7, 2010.
Article in English | MEDLINE | ID: mdl-20307688

ABSTRACT

Cardiac mast cells (MC) are apposed to capillaries within the heart and release renin and proteases capable of metabolizing angiotensins (Ang). Therefore, we hypothesized that mast cell degranulation could alter the rat coronary vascular responsiveness to the arterial delivered Ang I and Ang II, taking into account carboxypeptidase and chymase-1 activities. Hearts from animals that were either pretreated or not with systemic injection of the secretagogue compound 48/80 were isolated and mounted on a Langendorff apparatus to investigate coronary reactivity. The proteolytic activity of the cardiac perfusate from isolated hearts, pretreated or not with the secretagogue, toward Ang I and tetradecapeptide renin substrate was analyzed by HPLC. Coronary vascular reactivity to peptides was not affected by compound 48/80 pretreatment, despite the extensive amount of cardiac MC degranulation. Cardiac MC activation did not modify the generation of both Ang II and Ang 5-10 from Ang I by cardiac perfusate, activities that could be ascribed to MC carboxypeptidase and chymase-1, respectively. An aliskiren-resistant Ang I-forming activity was increased in perfusates from secretagogue-treated hearts. Thus, cardiac MC proteases capable of metabolizing angiotensins do not affect rat coronary reactivity to arterial delivered Ang I and II.


Subject(s)
Angiotensin II/pharmacology , Angiotensin I/pharmacology , Mast Cells/drug effects , Angiotensin I/administration & dosage , Angiotensin I/metabolism , Angiotensin II/administration & dosage , Angiotensin II/metabolism , Angiotensinogen/pharmacology , Animals , Carboxypeptidases/metabolism , Chromatography, High Pressure Liquid , Chymases/metabolism , Coronary Vessels/drug effects , Coronary Vessels/metabolism , Male , Mast Cells/enzymology , Mast Cells/metabolism , Rats , Rats, Wistar , p-Methoxy-N-methylphenethylamine/pharmacology
4.
Am J Physiol Heart Circ Physiol ; 293(6): H3550-7, 2007 Dec.
Article in English | MEDLINE | ID: mdl-17906107

ABSTRACT

We describe the enzymes that constitute the major bradykinin (BK)-processing pathways in the perfusates of mesenteric arterial bed (MAB) and coronary vessels isolated from Wistar normotensive rats (WNR) and spontaneously hypertensive rats. The contribution of particular proteases to BK degradation was revealed by the combined analysis of fragments generated during incubation of BK with representative perfusate samples and the effect of selective inhibitors on the respective reactions. Marked differences were seen among the perfusates studied; MAB secretes, per minute of perfusion, kininase activity capable of hydrolyzing approximately 300 pmol of BK/min, which is approximately 250-fold larger amount on a per unit time basis than that of its coronary counterpart. BK degradation in the coronary perfusate seems to be mediated by ANG I-converting enzyme, neutral endopeptidase 24.11-like enzyme, and a dl-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid-sensitive basic carboxypeptidase; coronary perfusate of WNR contains an additional BK-degrading enzyme whose specificity resembles that of neurolysin or thimet oligopeptidase. Diversely, a des-Arg(9)-BK-forming enzyme, responsible for nearly all of the kininase activity of MAB perfusates of WNR and spontaneously hypertensive rats, could be purified by a procedure that involved affinity chromatography over potato carboxypeptidase inhibitor-Sepharose column and shown to be structurally identical to rat pancreatic carboxypeptidase B (CPB). Comparable levels of CPB mRNA expression were observed in pancreas, liver, mesentery, and kidney, but very low levels were detected in lung, heart, aorta, and carotid artery. In conclusion, distinct BK-processing pathways operate in the perfusates of rat MAB and coronary bed, with a substantial participation of a des-Arg(9)-BK-forming enzyme identical to pancreatic CPB.


Subject(s)
Bradykinin/metabolism , Carboxypeptidase B/blood , Coronary Circulation , Hypertension/enzymology , Metalloendopeptidases/metabolism , Peptidyl-Dipeptidase A/metabolism , Splanchnic Circulation , Angiotensin-Converting Enzyme Inhibitors/pharmacology , Animals , Blood Pressure , Bradykinin/analogs & derivatives , Carboxypeptidase B/antagonists & inhibitors , Carboxypeptidase B/genetics , Carboxypeptidase B/isolation & purification , Disease Models, Animal , Gene Expression Regulation, Enzymologic , Hydrolysis , Hypertension/physiopathology , Male , Metalloendopeptidases/antagonists & inhibitors , Neprilysin/metabolism , Pancreas/enzymology , Perfusion , Protease Inhibitors/pharmacology , Rats , Rats, Inbred SHR , Rats, Wistar , Substrate Specificity , Tissue Distribution
5.
Hypertension ; 50(1): 110-5, 2007 Jul.
Article in English | MEDLINE | ID: mdl-17470724

ABSTRACT

Angiotensin-converting enzyme (kininase II [ACE]) inhibitors are capable of potentiating bradykinin (BK) effects by enhancing the actions of bradykinin on B(2) receptors independent of blocking its inactivation. To investigate further the importance of ACE kininase activity on BK-induced vasodilation, we investigated the effect of inhibiting ACE, as well as other kininases, on both BK metabolism and vasodilator effect in preparations that exhibit increased ACE activity. Mesenteric arterial beds obtained from 1-kidney, 1-clip hypertensive rats presented augmented ACE and angiotensin I converting activities compared with normotensive rats. The isolated and perfused mesenteric beds were exposed to BK for 15 minutes in the absence or in the presence of kininase inhibitors; then, the perfusate was collected for analysis of the products of BK metabolism by high-performance liquid chromatography. BK was metabolized to the fragments BK(1-8), BK(1-7), and BK(1-5), and the recovery of intact BK was reduced by 47% in the hypertensive group. Recovery of BK was increased in both groups in the presence of a kininase I inhibitor and in the hypertensive group by neutral endopeptidase 24.11 inhibitor; however, ACE inhibition did not affect BK metabolism in both groups. In contrast, only the ACE inhibitor potentiated the vasodilator effect of BK in a mesenteric bed preconstricted with phenylephrine; the increase in BK effect, nevertheless, was not greater in arteries from hypertensive rats that presented an increased ACE activity when compared with those in the normotensive group. These data demonstrated that ACE inhibitor-induced potentiation of BK vasodilator effects is not related to their actions on BK degradation.


Subject(s)
Angiotensin-Converting Enzyme Inhibitors/pharmacology , Bradykinin/pharmacology , Hypertension/physiopathology , Mesenteric Arteries/enzymology , Peptidyl-Dipeptidase A/metabolism , Vasodilator Agents/pharmacology , 3-Mercaptopropionic Acid/analogs & derivatives , 3-Mercaptopropionic Acid/pharmacology , Animals , Blood Pressure , Bradykinin/metabolism , Drug Synergism , Enzyme Inhibitors/pharmacology , Glycopeptides/pharmacology , Hypertension/enzymology , In Vitro Techniques , Lysine Carboxypeptidase/antagonists & inhibitors , Male , Mesenteric Arteries/drug effects , Mesenteric Arteries/physiopathology , Metalloendopeptidases/antagonists & inhibitors , Neprilysin/antagonists & inhibitors , Peptide Fragments/metabolism , Protease Inhibitors/pharmacology , Rats , Rats, Wistar , Vasodilation/drug effects , Vasodilator Agents/metabolism
6.
J Biomed Opt ; 7(2): 205-14, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11966305

ABSTRACT

Using scanning confocal microscopy, we measure the backscattered second harmonic signal generated by a 100 fs laser in rat-tail tendon collagen. Damage to the sample is avoided by using a continuous scanning technique, rather than measuring the signal at discrete points. The second harmonic signal varies by about a factor of 2 across a single cross section of the rat-tail tendon fascicle. The signal intensity depends both on the collagen organization and the backscattering efficiency. This implies that we cannot use intensity measurements alone to characterize collagen structure. However, we can infer structural information from the polarization dependence of the second harmonic signal. Axial and transverse scans for different linear polarization angles of the input beam show that second harmonic generation (SHG) in the rat-tail tendon depends strongly on the polarization of the input laser beam. We develop an analytical model for the SHG as a function of the polarization angle in the rat-tail tendon. We apply this model in determining the orientation of collagen fibrils in the fascicle and the ratio gamma between the two independent elements of the second-order nonlinear susceptibility tensor. There is a good fit between our model and the measured data.


Subject(s)
Collagen/chemistry , Microscopy, Confocal/methods , Tendons/chemistry , Animals , Lasers , Microscopy, Confocal/instrumentation , Optics and Photonics/instrumentation , Rats , Scattering, Radiation , Signal Processing, Computer-Assisted , Tail
7.
Lasers Surg Med ; 30(3): 216-20, 2002.
Article in English | MEDLINE | ID: mdl-11891741

ABSTRACT

BACKGROUND AND OBJECTIVE: The purpose of this study was to evaluate the ablation of ossicular tissue using a 1,053 nm Ti:Sapphire chirped pulse amplifier laser system configured to deliver ultrashort pulses of 350 femtoseconds (fs) (3.5x10(-13) seconds) in cadaver temporal bone. STUDY DESIGN/MATERIALS AND METHODS: Ablation of the formalin-fixed incus and stapes was performed using an ultrashort pulse laser (USPL) (0.4 mm beam diameter, pulse fluence of 2.0 J/cm2, and pulse repetition rate of 10 Hz). The ablation rate was measured using optical micrometry, and crater surface morphology examined using scanning electron microscopy. RESULTS: The laser produced precise bone ablation at a rate of 1.26 microm/pulse, with almost no evidence of thermal damage, and very little evidence of photomechanical injury. CONCLUSIONS: Ultrashort pulse lasers may provide a useful clinical tool for otologic and skull base surgery, where precise hard tissue ablation is required adjacent to critical structures.


Subject(s)
Ear Ossicles/surgery , Laser Therapy/methods , Stapes Surgery/methods , Cadaver , Humans , Laser Therapy/adverse effects , Stapes Surgery/adverse effects , Time Factors
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