Cis-Platinum Nephrotoxicity: Changes in Urinary Enzyme Pattern in Patients Submitted to Two Different Dosages1

2015 ◽  
pp. 242-247 ◽  
Author(s):  
Pasquale Coratelli ◽  
Maurizio Antonelli ◽  
Maria S. Giangrande ◽  
Giuseppe Passavanti ◽  
Michele Giannattasio
Keyword(s):  
Urinary Enzyme ◽  
Enzyme Pattern

Urinary enzyme pattern in acute renal failure

1982 ◽  
Vol 394 (S1) ◽  
pp. R24-R24
Author(s):  
P. Kotanko ◽  
G. Gstraunthaler ◽  
W. Pfaller
Keyword(s):  
Renal Failure ◽  
Acute Renal Failure ◽  
Urinary Enzyme ◽  
Enzyme Pattern

Ontogenesis of Tissue Plasminogen Activator in the Human

1971 ◽  
Vol 25 (03) ◽  
pp. 469-480 ◽  
Author(s):  
B Åstedt ◽  
M Pandolfi
Keyword(s):  
Plasminogen Activator ◽  
Tissue Plasminogen Activator ◽  
Vena Cava ◽  
Vasa Vasorum ◽  
Moderate Activity ◽  
Foetal Development ◽  
Plasminogen Activator Activity ◽  
Stage Of Development ◽  
Tissue Plasminogen ◽  
Enzyme Pattern

SummaryThe ontogenesis of tissue plasminogen activator in various tissues was studied in 10 embryos and 58 foetuses with a histochemical method.The first appearance of activator activity was seen in a 4-weeks old embryo. At 8-9 weeks it was seen in the eye, meninges, heart, lungs, kidney and vena cava. In the foetal heart high activity was found in the coronary vessels, which can be regarded as the vasa vasorum of the heart. In the lungs a moderate activity increased at 24 weeks of age, when vascularisation increases more rapidly. Intense activity was seen in the highly vascularized corneoscleral junction of the eye later involved in the drainage of aqueous humor.In the kidney the activity could be related to the vessels, while no activity was seen in the glomeruli, the collecting system or the pelvis. In the vessels the activator activity was fairly high. No activity was seen in any stage of development of the liver.The plasminogen activator activity may be of importance for maintaining the foetomaternal circulation and micro-circulation in rapidly growing foetal organs. In the embryo the enzyme pattern is dominated by protein synthetizing enzymes. During foetal development the enzyme pattern changes owing to supervention of enzymes necessary for the function of the various organs. Plasminogen activator belongs to this latter group. The appearance of plasminogen activator activity may therefore be regarded mainly as a sign of functional maturity of the foetal organs.

The diagnostic value of urinary enzyme measurements in hypertension

1983 ◽  
Vol 133 (3) ◽  
pp. 317-325 ◽  
Author(s):  
Ian D.A. Johnston ◽  
Norman F. Jones ◽  
John E. Scoble ◽  
Chun-Ting Yuen ◽  
Robert G. Price
Keyword(s):  
Diagnostic Value ◽  
Urinary Enzyme

scholarly journals Superoxide dismutase, glutathione peroxidase and catalase in developing rat brain

1982 ◽  
Vol 204 (2) ◽  
pp. 535-540 ◽  
Author(s):  
I Mavelli ◽  
A Rigo ◽  
R Federico ◽  
M R Ciriolo ◽  
G Rotilio
Keyword(s):  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Rat Brain ◽  
Rat Hepatocytes ◽  
Mitochondrial Fraction ◽  
Cytoplasmic Fraction ◽  
Mouse Ascites ◽  
Enzyme Pattern ◽  
Relative Deficiency ◽  
The Brain

The specific activities of Cu, Zn- and Mn-superoxide dismutases, of glutathione peroxidase and of catalase, the enzymes considered to be specifically involved in the defence of the cell against the partially reduced forms of oxygen, were determined as the function of postnatal age in the early (up to 60 days) period of rat brain development. The enzymes were assayed in the cytoplasmic fraction, in the crude mitochondrial fraction including peroxisomes, and in the mitochondria. The results show that the temporal changes of these enzymes cannot be correlated with each other, thus indicating that they do not concertedly parallel the increasing activity of aerobic brain metabolism during development. Specifically the cytoplasmic fraction shows a gradual increase of the Cu, Zn-superoxide dismutase activity with age, whereas the glutathione peroxidase activity is constant from birth. Furthermore the increase of the mitochondrial Mn-superoxide dismutase as a function of postnatal age is more remarkable than that of the cytoplasmic Cu, Zn-enzyme. Higher activities of catalase in adult animals are detectable only in the subcellular fraction containing peroxisomes, because of the modest catalase activity of the brain. These results indicate independent regulation of the expression of these enzyme activities in the process of brain differentiation and point to a relative deficiency of enzymic protection of the brain differentiation and point to a relative deficiency of enzymic protection of the brain against potentially toxic oxygen derivatives. This situation is similar to the pattern already described in the rat heart and in rat and mouse ascites-tumour cells, at variance with the much more efficient enzyme pattern present in rat hepatocytes.

ELECTROPHORETIC EVIDENCE FOR ISOZYMES OF ARYLAMIDASE ("AMINOPEPTIDASE") IN THE RAT. I. RENAL, SERUM AND URINARY ENZYMES SPLITTING dl-ALANYL-2-NAPHTHYLAMIDE AND l-LEUCYL-2-NAPHTHYLAMIDE

1964 ◽  
Vol 12 (12) ◽  
pp. 869-874 ◽  
Author(s):  
BENITO MONIS
Keyword(s):  
Present Report ◽  
Molecular Forms ◽  
Supernatant Fraction ◽  
Blood Levels ◽  
Rat Tissues ◽  
Bilateral Nephrectomy ◽  
Rat Urine ◽  
Urinary Enzyme ◽  
Renal Ablation ◽  
Starting Point

Bilateral nephrectomy elicited no changes of serum blood levels of arylamidase assayed with two chromogenic substrates (l-leucyl-2-naphthylamide and dl-alanyl-2-naphthylamide) two days after the operation. Since rat urine contains similar enzymes it was postulated that the urinary enzyme is of renal origin and distinct from serum arylamidase. For this purpose, electrophoretic studies were undertaken. Starch block (for quantitative determinations) and starch gel for zymograms of arylamidase were used. It was shown that both procedures demonstrated the identity of urinary and renal arylamidase, which was distinct from the serum enzyme. The renal and urinary enzyme showed two distinct isozymes: one remaining at the origin and the other migrating somewhat less than the isozyme in serum. It is postulated that the isozyme remaining at the origin corresponds to a membrane-bound form, whereas the electrophoretically-mobile isozyme is found in the cellular supernatant fraction. The arylamidase from serum was represented by a single enzyme which migrated farthest towards the anode. Histochemical procedures for the demonstration of arylamidase activity in tissues at the light microscopic level permit the localization of enzyme(s) that can hydrolyze synthetic chromogenic naphthylamides containing l-leucyl and dl-alanyl groups (1). Rat kidneys have a high concentration of histochemically demonstrable arylamidase in the proximal convoluted tubules (2). Blood levels of arylamidase in the normal adult rat vary within a narrow range (3). The observation of arylamidase activity in rat urine raised several questions that led to the studies which are the basis of the present report. The relationship of serum and urinary arylamidase was the starting point of this investigation. It was speculated that if the urinary enzyme had its origin in the serum, bilateral nephrectomy should alter blood levels of the enzyme. If no such changes occurred, this would suggest that the urinary enzyme was released from the proximal convoluted tubule. In fact, total renal ablation led to no significant variation of serum arylamidase activity. It was therefore postulated that urinary arylamidase originated in the kidneys and that both are distinct from serum arylamidase. To test this hypothesis, zone electrophoretic studies were undertaken using two different supporting media. It will be shown that distinct molecular forms or isozymes of arylamidase can be separated from rat tissues and fluids by differential electrophoretic mobility. The electrophoretic identity of urinary and renal arylamidase, both of which are distinct from the serum arylamidase, is demonstrated in this study.

Effect of Amikacin and Gentamicin on Urinary Enzyme Excretion

1983 ◽  
Vol 17 (10) ◽  
pp. 752-753
Author(s):  
Juan Jimenez-Alonso ◽  
Luciano Barrios ◽  
Rafael Bejarano ◽  
Laura Jaimez ◽  
Francisco Perez-Jimenez ◽  
...  
Keyword(s):  
Urinary Enzyme ◽  
Urinary Enzyme Excretion
Sign in / Sign up

Export Citation Format

Share Document