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  • 1
    Electronic Resource
    Electronic Resource
    Cytochrome P450 Arachidonic Acid ω-Hydroxylation in the Proximal Tubule of the Rat Kidney (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 744 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb52719.x
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  • 2
    Electronic Resource
    Electronic Resource
    The renal cytochrome P-450 arachidonic acid system (1992)
    Springer
    Pediatric nephrology 6 (1992), S. 490-498 
    Details
    ISSN: 1432-198X
    Keywords: Renal cytochrome P-450 ; Arachidonic acid metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In addition to cyclooxygenase and lipoxygenase, arachidonic acid (AA) is metabolized by the cytochrome P-450 monooxygenase system. The kidney is one of the major extrahepatic tissues that display cytochrome P-450 enzyme activities, in particular the cortex, specifically the proximal tubule demonstrate the highest concentration. AA is metabolized by the renal cytochrome P-450 epoxygenase and ω/ω-1 hydroxylases to epoxyeicosatrienoic acids and ω/ω-1 alcohols (20- and 19-mono-hydroxyeicosatetraenoic acids), respectively. These metabolites possess a broad spectrum of biological and renal effects which include: vasodilation, vasoconstriction, inhibition and stimulation of Na+−K+-ATPase, inhibition of ion transport mechanisms, natriuresis, inhibition of renin release and stimulation of cell growth. These metabolites are endogenous constituents of the kidney and are present in urine with increasing concentration under pathological conditions such as pregnancy-induced hypertension. The cytochrome P-450-dependent metabolism of AA is specifically localized to the proximal tubule and exhibits developmental changes, i.e., renal production of metabolites is very low in the fetus, newborn and up to 3 weeks of age, after which a remarkable increase in enzyme activities is observed. These characteristics call attention to the importance of this enzyme system in producing cellular mediators for regulating renal function in normal and diseased states.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00874022
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  • 3
    Electronic Resource
    Electronic Resource
    Role of heme oxygenase in heme-mediated inhibition of rat brain Na+−K+-ATPase: Protection by tin-protoporphyrin (1989)
    Springer
    Neurochemical research 14 (1989), S. 861-864 
    Details
    ISSN: 1573-6903
    Keywords: Heme oxygenase ; brain Na+−K+-ATPase ; heme ; iron ; tin-protoporphyrin ; rat brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Hemoglobin has been shown to inhibit brain Na+−K+-ATPase through an iron-dependent mechanism. Both hemoglobin and iron cause spontaneous peroxidation of brain lipids. Release of iron from the heme molecule in animal tissues is dependent on the activity of heme oxygenase. We hypothesized that inhibition of heme catabolism by heme oxygenase prevents the iron-mediated inhibition of Na+−K+-ATPase and might subsequently reduce the tissue damage. Therefore, we studied the effect of heme and tin-protoporphyrin, an inhibitor of heme oxygenase, on the activity of partially purified Na+−K+-ATPase from rat brain in the presence and absence of purified hepatic heme oxygenase. Heme alone at a concentration of 30 μM did not inhibit Na+−K+-ATPase. However, in the presence of heme oxygenase, heme inhibited Na+−K+-ATPase by 75%. Pretreatment of rats with SnCl2, a known inducer of heme oxygenase, reduced the basal activity of the brain Na+−K+-ATPase by 50%. Inhibition of heme oxygenase by tin-protoporphyrin (30 μM) prevented the inhibition of Na+−K+-ATPase which occurred in the presence of heme and heme oxygenase. It is concluded that suppression of heme oxygenase by tin-protoporphyrin might be a therapeutic approach to management of hemoglobin-associated brain injury following CNS hemorrhage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964815
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  • 4
    Electronic Resource
    Electronic Resource
    Differential heme oxygenase induction by stannous and stannic ions in the heart (1995)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 57 (1995), S. 409-414 
    Details
    ISSN: 0730-2312
    Keywords: heme ; heme oxygenase ; mRNA ; tin ; heart ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Heme oxygenase is the rate-limiting enzyme in heme catabolism, and is induced by oxidative stress, foreign and endogenous chemicals, and many trace elements and heavy metals. This study examined the effect of the oxidative state of the heavy metal tin, on heme oxygenase-1 induction in cardiac tissue. Subcutaneous administration of stannous and stannic chloride failed to induce the enzyme in this tissue. Atomic absorption spectroscopy revealed the absence of tin in the heart cells. Investigation of several metal formulations showed that both stannous and stannic citrate were able to enter the bloodstream from the injection site and into heart tissue. Northern blot analysis revealed that heme oxygenase-1 mRNA was elevated several-fold in rat hearts from animals which received either stannous or stannic citrate, and that mRNA levels corresponded with the increase in enzyme activity. The presence of citrate facilitated the transport of the tin ion into the blood stream and possibly across cardiac cell membrane. The stannous ion was more potent as an inducer of heme oxygenase than was the stannic ion.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240570306
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  • 5
    Electronic Resource
    Electronic Resource
    Localization of erythropoietin mRNA in the rat kidney by polymerase chain reaction (1994)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 54 (1994), S. 239-246 
    Details
    ISSN: 0730-2312
    Keywords: gene expression ; microdissection ; nephron segments ; endothelial cells ; in situ hybridization ; erythropoiesis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Erythropoietin (Epo) is a glycoprotein secreted by kidney cells which plays an important role in the regulation of erythropoiesis. Localization of the Epo production by immunohistochemical studies and in situ hybridization has not been definitively established and is still a matter of controversy. Epo and glyceraldehyde 3-dehydrogenase (GAPDH) mRNA levels were determined in total RNA isolated from control and CoCl2-treated rats using a coupled reverse transcriptase/polymerase chain reaction method (RT/PCR). As indicated by the amount of amplification product, Epo mRNA levels were several-fold higher in CoCl2-treated rat kidney. In contrast, GAPDH mRNA levels were similar in control and CoCl2-treated rats. This RT/PCR method was also used to assess the level of Epo and GAPDH mRNA in microdissected nephron segments. All nephron segments tested lacked any detectable levels of Epo mRNA in either control or CoCl2-treated rats. On the other hand, peritubular cells (capillary fraction: afferent/efferent arteriole, vasa recta) were the only cells where the Epo mRNA was detected. Using a specific primer for GAPDH, the RT/PCR method could identify GAPDH mRNA in all microdissected nephron segments where the Epo mRNA was not expressed. Thus, a combination of microdissected nephron segments and RT/PCR enabled us to detect GAPDH mRNA populations in all nephron segments, whereas the failure to detect Epo mRNA in all segments but the capillary fraction, is due to the specific and localized expression of the Epo gene to this fraction.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240540212
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  • 6
    Electronic Resource
    Electronic Resource
    Gene transfer of human heme oxygenase into coronary endothelial cells potentially promotes angiogenesis (1998)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 68 (1998), S. 121-127 
    Details
    ISSN: 0730-2312
    Keywords: heme oxygenase ; stress protein ; overexpression ; oxidative injury ; endothelial cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Heme oxygenase (HO-1) is a stress protein that has been suggested to participate in defense mechanisms against agents that induce oxidative injury such as hemoglobin/heme, hypoxia-ischemia and cytokines. Overexpression of HO-1 in endothelial cells (EC) might, therefore, protect against oxidative stress produced under these pathological conditions, by generation of CO, a vasodilator, and bilirubin, which has antioxidant properties that enhance blood vessel formation to counteract hypoxia-induced injury. A plasmid containing the cytomegalovirus promoter (pCMV) neomycin human HO-1 gene complexed to cationic liposomes, lipofectin, was used to transfect rabbit coronary microvessel EC. Cells transfected with human HO-1 gene demonstrated a twofold increase in HO activity and maintained a similar phenotype as in the nontransfected cells. Cell number in transfected cells with human HO-1 gene increased by about 45%, as compared to nontransfected or those transfected with control pCMV. Transfected and nontransfected EC revealed a similar response to basic fibroblast growth factor (bFGF) in capillary formation. However, transfected cells with the human HO-1 gene exhibited a twofold increase in blood vessel formation. The angiogenic response of EC to overexpression of HO-1 gene provides direct evidence that the inductive form of HO-1 following injury represents an important tissue adaptive mechanism for moderating the severity of cell damage produced in inflammatory reaction sites of hemorrhage, thrombosis and hypoxic-ischemia. Thus, HO-1 may participate in the regulation of EC activation, proliferation and angiogenesis. J. Cell. Biochem. 68:121-127, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Quantitative measurement of heme oxygenase-1 in the human renal adenocarcinoma (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 63 (1996), S. 342-348 
    Details
    ISSN: 0730-2312
    Keywords: heme oxygenase ; stress protein ; adenocarcinoma ; cancer ; RT/PCR ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Heme oxygenase (HO-1) is the rate-limiting enzyme in heme catabolism. HO-1, a stress protein, has been suggested to be involved in defense mechanisms against agents that may induce oxidative stress. It has been proposed that renal HO gene expression regulates important hemoprotein(s) such as cytochrome P450 and may be essential to maintain homeostasis in the kidney. Because accurate assessment of HO-1 mRNA in normal and disease states in kidney were not available due to the limited number of cells, we developed a system to quantitate human HO-1 mRNA in samples limited in cell number and/or mRNA copies. Total RNA from human kidney was used to establish this technique; it was reverse-transcribed and then amplified by polymerase chain reaction (PCR) in a tube also containing an internal standard obtained by deleting 50 bp from the original human HO-1 gene. This allowed us to use the same primers for both the sample and internal standard. After amplification, templates were resolved by acrylamide gel electrophoresis and quantitated either by densitometry or radioactivity counted from the bands excised from the gel. When the internal standard is present in the reaction mixture, the ratio of amplified sample vs. the standard template is proportional to the amount of sample RNA, and it is therefore possible to calculate the number of specific mRNA molecules. We have used this approach to quantitate the number of HO-1 mRNA molecules in adenocarcinoma cells. Results show that reverse transcription (RT)/PCR methods were able to determine the number of HO-1 mRNA copies in biopsy samples of human adenocarcinoma cells. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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