Oxidative damage to ferritin by 5-aminolevulinic acid

2003 ◽  
Vol 409 (2) ◽  
pp. 349-356 ◽  
Author(s):  
Maria E.M Rocha ◽  
Fernando Dutra ◽  
Brian Bandy ◽  
Regina L Baldini ◽  
Suely L Gomes ◽  
...  
Keyword(s):  
Oxidative Damage ◽  
Aminolevulinic Acid

scholarly journals Stimulation of the human mitochondrial transporter ABCB10 by zinc-mesoporphrin

PLoS ONE ◽  
2020 ◽  
Vol 15 (11) ◽  
pp. e0238754
Author(s):  
Melissa Martinez ◽  
Gregory A. Fendley ◽  
Alexandra D. Saxberg ◽  
Maria E. Zoghbi
Keyword(s):  
Oxidative Damage ◽  
Atpase Activity ◽  
Animal Studies ◽  
Atp Hydrolysis ◽  
Aminolevulinic Acid ◽  
Negative Control ◽  
Hydrolysis Rate ◽  
Inner Mitochondrial Membrane ◽  
Experimental Conditions ◽  
Mitochondrial Transporter

Heme biosynthesis occurs through a series of reactions that take place within the cytoplasm and mitochondria, so intermediates need to move across these cellular compartments. However, the specific membrane transport mechanisms involved in the process are not yet identified. The ATP-binding cassette protein ABCB10 is essential for normal heme production, as knocking down this transporter in mice is embryonically lethal and accompanied by severe anemia plus oxidative damage. The role of ABCB10 is unknown, but given its location in the inner mitochondrial membrane, it has been proposed as a candidate to export either an early heme precursor or heme. Alternatively, ABCB10 might transport a molecule important for protection against oxidative damage. To help discern between these possibilities, we decided to study the effect of heme analogs, precursors, and antioxidant peptides on purified human ABCB10. Since substrate binding increases the ATP hydrolysis rate of ABC transporters, we have determined the ability of these molecules to activate purified ABCB10 reconstituted in lipid nanodiscs using ATPase measurements. Under our experimental conditions, we found that the only heme analog increasing ABCB10 ATPase activity was Zinc-mesoporphyrin. This activation of almost seventy percent was specific for ABCB10, as the ATPase activity of a negative control bacterial ABC transporter was not affected. The activation was also observed in cysteine-less ABCB10, suggesting that Zinc-mesoporphyrin’s effect did not require binding to typical heme regulatory motifs. Furthermore, our data indicate that ABCB10 was not directly activated by neither the early heme precursor delta-aminolevulinic acid nor glutathione, downsizing their relevance as putative substrates for this transporter. Although additional studies are needed to determine the physiological substrate of ABCB10, our findings reveal Zinc-mesoporphyrin as the first tool compound to directly modulate ABCB10 activity and raise the possibility that some actions of Zinc-mesoporphyrin in cellular and animal studies could be mediated by ABCB10.

Melatonin's antioxidant protection against ?-aminolevulinic acid-induced oxidative damage in rat cerebellum

1997 ◽  
Vol 23 (1) ◽  
pp. 40-46 ◽  
Author(s):  
Fernando G. Princ ◽  
Adela Ana Juknat ◽  
Andrea Grisel Maxit ◽  
Carina Cardalda ◽  
Alcira Battle
Keyword(s):  
Oxidative Damage ◽  
Aminolevulinic Acid ◽  
Antioxidant Protection ◽  
Rat Cerebellum

scholarly journals Stimulation of the human mitochondrial transporter ABCB10 by zinc-mesoporphrin

2020 ◽  
Author(s):  
Melissa Martinez ◽  
Gregory A. Fendley ◽  
Alexandra D. Saxberg ◽  
Maria E. Zoghbi
Keyword(s):  
Oxidative Damage ◽  
Atpase Activity ◽  
Animal Studies ◽  
Atp Hydrolysis ◽  
Aminolevulinic Acid ◽  
Negative Control ◽  
Hydrolysis Rate ◽  
Inner Mitochondrial Membrane ◽  
Experimental Conditions ◽  
Mitochondrial Transporter

AbstractHeme biosynthesis occurs through a series of reactions that take place within the cytoplasm and mitochondria, thus intermediates need to move across these cellular compartments. However, the specific membrane transport mechanisms involved in the process are not yet identified. The ATP-binding cassette protein ABCB10 is essential for normal heme production, as knocking down this transporter in mice is embryonically lethal and accompanied by severe anemia plus oxidative damage. The role of ABCB10 is unknown, but given its location in the inner mitochondrial membrane, it has been proposed as a candidate to export either an early heme precursor or heme. Alternatively, ABCB10 might transport a molecule important for protection against oxidative damage. To help discern between these possibilities, we decided to study the effect of heme analogs, precursors and antioxidant peptides on purified human ABCB10. Since substrate binding increases the ATP hydrolysis rate of ABC transporters, we have determined the ability of these molecules to activate purified ABCB10 reconstituted in lipid nanodiscs using ATPase measurements. Under our experimental conditions, we found that the only heme analog increasing ABCB10 ATPase activity was Zinc-mesoporphyrin. This activation of almost seventy percent was specific for ABCB10, as the ATPase activity of a negative control bacterial ABC transporter was not affected. The activation was also observed in cysteine-less ABCB10, suggesting that Zinc-mesoporphyrin’s effect did not require binding to typical heme regulatory motifs. Furthermore, our data indicate that ABCB10 was not directly activated by neither the early heme precursor delta-aminolevulinic acid nor glutathione, downsizing their relevance as putative substrates for this transporter. Although additional studies are needed to determine the physiological substrate of ABCB10, our findings reveal Zinc-mesoporphyrin as the first tool compound to directly modulate ABCB10 activity and raise the possibility that some actions of Zinc-mesoporphyrin in cellular and animal studies could be mediated by ABCB10.

Calcium-dependent mitochondrial oxidative damage promoted by 5-aminolevulinic acid

1992 ◽  
Vol 1180 (2) ◽  
pp. 201-206 ◽  
Author(s):  
Marcelo Hermes-Lima ◽  
Roger F. Castilho ◽  
Valderez G.R. Valle ◽  
Etelvino J.H. Bechara ◽  
Anibal E. Vercesi
Keyword(s):  
Oxidative Damage ◽  
Aminolevulinic Acid ◽  
Calcium Dependent ◽  
Mitochondrial Oxidative Damage

Oxidative damage of mitochondria induced by 5-aminolevulinic acid: Role of Ca2+ and membrane protein thiols

1994 ◽  
Vol 1188 (1-2) ◽  
pp. 86-92 ◽  
Author(s):  
Anibal E. Vercesi ◽  
Roger F. Castilho ◽  
AndréR. Meinicke ◽  
Valderez G.R. Valle ◽  
Marcelo Hermes-Lima ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Oxidative Damage ◽  
Aminolevulinic Acid ◽  
Protein Thiols

7-Chloro-4-(phenylselanyl) quinoline reduces renal oxidative stress induced by oxaliplatin in mice

2021 ◽  
Author(s):  
Ketlyn P. da Motta ◽  
Briana B. Lemos ◽  
Jaini J. Paltian ◽  
Angélica S Reis ◽  
Gustavo B. Blödorn ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Oxidative Damage ◽  
Aminolevulinic Acid ◽  
Therapeutic Potential ◽  
Thiobarbituric Acid ◽  
Protein Carbonyl ◽  
Glutathione S Transferase ◽  
Protein Thiol ◽  
The Relationship

Purpose: evaluating the relationship between oxidative damage oxaliplatin (OXA)-induced and the therapeutic potential of 7-chloro-4-(phenylselanyl) quinoline (4-PSQ) in kidney of mice. Methods: Mice received OXA (10 mg/kg) or vehicle by intraperitoneal route (days 0 and 2). Oral administration of 4-PSQ (1 mg/kg) or vehicle was performed on days 2 to 14. On day 15, the animals were euthanized, and the kidneys and blood collected. The effect of OXA and/or 4-PSQ on urea, thiobarbituric acid reactive species (TBARS), non-protein thiol (NPSH) and protein carbonyl (PC) levels were investigated. Moreover, renal superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione reductase (GR), glutathione S-transferase (GST), δ-aminolevulinic acid dehydratase (δ-ALA-D) and Na+, K+ ATPase activities were evaluated. Results: Our findings revealed an increase on urea levels and a significant renal oxidative damage in OXA-induced mice. OXA exposure increased SOD, GPx and GST activities and caused a reduction on NPSH levels, CAT and GR activities. Na+, K+ ATPase and -ALA-D activities were reduced by OXA. 4-PSQ decreased plasmatic urea levels and renal oxidative damage. SOD, GPx, CAT, GR and Na+, K+ ATPase activities were restored by 4-PSQ. Conclusion: 4-PSQ may be a good prototype for the treatment of OXA-induced renal injury.

In vivo protection by melatonin against δ-aminolevulinic acid-induced oxidative damage and its antioxidant effect on the activity of haem enzymes

1998 ◽  
Vol 24 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Fernando G. Princ ◽  
Andrea G. Maxit ◽  
Carina Cardalda ◽  
Alcira Batlle ◽  
Adela Ana Juknat
Keyword(s):  
Oxidative Damage ◽  
Aminolevulinic Acid ◽  
Antioxidant Effect

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

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