Isotope effect studies of chicken liver NADP malic enzyme: role of the metal ion and viscosity dependence

Biochemistry ◽  
1988 ◽  
Vol 27 (8) ◽  
pp. 2927-2934 ◽  
Author(s):  
Charles B. Grissom ◽  
W. W. Cleland
Keyword(s):  
Isotope Effect ◽  
Malic Enzyme ◽  
Metal Ion ◽  
Chicken Liver ◽  
Viscosity Dependence

scholarly journals The role of malic enzyme in the regulation of lipid accumulation in filamentous fungi

Microbiology ◽  
1999 ◽  
Vol 145 (8) ◽  
pp. 1911-1917 ◽  
Author(s):  
James P. Wynn ◽  
Aidil bin Abdul Hamid ◽  
Colin Ratledge
Keyword(s):  
Filamentous Fungi ◽  
Lipid Accumulation ◽  
Malic Enzyme

scholarly journals Role of hepcidin in oxidative stress and cell death of cultured mouse renal collecting duct cells: protection against iron and sensitization to cadmium

2021 ◽  
Author(s):  
Stephanie Probst ◽  
Johannes Fels ◽  
Bettina Scharner ◽  
Natascha A. Wolff ◽  
Eleni Roussa ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Death ◽  
Cell Fate ◽  
Catalase Activity ◽  
Metal Ion ◽  
Iron Homeostasis ◽  
Collecting Duct ◽  
Duct Cell ◽  
Plasmid Transfection

AbstractThe liver hormone hepcidin regulates systemic iron homeostasis. Hepcidin is also expressed by the kidney, but exclusively in distal nephron segments. Several studies suggest hepcidin protects against kidney damage involving Fe2+ overload. The nephrotoxic non-essential metal ion Cd2+ can displace Fe2+ from cellular biomolecules, causing oxidative stress and cell death. The role of hepcidin in Fe2+ and Cd2+ toxicity was assessed in mouse renal cortical [mCCD(cl.1)] and inner medullary [mIMCD3] collecting duct cell lines. Cells were exposed to equipotent Cd2+ (0.5–5 μmol/l) and/or Fe2+ (50–100 μmol/l) for 4–24 h. Hepcidin (Hamp1) was transiently silenced by RNAi or overexpressed by plasmid transfection. Hepcidin or catalase expression were evaluated by RT-PCR, qPCR, immunoblotting or immunofluorescence microscopy, and cell fate by MTT, apoptosis and necrosis assays. Reactive oxygen species (ROS) were detected using CellROX™ Green and catalase activity by fluorometry. Hepcidin upregulation protected against Fe2+-induced mIMCD3 cell death by increasing catalase activity and reducing ROS, but exacerbated Cd2+-induced catalase dysfunction, increasing ROS and cell death. Opposite effects were observed with Hamp1 siRNA. Similar to Hamp1 silencing, increased intracellular Fe2+ prevented Cd2+ damage, ROS formation and catalase disruption whereas chelation of intracellular Fe2+ with desferrioxamine augmented Cd2+ damage, corresponding to hepcidin upregulation. Comparable effects were observed in mCCD(cl.1) cells, indicating equivalent functions of renal hepcidin in different collecting duct segments. In conclusion, hepcidin likely binds Fe2+, but not Cd2+. Because Fe2+ and Cd2+ compete for functional binding sites in proteins, hepcidin affects their free metal ion pools and differentially impacts downstream processes and cell fate.

scholarly journals Catalytic and structural role of the metal ion in dUTP pyrophosphatase

2003 ◽  
Vol 100 (10) ◽  
pp. 5670-5675 ◽  
Author(s):  
D. Mustafi ◽  
A. Bekesi ◽  
B. G. Vertessy ◽  
M. W. Makinen
Keyword(s):  
Metal Ion ◽  
Structural Role

Thermally Induced Electron Transfer in a CsCoFe Prussian Blue Derivative: The Specific Role of the Alkali-Metal Ion

2004 ◽  
Vol 116 (28) ◽  
pp. 3814-3817 ◽  
Author(s):  
Anne Bleuzen ◽  
Virginie Escax ◽  
Alban Ferrier ◽  
Françoise Villain ◽  
Michel Verdaguer ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Alkali Metal ◽  
Prussian Blue ◽  
Metal Ion ◽  
Specific Role ◽  
Alkali Metal Ion ◽  
Thermally Induced
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