Non-reductive iron release from horse spleen ferritin using desferoxamine chelation

2011 ◽  
Vol 105 (2) ◽  
pp. 202-207 ◽  
Author(s):  
Joseph Johnson ◽  
Jason Kenealey ◽  
Robert J. Hilton ◽  
David Brosnahan ◽  
Richard. K. Watt ◽  
...  
Keyword(s):  
Iron Release ◽  
Horse Spleen Ferritin

scholarly journals Electron transfer between horse ferritin and ferrihaemoproteins

1991 ◽  
Vol 278 (3) ◽  
pp. 817-820 ◽  
Author(s):  
F H A Kadir ◽  
F K al-Massad ◽  
S J A Fatemi ◽  
H K Singh ◽  
M T Wilson ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Pseudomonas Aeruginosa ◽  
Electron Transfer ◽  
Long Range ◽  
Phosphate Buffer ◽  
Sperm Whale ◽  
Iron Release ◽  
Visible Spectrophotometry ◽  
Ferricytochrome C ◽  
Horse Spleen Ferritin

Reactions of reduced horse spleen ferritin with horse and Saccharomyces cerevisiae ferricytochromes c, cow ferricytochrome b5, sperm-whale metmyoglobin and Pseudomonas aeruginosa ferricytochrome c-551 were investigated by u.v.-visible spectrophotometry. In all cases the reduced ferritin reduced the ferrihaemoproteins. The rate of reduction varied from less than 0.2 M-1.s-1 for metmyoglobin to 1.1 x 10(3) M-1.s-1 for horse ferricytochrome c (0.1 M-phosphate buffer, pH 7.4, at 25 degrees C). We conclude that the mechanism of ferrihaemoprotein reduction involves long-range electron transfer through the coat of ferritin and that such electron transfer is rapid enough to account for the rates of iron release observed by other workers in reductive release assays.

scholarly journals Haem binding to horse spleen ferritin and its effect on the rate of iron release

1992 ◽  
Vol 282 (3) ◽  
pp. 867-870 ◽  
Author(s):  
F H A Kadir ◽  
F K al-Massad ◽  
G R Moore
Keyword(s):  
Electron Transfer ◽  
Redox Potential ◽  
Molecular Mass ◽  
Functional Role ◽  
Iron Core ◽  
Iron Release ◽  
Horse Spleen Ferritin ◽  
Rate Limiting ◽  
Haem Iron

Horse spleen ferritin is shown to bind haem to generate a haemoprotein, named herein haemoferritin. A total of 14-16 haem molecules are bound per 24 subunits of ferritin. The molecular mass of the non-haem-iron-free haemoferritin has been determined to be 420 +/- 40 kDa, indicating that haem binding does not lead to dissociation of the 24 subunits that comprise the ferritin molecule. The functional role of the bound haem has been investigated with respect to the release of iron from the non-haem iron core. The bound haem is shown to increase the rate of iron release in a reductive assay system. In the absence of haem the rate of iron release depends on the redox potential of the reductant, but in the presence of haem the rate is largely independent of the reductant and is faster than the rate for the haem-free ferritin. These data haem, but in the presence of haem electron transfer is not rate-limiting.

Electrochemically Induced Iron Release of Adsorbed Horse Spleen Ferritin: Quantitation of Iron Using Long Optical Path Length Thin-Layer Spectroelectrochemistry

2007 ◽  
Vol 19 (23) ◽  
pp. 2479-2482 ◽  
Author(s):  
Todd B. Kreutzian ◽  
Khalid S. A. Seraj ◽  
Larry G. Anderson ◽  
Donald C. Zapien
Keyword(s):  
Thin Layer ◽  
Path Length ◽  
Optical Path Length ◽  
Optical Path ◽  
Iron Release ◽  
Horse Spleen Ferritin

scholarly journals CBIO-10. REDUCED IRON EXPORT FUNCTIONS IN A CELL INTRINSIC MANNER TO DRIVE GLIOBLASTOMA GROWTH

2020 ◽  
Vol 22 (Supplement_2) ◽  
pp. ii17-ii17
Author(s):  
Katie Troike ◽  
Erin Mulkearns-Hubert ◽  
Daniel Silver ◽  
James Connor ◽  
Justin Lathia
Keyword(s):  
Tumor Cells ◽  
Iron Uptake ◽  
Iron Homeostasis ◽  
Iron Status ◽  
Tumor Grade ◽  
Hfe Gene ◽  
Iron Release ◽  
Female Patients ◽  
Cellular Iron

Abstract Glioblastoma (GBM), the most common primary malignant brain tumor in adults, is characterized by invasive growth and poor prognosis. Iron is a critical regulator of many cellular processes, and GBM tumor cells have been shown to modulate expression of iron-associated proteins to enhance iron uptake from the surrounding microenvironment, driving tumor initiation and growth. While iron uptake has been the central focus of previous investigations, additional mechanisms of iron regulation, such as compensatory iron efflux, have not been explored in the context of GBM. The hemochromatosis (HFE) gene encodes a transmembrane glycoprotein that aids in iron homeostasis by limiting cellular iron release, resulting in a sequestration phenotype. We find that HFE is upregulated in GBM tumors compared to non-tumor brain and that expression of HFE increases with tumor grade. Furthermore, HFE mRNA expression is associated with significantly reduced survival specifically in female patients with GBM. Based on these findings, we hypothesize that GBM tumor cells upregulate HFE expression to augment cellular iron loading and drive proliferation, ultimately leading to reduced survival of female patients. To test this hypothesis, we generated Hfe knockdown and overexpressing mouse glioma cell lines. We observed significant alterations in the expression of several iron handling genes with Hfe knockdown or overexpression, suggesting global disruption of iron homeostasis. Additionally, we show that knockdown of Hfe in these cells increases apoptosis and leads to a significant impairment of tumor growth in vivo. These findings support the hypothesis that Hfe is a critical regulator of cellular iron status and contributes to tumor aggression. Future work will include further exploration of the mechanisms that contribute to these phenotypes as well as interactions with the tumor microenvironment. Elucidating the mechanisms by which iron effulx contributes to GBM may inform the development of next-generation targeted therapies.

scholarly journals The effect of chelating agents on iron mobilization in Chang cell cultures

Blood ◽  
1976 ◽  
Vol 48 (6) ◽  
pp. 923-929 ◽  
Author(s):  
GP White ◽  
A Jacobs ◽  
RW Grady ◽  
A Cerami
Keyword(s):  
Cell Cultures ◽  
Chelating Agents ◽  
Transferrin Saturation ◽  
Molar Ratio ◽  
Iron Release ◽  
Dihydroxybenzoic Acid ◽  
Equal Degree ◽  
Therapeutic Value ◽  
Chang Cell

Abstract The investigation of chelating agents with potential therapeutic value in patients with transfusional iron overload has been facilitated by the use of Chang cell cultures. These cells have been incubated with [59Fe]transferrin for 22 hr, following which most of the intracellular radioiron is found in the cytosol, distributed between a ferritin and a nonferritin form. Iron release from the cells depends on transferrin saturation in the medium, but when transferrin is 100% saturated, which normally does not allow iron release, desferrioxamine, 2,3- dihydroxybenzoic acid, rhodotorulic acid, cholythydroxamic acid, and tropolone all promote the mobilization of ferritin iron and its release from cells. They are effective to an approximately equal degree. The incubation of [59Fe]transferrin with tropolone in vitro at a molar ratio of 1:500 results in the transfer of most of the labeled iron to the chelator, reflecting the exceptionally high binding constant of this compound. How far these phenomena relate to therapeutic potentially remains to be seen.

Characterization of chemical composition and bacterial community of corrosion scales in different drinking water distribution systems

2017 ◽  
Vol 3 (1) ◽  
pp. 147-155 ◽  
Author(s):  
Haibo Wang ◽  
Chun Hu ◽  
Lang Yin ◽  
Sujia Zhang ◽  
Lizhong Liu
Keyword(s):  
Drinking Water ◽  
Chemical Composition ◽  
Distribution Systems ◽  
Water Distribution ◽  
Iron Release ◽  
Drinking Water Distribution Systems ◽  
Biochemical Function ◽  
Drinking Water Distribution ◽  
Corrosion Scales

There is a relationship between biochemical function and chemical composition of corrosion scales, and Fe3O4formation reduced iron release.

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