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Article ; Online: Another tool in the toolkit to manage iron overload.

Philpott, Caroline C

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 31, Page(s) e2208868119

MeSH term(s)	Humans ; Iron Chelating Agents/therapeutic use ; Iron Overload/drug therapy
Chemical Substances	Iron Chelating Agents
Language	English
Publishing date	2022-07-26
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2208868119
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Article ; Online: Iron on the move: mobilizing liver iron via NCOA4.

Philpott, Caroline C

Blood

2020 Volume 136, Issue 23, Page(s) 2604–2605

MeSH term(s)	Animals ; Erythropoiesis ; Ferritins ; Iron/metabolism ; Liver/metabolism ; Mice ; Nuclear Receptor Coactivators/metabolism
Chemical Substances	NcoA4 protein, mouse ; Nuclear Receptor Coactivators ; Ferritins (9007-73-2) ; Iron (E1UOL152H7)
Language	English
Publishing date	2020-12-03
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2020007971
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Article ; Online: The flux of iron through ferritin in erythrocyte development.

Philpott, Caroline C

Current opinion in hematology

2018 Volume 25, Issue 3, Page(s) 183–188

Abstract: Purpose of review: Terminal differentiation of erythropoietic progenitors requires the rapid accumulation of large amounts of iron, which is transported to the mitochondria, where it is incorporated into heme. Ferritin is the sole site of iron storage ... ...

Abstract	Purpose of review: Terminal differentiation of erythropoietic progenitors requires the rapid accumulation of large amounts of iron, which is transported to the mitochondria, where it is incorporated into heme. Ferritin is the sole site of iron storage present in the cytosol. Yet the role of iron accumulation into ferritin in the context of red cell development had not been clearly defined. Early studies indicated that at the onset of terminal differentiation, iron initially accumulates in ferritin and precedes heme synthesis. Whether this accumulation is physiologically important for red cell development was unclear until recent studies defined an obligatory pathway of iron flux through ferritin. Recent findings: The iron chaperone functions of poly rC-binding protein 1 (PCBP1) and the autophagic cargo receptor for ferritin, nuclear co-activator 4 (NCOA4) are required for the flux of iron through ferritin in developing red cells. In the absence of these functions, iron delivery to mitochondria for heme synthesis is impaired. Summary: The regulated trafficking of iron through ferritin is important for maintaining a consistent flow of iron to mitochondria without releasing potentially damaging redox-active species in the cell. Other components of the iron trafficking machinery are likely to be important in red cell development.
MeSH term(s)	Animals ; Cytosol/metabolism ; Erythrocytes/cytology ; Erythrocytes/metabolism ; Erythropoiesis/physiology ; Ferritins/metabolism ; Heme/biosynthesis ; Heterogeneous-Nuclear Ribonucleoproteins/metabolism ; Humans ; Iron/metabolism ; Nuclear Receptor Coactivators/metabolism
Chemical Substances	Heterogeneous-Nuclear Ribonucleoproteins ; NCOA4 protein, human ; Nuclear Receptor Coactivators ; PCBP1 protein, human ; Heme (42VZT0U6YR) ; Ferritins (9007-73-2) ; Iron (E1UOL152H7)
Language	English
Publishing date	2018-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/MOH.0000000000000417
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Article ; Online: Pumping iron.

Philpott, Caroline C

eLife

2014 Volume 3, Page(s) e03997

Abstract: The primary role of the ZIP13 metal transporter in flies is to move iron ions out of cells, rather than moving zinc ions into cells, as is the case in human cells. ...

Abstract	The primary role of the ZIP13 metal transporter in flies is to move iron ions out of cells, rather than moving zinc ions into cells, as is the case in human cells.
MeSH term(s)	Animals ; Cation Transport Proteins/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Ehlers-Danlos Syndrome/metabolism ; Humans ; Secretory Pathway/genetics
Chemical Substances	Cation Transport Proteins ; Drosophila Proteins ; SLC39A13 protein, human
Language	English
Publishing date	2014-08-15
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.03997
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Article ; Online: PCBP2 post-transcriptionally regulates sortilin expression by binding to a C-rich element in its 3' UTR.

Yabe-Wada, Toshiki / Philpott, Caroline C / Onai, Nobuyuki

FEBS open bio

2020 Volume 10, Issue 3, Page(s) 407–413

Abstract: ... mechanism employed by PCBP1. PCBP2 recognized the C-rich element in the 3' UTR of sortilin mRNA, and PCBP2 ...

Abstract	Post-transcriptional regulation of cytokine production is crucial to ensure appropriate immune responses. We previously demonstrated that poly-rC-binding protein-1 (PCBP1) can act as a trans-acting factor to stabilize transcripts encoding sortilin, which mediates cytokine trafficking. Here, we report that PCBP2, which strongly resembles PCBP1, can stabilize sortilin transcripts in macrophages using the same mechanism employed by PCBP1. PCBP2 recognized the C-rich element in the 3' UTR of sortilin mRNA, and PCBP2 knockdown decreased sortilin transcripts, indicating that PCBP2 stabilizes sortilin mRNA by binding to its 3' UTR. Zn
Language	English
Publishing date	2020-02-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	2651702-4
ISSN	2211-5463 ; 2211-5463
ISSN (online)	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12794
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Article ; Online: Management versus miscues in the cytosolic labile iron pool: The varied functions of iron chaperones.

Philpott, Caroline C / Patel, Sarju J / Protchenko, Olga

Biochimica et biophysica acta. Molecular cell research

2020 Volume 1867, Issue 11, Page(s) 118830

Abstract: ... on the major iron chaperone protein coordinating the labile iron pool: poly C-binding protein 1. ...

Abstract	Iron-containing proteins rely on the incorporation of a set of iron cofactors for activity. The cofactors must be synthesized or assembled from raw materials located within the cell. The chemical nature of this pool of raw material - referred to as the labile iron pool - has become clearer with the identification of micro- and macro-molecules that coordinate iron within the cell. These molecules function as a buffer system for the management of intracellular iron and are the focus of this review, with emphasis on the major iron chaperone protein coordinating the labile iron pool: poly C-binding protein 1.
MeSH term(s)	Cytosol/metabolism ; DNA-Binding Proteins/genetics ; Fatty Liver/genetics ; Fatty Liver/pathology ; Ferroptosis/genetics ; Glutathione/genetics ; Glutathione/metabolism ; Humans ; Iron/metabolism ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/metabolism ; Molecular Chaperones/genetics ; RNA-Binding Proteins/genetics
Chemical Substances	DNA-Binding Proteins ; Iron-Sulfur Proteins ; Molecular Chaperones ; PCBP1 protein, human ; RNA-Binding Proteins ; Iron (E1UOL152H7) ; Glutathione (GAN16C9B8O)
Language	English
Publishing date	2020-08-21
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2020.118830
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Article ; Online: The ins and outs of iron: Escorting iron through the mammalian cytosol.

Philpott, Caroline C / Jadhav, Shyamalagauri

Free radical biology & medicine

2018 Volume 133, Page(s) 112–117

Abstract: Mammalian cells contain thousands of metalloproteins and have evolved sophisticated systems for ensuring that metal cofactors are correctly assembled and delivered to their proper destinations. Equally critical in this process are the strategies to avoid ...

Abstract	Mammalian cells contain thousands of metalloproteins and have evolved sophisticated systems for ensuring that metal cofactors are correctly assembled and delivered to their proper destinations. Equally critical in this process are the strategies to avoid the insertion of the wrong metal cofactor into apo-proteins and to avoid the damage that redox-active metals can catalyze in the cellular milieu. Iron and zinc are the most abundant metal cofactors in cells and iron cofactors include heme, iron-sulfur clusters, and mono- and dinuclear iron centers. Systems for the intracellular trafficking of iron cofactors are being characterized. This review focuses on the trafficking of ferrous iron cofactors in the cytosol of mammalian cells, a process that involves specialized iron-binding proteins, termed iron chaperones, of the poly rC-binding protein family.
MeSH term(s)	Animals ; Cytosol/metabolism ; Heme/genetics ; Heme/metabolism ; Humans ; Iron/metabolism ; Iron-Binding Proteins/genetics ; Iron-Binding Proteins/metabolism ; Iron-Sulfur Proteins/genetics ; Iron-Sulfur Proteins/metabolism ; Metalloproteins/genetics ; Metalloproteins/metabolism ; Molecular Chaperones/metabolism ; Sulfur/metabolism
Chemical Substances	Iron-Binding Proteins ; Iron-Sulfur Proteins ; Metalloproteins ; Molecular Chaperones ; Heme (42VZT0U6YR) ; Sulfur (70FD1KFU70) ; Iron (E1UOL152H7)
Language	English
Publishing date	2018-10-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2018.10.411
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Article: Iron-tracking strategies: Chaperones capture iron in the cytosolic labile iron pool.

Philpott, Caroline C / Protchenko, Olga / Wang, Yubo / Novoa-Aponte, Lorena / Leon-Torres, Andres / Grounds, Samantha / Tietgens, Amber J

Frontiers in molecular biosciences

2023 Volume 10, Page(s) 1127690

Abstract: ... in mammalian cells. The first identified iron chaperone, poly C-binding protein 1 (PCBP1), has also been ...

Abstract	Cells express hundreds of iron-dependent enzymes that rely on the iron cofactors heme, iron-sulfur clusters, and mono-or di-nuclear iron centers for activity. Cells require systems for both the assembly and the distribution of iron cofactors to their cognate enzymes. Proteins involved in the binding and trafficking of iron ions in the cytosol, called cytosolic iron chaperones, have been identified and characterized in mammalian cells. The first identified iron chaperone, poly C-binding protein 1 (PCBP1), has also been studied in mice using genetic models of conditional deletion in tissues specialized for iron handling. Studies of iron trafficking in mouse tissues have necessitated the development of new approaches, which have revealed new roles for PCBP1 in the management of cytosolic iron. These approaches can be applied to investigate use of other nutrient metals in mammals.
Language	English
Publishing date	2023-02-02
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2814330-9
ISSN	2296-889X
ISSN	2296-889X
DOI	10.3389/fmolb.2023.1127690
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Article ; Online: The iron chaperone poly(rC)-binding protein 1 regulates iron efflux through intestinal ferroportin in mice.

Wang, Yubo / Protchenko, Olga / Huber, Kari D / Shakoury-Elizeh, Minoo / Ghosh, Manik C / Philpott, Caroline C

Blood

2023 Volume 142, Issue 19, Page(s) 1658–1671

Abstract: Iron is an essential nutrient required by all cells but used primarily for red blood cell production. Because humans have no effective mechanism for ridding the body of excess iron, the absorption of dietary iron must be precisely regulated. The critical ...

Abstract	Iron is an essential nutrient required by all cells but used primarily for red blood cell production. Because humans have no effective mechanism for ridding the body of excess iron, the absorption of dietary iron must be precisely regulated. The critical site of regulation is the transfer of iron from the absorptive enterocyte to the portal circulation via the sole iron efflux transporter, ferroportin. Here, we report that poly(rC)-binding protein 1 (PCBP1), the major cytosolic iron chaperone, is necessary for the regulation of iron flux through ferroportin in the intestine of mice. Mice lacking PCBP1 in the intestinal epithelium exhibit low levels of enterocyte iron, poor retention of dietary iron in enterocyte ferritin, and excess efflux of iron through ferroportin. Excess iron efflux occurred despite lower levels of ferroportin protein in enterocytes and upregulation of the iron regulatory hormone hepcidin. PCBP1 deletion and the resulting unregulated dietary iron absorption led to poor growth, severe anemia on a low-iron diet, and liver oxidative stress with iron loading on a high-iron diet. Ex vivo culture of PCBP1-depleted enteroids demonstrated no defects in hepcidin-mediated ferroportin turnover. However, measurement of kinetically labile iron pools in enteroids competent or blocked for iron efflux indicated that PCBP1 functioned to bind and retain cytosolic iron and limit its availability for ferroportin-mediated efflux. Thus, PCBP1 coordinates enterocyte iron and reduces the concentration of unchaperoned "free" iron to a low level that is necessary for hepcidin-mediated regulation of ferroportin activity.
MeSH term(s)	Humans ; Mice ; Animals ; Iron/metabolism ; Hepcidins/genetics ; Hepcidins/metabolism ; Iron, Dietary/metabolism ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Intestines ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Iron Overload
Chemical Substances	Iron (E1UOL152H7) ; Hepcidins ; metal transporting protein 1 ; Iron, Dietary ; Cation Transport Proteins ; Molecular Chaperones
Language	English
Publishing date	2023-08-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2023020504
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Article ; Online: Vitamin E Induces Liver Iron Depletion and Alters Iron Regulation in Mice.

Baratz, Ethan / Protchenko, Olga / Jadhav, Shyamalagauri / Zhang, Deliang / Violet, Pierre-Christian / Grounds, Samantha / Shakoury-Elizeh, Minoo / Levine, Mark / Philpott, Caroline C

The Journal of nutrition

2023 Volume 153, Issue 7, Page(s) 1866–1876

Abstract: Background: Vitamin E (vit E) is an essential nutrient that functions as a lipophilic antioxidant and is used clinically to treat nonalcoholic fatty liver disease, where it suppresses oxidative damage and impedes the progression of steatosis and ... ...

Abstract	Background: Vitamin E (vit E) is an essential nutrient that functions as a lipophilic antioxidant and is used clinically to treat nonalcoholic fatty liver disease, where it suppresses oxidative damage and impedes the progression of steatosis and fibrosis. Mice lacking a critical liver iron-trafficking protein also manifest steatosis because of iron-mediated oxidative damage and are protected from liver disease by oral vit E supplements. Objectives: We aimed to examine the role of dietary vit E supplementation in modulating iron-sensing regulatory systems and nonheme iron levels in mouse liver. Methods: C57Bl/6 male mice, aged 6 wk, were fed purified diets containing normal amounts of iron and either control (45 mg/kg) or elevated (450 mg/kg) levels of 2R-α-tocopherol (vit E) for 18 d. Mouse plasma and liver were analyzed for nonheme iron, levels and activity of iron homeostatic proteins, and markers of oxidative stress. We compared means ± SD for iron and oxidative stress parameters between mice fed the control diet and those fed the vit E diet. Results: The Vit E-fed mice exhibited lower levels of liver nonheme iron (38% reduction, P < 0.0001) and ferritin (74% reduction, P < 0.01) than control-fed mice. The levels of liver mRNA for transferrin receptor 1 and divalent metal transporter 1 were reduced to 42% and 57% of the control, respectively. The mRNA levels for targets of nuclear factor erythroid 2-related factor (Nrf2), a major regulator of the oxidative stress response and iron-responsive genes, were also suppressed in vit E livers. Hepcidin, an iron regulatory hormone, levels were lower in the plasma (P < 0.05), and ferroportin (FPN), the iron exporter regulated by hepcidin, was expressed at higher levels in the liver (P < 0.05). Conclusions: Oral vit E supplementation in mice can lead to depletion of liver iron stores by suppressing the iron- and redox-sensing transcription factor Nrf2, leading to enhanced iron efflux through liver FPN. Iron depletion may indirectly enhance the antioxidative effects of vit E.
MeSH term(s)	Mice ; Male ; Animals ; Iron/metabolism ; Vitamin E/pharmacology ; Hepcidins ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; NF-E2-Related Factor 2/pharmacology ; Liver/metabolism ; Antioxidants/metabolism ; RNA, Messenger/genetics ; Mice, Inbred C57BL
Chemical Substances	Iron (E1UOL152H7) ; Vitamin E (1406-18-4) ; Hepcidins ; NF-E2-Related Factor 2 ; Antioxidants ; RNA, Messenger
Language	English
Publishing date	2023-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	218373-0
ISSN	1541-6100 ; 0022-3166
ISSN (online)	1541-6100
ISSN	0022-3166
DOI	10.1016/j.tjnut.2023.04.018
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