Iron speciation study in Hfe knockout mice tissues: Magnetic and ultrastructural characterisation

Gutiérrez, Lucía; Quintana, Carmen; Patiño, Cristina; Bueno, J. Trujillo; Coppin, Hélène; Roth, Marie Paule; Lázaro, Francisco J.

doi:10.1016/j.bbadis.2009.03.007

Cited by 25 publications

(22 citation statements)

References 39 publications

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“…Goethite-like iron particles similar to those observed in these fossil soft tissues have been identified in modern tissues and are possibly derived from HB through formation of ferritin protein-caged iron biominerals [44,[75][76][77][78][79] during degradation. Ferritins are stable proteins that retain activity post-mortem.…”

Section: Discussionmentioning

confidence: 93%

A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time

Schweitzer¹,

et al. 2014

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The persistence of original soft tissues in Mesozoic fossil bone is not explained by current chemical degradation models. We identified iron particles (goethite-aFeO(OH)) associated with soft tissues recovered from two Mesozoic dinosaurs, using transmission electron microscopy, electron energy loss spectroscopy, micro-X-ray diffraction and Fe micro-X-ray absorption nearedge structure. Iron chelators increased fossil tissue immunoreactivity to multiple antibodies dramatically, suggesting a role for iron in both preserving and masking proteins in fossil tissues. Haemoglobin (HB) increased tissue stability more than 200-fold, from approximately 3 days to more than two years at room temperature (258C) in an ostrich blood vessel model developed to test post-mortem 'tissue fixation' by cross-linking or peroxidation. HB-induced solution hypoxia coupled with iron chelation enhances preservation as follows: HB þ O 2 . HB 2 O 2 . 2O 2 þO 2 . The well-known O 2 /haeme interactions in the chemistry of life, such as respiration and bioenergetics, are complemented by O 2 /haeme interactions in the preservation of fossil soft tissues.

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Section: Discussionmentioning

confidence: 93%

A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time

Schweitzer¹,

et al. 2014

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“…The complexity of the hysteresis loops (especially for class III sample) may be caused by a multicomponent composition of the samples containing deposits of several magnetic and non-magnetic iron oxides (α-Fe 2 O 3 , γ-Fe 2 O 3 , Fe 3 O 4 ) of different size, shape, and count [34].…”

Section: Discussionmentioning

confidence: 99%

Magnetic Properties of Iron Oxides in the Human Globus pallidus

Kopáni¹,

Hlinkova²,

Ehrlich³

et al. 2017

J Bioanal Biomed

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Postmortem brain tissue sections from Globus pallidus externus were routinely obtained during the autopsy to prepare tissue sections for the pathology diagnosis at Department of pathology, Comenius University, Bratislava. Tissues were taken from individuals without clinical findings of any motor abnormalities, iron metabolism, movements involving limbs, face, and tongues (Table 1). All procedures were conducted in accordance with the Declaration of Helsinki. AbstractSeveral types of iron oxides can be found in the various parts of the human brain. These can be highlighted in the light microscopy and using scanning or transmission mode of the electron microscopy. Some of them are non-magnetic, some, on the contrary, display magnetic response. It is not clear which kind of magnetic particles are accumulated in the human brain as inorganic deposits. Light microscopy, electron microscopy and sensitive Superconducting Quantum Interference Device (SQUID magnetometer) were used in order to detect iron deposits and their magnetic response in the samples extracted from the Globus pallidus of the human brain. Electron microscopy reveals a presence of the single crystals of hematite (α-Fe 2 O 3 ) of the size up to 1000 nm in the samples extracted from G. pallidus because of the diffractograms characteristic for the hexagonal unit cell; this mineral offers basically a diamagnetic response. The temperature dependence of the magnetic susceptibility allows a classification of the samples into three groups: mostly diamagnetic I, prevailing paramagnetic III, and an intermediate class II. The bulk samples exhibit a long-range magnetic ordering with magnetic hysteresis evidenced not only at low temperature but also at the room temperature. The recorded magnetic functions refer either to the presence of magnetite (Fe 3 O 4 ), or maghemite (γ-Fe 2 O 3 ). Iron oxides and oxidohydroxides found as inorganic deposits in the human brain can result from interaction between iron and microenvironment in the form of polysaccharides of glycoconjugates. They display magnetoactivity characteristic for magnetite and/or maghemite.

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“…46 Mouse serum ferritin contains a measurable but low amount of iron. This low iron content and the extreme similarity of the serum and liver ferritin cores, assessed by TEM and AC susceptometry, 30 suggest that the few serum ferritin cages that contain an H-subunit accumulate iron as ferrihydrite as well. The fact that the average iron content of liver ferritin is much higher than the average iron found in serum ferritin, despite the fact that the core sizes are similar, supports the notion that most ferritin in serum is apoferritin.…”

Section: Iron In Serum Ferritinmentioning

confidence: 99%

“…4,29 To broaden the knowledge of serum ferritin to other species and conditions, we characterized mouse serum ferritin in control mice and chemically iron-loaded animals. We used mass spectrometry (MS), transmission electron microscopy (TEM), alternating current (AC) magnetic susceptometry for ferritin-iron core analysis, 30 Western blotting, and glycosylation analysis, along with additional sensitive assays for iron determination, to characterize serum ferritin and to gain further insight into mechanisms of secretion and the possible role of serum ferritin in reallocation of body iron stores. We concluded that murine serum ferritin is mainly secreted by macrophages through a nonclassical secretion process involving secretory lysosomes and not the ER.…”

mentioning

confidence: 99%

Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway

Cohen

Gutiérrez

Weiss

et al. 2010

Blood

386

324

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The serum ferritin concentration is a clinical parameter measured widely for the differential diagnosis of anemia. Its levels increase with elevations of tissue iron stores and with inflammation, but studies on cellular sources of serum ferritin as well as its subunit composition, degree of iron loading and glycosylation have given rise to conflicting results. To gain further understanding of serum ferritin, we have used traditional and modern methodologies to characterize mouse serum ferritin. We find that both splenic macrophages and proximal tubule cells of the kidney are possible cellular sources for serum ferritin and that serum ferritin is secreted by cells rather than being the product of a cytosolic leak from damaged cells. Mouse serum ferritin is composed mostly of L-subunits, whereas it contains few H-subunits and iron content is low. L-subunits of serum ferritin are frequently truncated at the C-terminus, giving rise to a characteristic 17-kD band that has been previously observed in lysosomal ferritin. Taken together with the fact that mouse serum ferritin is not detectably glycosylated, we propose that mouse serum ferritin is secreted through the nonclassical lysosomal secretory pathway. (Blood. 2010;116(9):1574-1584) IntroductionFerritin in mammals is a mostly intracellular, cytosolic iron storage and detoxification protein. It consists of H-and L-subunits that assemble into a 24-subunit hollow sphere in which iron is sequestered. 1 However, ferritin can also be detected extracellularly, in cerebrospinal fluid and sinovial fluid. In serum it is an extracellular ferritin that has been used extensively in diagnostic tests. In the clinical setting, serum ferritin evaluation is most commonly used to estimate body iron stores as low serum ferritin correlates with iron depletion, whereas high serum ferritin correlates with elevated body iron stores or with inflammation in patients with normal body iron stores. 2,3 Characterization of serum ferritin has produced many controversial results regarding subunit composition, iron content and other features. It has been compared in some studies to the "natural apoferritin" fraction found in many tissues, which is essentially devoid of iron 4 while other studies have claimed that serum ferritin contains considerable amounts of iron. 5 In insects, ferritin is a secreted protein composed of 2 types of subunits and the heteropolymer functions most likely as an iron transporter in the hemolymph. Each of the subunits has a classical secretion signal and ferritin is secreted from the insect fat body. 6 In contrast, mammalian H-and L-ferritin subunits lack signals mediating endoplasmic reticulum (ER) targeting, but ferritin can traffic to the lysosomal compartment through autophagy. 7 Binding of human serum ferritin to the lectin Concanavalin A (ConA) has previously suggested that ferritin is glycosylated 8,9 and actively secreted through the ER-Golgi pathway. 10 Indeed, it was shown in hepatocyte cell-models that inhibition of ER-Golgi trafficking abolished secretion o...

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Iron speciation study in Hfe knockout mice tissues: Magnetic and ultrastructural characterisation

Cited by 25 publications

References 39 publications

A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time

A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time

Magnetic Properties of Iron Oxides in the Human Globus pallidus

Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway

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