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Ferritin levels after ferrous fumarate supplementation in the 2nd trimester of pregnancy
Published in Cut Adeya Adella, Stem Cell Oncology, 2018
Ferritin is a protein that is present in almost all cells. The water-soluble iron-containing protein comprises a protein (apoferritin) shell, which is a combination of ferric salts with proteins and inticristalin comprising thousands of ferrioxihydroxide molecules (Fleming & Bacon, 2005). Free iron is toxic, and the body is able to protect itself by binding the free iron. In the cells, iron is stored in bonded form with ferritin proteins. Ferritin serves to store iron in a dissolved and nontoxic form. The level of ferritin in blood serum is correlated with the total amount of body iron deposits. Ferritin contains about 23% iron; one ferritin complex can store ± 3,000-4,500 Fe3e + ions therein. Ferritin is stored and acquired in the liver, spleen, skeletal muscle and bone marrow (Wallace et al., 2005).
Bioinspired Magnetic Nanoparticles for Biomedical Applications
Published in Nguyễn T. K. Thanh, Clinical Applications of Magnetic Nanoparticles, 2018
Ferritin is an iron storage protein existing in nearly all organisms. Through biomimetic mineralization, a magnetite core can be mineralized into human H-chain ferritin (HFn) cavity to form magnetoferritin (M-HFn) nanoparticles. Recent studies have indicated that M-HFn nanoparticles have potential in early diagnosis of microscopic (<1–2 mm) tumours at the preangiogenic stage due to their intrinsic tumour targeting ability.16 Tumour-targeting peptides can also be fused to HFn-based nanoparticles through genetic engineering, which avoids nonspecific linking by current chemical surface modification.
Sustainable Green Polymeric Nanoconstructs for Active and Passive Cancer Therapeutics
Published in Vladimir Torchilin, Handbook of Materials for Nanomedicine, 2020
Ankit Rochani, Sreejith Raveendran, D. Sakthi Kumar
As mentioned previously, Hft nanocages are transported inside cell via TfR1-mediated endocytosis in human. However, TfR1 is overexpressed in many types of cancer conditions. Further, it is being previously reported that Hft is naturally overexpressed in inflammation and cancer [192]. Perhaps, TfR1 overexpression in cancer is the best way to cope with this excessive demand of Hft. Hence, this makes Hft a naturally occurring targeting material or for cancer therapy [193]. Additionally, a number of conventional nanomedicine-based strategies like developing FA, aptamer, antibody or peptide tagged drug or metal-encapsulated ferritin nanocages were explored improving anticancer potential [193, 194]. For instance, Ft-nanocages were genetically modified to get RGD peptide sequence on the surface. As discussed in the previous section, RGD sequence can selectively bind tumors via RGD-integrin αvβ3 interaction. This modified Hft was used for developing pre-complexed Cu(II) and DOX-loaded Cu-Dox-Ft nanocages. The study showed high cellular uptake by U87MG subcutaneous tumor models, high anticancer efficacy with less cardiotoxicity [195]. Further, a smart strategy was developed to improve efficacy towards melanoma cell lines. Here, α-melanocyte-stimulating hormone peptide (MSH) peptide tagged Peg-coated cobalt doped ferrite nanocages were developed. The concept provided high retention in cancer cells. Moreover, when exposed to the alternate magnetic field, it provided efficient hyperthermia-mediated anticancer effect [186]. In another study, FA tagged-Hft was used for cancer-targeted photodynamic therapy using ZnF16Pc [196]. These examples clearly indicate the importance of Hft with modifiable characteristics for increasing efficacy towards cancer. Ferritin is one of the few examples of smart biomaterials that can be used for the development of cancer-targeted anticancer nanotherapies.
Serum ferritin and vitamin D evaluation in response to high altitude comparing Italians trekkers vs Nepalese porters
Published in European Journal of Sport Science, 2021
Laura Magliulo, Danilo Bondi, Tiziana Pietrangelo, Stefania Fulle, Raffaela Piccinelli, Tereza Jandova, Gaetano Di Blasio, Mattia Taraborrelli, Vittore Verratti
Nevertheless, these parameters are often complex to analyze as they are strongly dependent on factors such as age, gender, health and nutritional status and diseases (Morris et al., 2019). The first erythropoietic response to altitude is dependent on both hypoxic dose and iron stores (Serpell et al., 2020). Broadly speaking, the greatest effects of hypoxia on the haematological parameters occur at 2200–2500 m, with a minimum exposure of 12 h/day for a minimum period of 3 weeks (Millet, Roels, Schmitt, Woorons, & Richalet, 2010). Research studies have specifically highlighted the role of sFER in maintaining blood cell homeostasis and turnover during living or training at altitude (Latunde-Dada, Vulpe, Anderson, Simpson, & McKie, 2004; Mairbäurl, Ruppe, & Bärtsch, 2013; Morris et al., 2019). Ferritin is a globular protein which serves to store iron in a non-toxic form in the cells and to transport it where is required, particularly it can store up to 4500 atoms of iron. Its expression is regulated post-transcriptionally by cellular iron status: a higher intracellular iron concentration result in increased ferritin expression, whereas iron deficiency inhibits its expression. As iron storage reflects changes in iron metabolism, absorption, plasmatic turnover rate and of the RBCs’ iron uptake, sFER represents a valid marker of an iron reservoir into red blood cells (Serpell et al., 2020) and serves as an indicator of metabolic and iron-related disorders (Felipe et al., 2015).
Synthesis, crystal structure, and properties of a tetrairon cluster based on 2-methyl-8-hydroxyquinoline
Published in Journal of Coordination Chemistry, 2018
Ting Meng, Jia-Shun Wang, Hua-Hong Zou, Feng-Hua Liang, Fu-Pei Liang
Iron(III) complexes continue to be studied extensively in the fields of bioinorganic chemistry and molecular magnetism because of the protein ferritin and their interesting magnetic properties [1–4]. Many polynuclear iron complexes can sometimes possess large ground-state spin (S) values due to the relatively large number of unpaired electrons of high-spin FeIII ions, and can even occasionally behave as single-molecule magnets (SMMs) [5–8]. From a structural viewpoint, previous studies have led to successful isolations of various topological iron clusters with help from designed, suitable organic ligands [9]. Another important aspect of iron complexes is the biological importance of the role of the protein ferritin in the storage and recycling of iron [10]. So, the synthesis of iron(III) complexes is not only in academic interest. Self-assembly between organic ligands and metal ions may lead to the formation of functional supramolecular architectures exhibiting unusual properties. More recently, the use of quinoline ligands has enabled the preparation of many different complexes with interesting topologies and functional properties such as bioactivity and magnetic properties [11]. From the structural point of view, we selected the bidentate 2-methyl-8-hydroxyquinoline ligand to construct complexes based on the following considerations: (1) the simple ligand structure; (2) versatile coordination modes (monodentate, chelating, monodentate bridging, and bidentate bridging); (3) it contains a coordination pocket to accommodate metal ions; (4) special biologic activity [12].
Environmental exposure to lead and hematological parameters in Afro-Brazilian children living near artisanal glazed pottery workshops
Published in Journal of Environmental Science and Health, Part A, 2020
Homegnon A. F. Bah, Matheus J. Bandeira, Erival A. Gomes-Junior, Ana Laura S. Anjos, Ynayara J. M. Rodrigues, Nathália R. dos Santos, Victor O. Martinez, Rômula B. M. A. Rocha, Renata G. Costa, Elisângela V. Adorno, José A. Menezes-Filho
Since iron interacts with Pb toxicokinetics, its nutritional deficiency was assessed. Hemoglobin concentration was determined using the portable equipment Hemocue (HemoCue AB, Angelholm, Sweden). Anemia was defined as an Hb concentration lower than 11.5 g/dL.[33] Serum ferritin was evaluated from serum by chemiluminescence method with an Access 2 Immunoassay System (Beckman Coulter, USA). Serum iron (FeS) and TIBC were evaluated by the ferrozine methodology with a Labmax 560 analyzer (LabtestDiagnóstica, MG, Brazil). The transferrin saturation (Tr Sat.) was deduced according to the Eq. (4).[39]