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Diabetes Mellitus, Obesity, Lipoprotein Disorders and other Metabolic Diseases
Published in John S. Axford, Chris A. O'Callaghan, Medicine for Finals and Beyond, 2023
This is an acquired or inherited deficiency of hepatic uroporphyrinogen decarboxylase. Iron and transferrin levels can be raised, and mild hepatic iron overload can occur.
Iron, Oxygen Stress, and The Preterm Infant
Published in Bo Lönnerdal, Iron Metabolism in Infants, 2020
Human plasma is a powerful antioxidant.22 The major responsible factors are transferrin and ceruloplasmin. Both of these plasma products act by minimizing the availability of iron for participation in free-radical reactions. Ceruloplasmin is a ferroxidase23 promoting the oxidation of ferrous iron (Fe2+) to the ferric form (Fe3+), thereby preventing iron from donating electrons to oxygen. In addition, ceruloplasmin may even directly scavenge the inline 13 radical.24 Transferrin is the iron transport protein in plasma. In healthy individuals, transferrin is not fully saturated with iron. This leaves a capacity to bind ionic iron in plasma. In patients with iron overload, transferrin may be fully saturated with iron, and there is evidence that some toxic effects of iron overload are caused by free-radical reactions.25
PlasmaThe Non-cellular Components of Blood
Published in Peter Kam, Ian Power, Michael J. Cousins, Philip J. Siddal, Principles of Physiology for the Anaesthetist, 2020
Peter Kam, Ian Power, Michael J. Cousins, Philip J. Siddal
Transferrin is the plasma protein that transports iron. Apotransferrin, its precursor, is produced in the liver. One molecule of transferrin will bind two ferric ions and is normally approximately one-third saturated with iron. Haemopexin is a β-globulin that binds to haem and releases it to the reticuloendothelial system.
A deep dive into future therapies for microcytic anemias and clinical considerations
Published in Expert Review of Hematology, 2023
François Rodrigues, Tereza Coman, Guillemette Fouquet, Francine Côté, Geneviève Courtois, Thiago Trovati Maciel, Olivier Hermine
Approximately 70% of the total body iron (3–5 g in adult humans) is bound to heme in red blood cells [2]. Significant fractions are distributed within the liver hepatocytes (20%) and macrophages (5%). On a daily basis, erythropoiesis requires up to 30 mg of iron, while non-erythroid cell requirements are about 5 mg. The plasma iron pool is only 3–4 mg and thus turns over more than ten times per day to satisfy the daily iron requirements. The iron carrier transferrin is central to iron trafficking. Transferrin not only serves as an iron carrier but also keeps circulating iron in a redox-inactive state. Under physiological conditions, only 30% of transferrin molecules are saturated with Fe3+. A rare genetic cause of microcytic anemia, congenital atransferrinemia, highlights the central role of transferrin as a regulated distributor of iron to erythroid and non-erythroid tissues [3]. Children affected by this condition present microcytic anemia due to inefficient iron delivery to erythroblasts, associated with iron overload in non-erythroid tissues, such as the myocardium, liver, or central nervous system because of free iron toxicity.
Advances in tests for colorectal cancer screening and diagnosis
Published in Expert Review of Molecular Diagnostics, 2022
Sarah Cheuk Hei Chan, Jessie Qiaoyi Liang
Aside from hemoglobin, other fecal proteins can also be detected for CRC screening. However, the number of studies on this topic is limited. Transferrin is the main protein in the blood that binds to and transports iron throughout the body. Normally absent in the gastrointestinal tract, the presence of transferrin in feces indicates gastrointestinal bleeding [46]. Most studies indicate the detection of transferrin and hemoglobin improves the diagnostic accuracy for CRC [46–50]. Calprotectin is released by a type of white blood cell, neutrophil, and acts as a biomarker for gastrointestinal inflammation [51]. Although inflammation is involved in tumor progression [52], the effectiveness of calprotectin for CRC diagnosis is inconclusive, regardless of being measured alone or in combination with other markers [51,53–56]. The same situation applies to lactoferrin, another inflammatory marker. Lactoferrin is a non-heme iron-binding glycoprotein and is a prominent component of the first line of mammalian host defense. While some studies find fecal lactoferrin useful in detecting CRC [57–59], others have opposite findings [60].
Modulations of ferroptosis in lung cancer therapy
Published in Expert Opinion on Therapeutic Targets, 2022
Robert Walters, Shaker A. Mousa
Lastly, lactoferrin is a naturally occurring non-heme iron-binding protein and member of the transferrin family commonly found in mammalian secretions, such as milk, seminal fluid, intestinal secretions, tears, sweat, saliva, nasal secretions, as well as secretory granules of neutrophils [79,80]. As a transferrin, its role is to transport iron in the blood serum. The use of iron-saturated lactoferrin (Holo-Lactoferrin) has been shown to significantly increase total iron content, initiate ROS generation, increase lipid peroxidation, leading to enhancement of ferroptosis [81]. Lactoferrin has also shown anticancer effects in NSCLC. In a randomized control trial, talactoferrin, an oral recombinant lactoferrin produced by fungus Aspergillus Niger var. awamori, significantly increased overall survival by 65% compared to placebo in advanced NSCLC patients [82]. Thus, lactoferrin has effects on both ferroptosis induction and anticancer effects, allowing for potential synergistic manipulation to enhance its utility in lung cancer patients.