China 
Africa 
Explore chapters and articles related to this topic
Nutritional and Medicinal Properties of Camel Milk
Published in Mehwish Iqbal, Complementary and Alternative Medicinal Approaches for Enhancing Immunity, 2023
One of the studies explored the capability of lactoferrin from camel milk to impede the growth of cancer cells. This research has documented that 3–5 mg/ml (high concentrations) of lactoferrin from camel milk diminish the multiplication of HCT-116 cancer cells in the colon by approximately 56%. On the other hand, no considerable reduction of cell multiplication was observed at minimum concentrations, i.e. less than 1 mg. Lactoferrin (Figure 15.2) has also been demonstrated to have a range of biological properties, including antimicrobial activity (Tsuda & Sekine, 2000). Gader and Al-Haider (2016) reported that camel milk could eliminate lung, liver, leukaemia, glioma and colon cancer cells (Abdel Gader & Alhaider, 2016). The dynamic immunoglobulins of camel milk have the capacity to damage tumour cells (Levy et al., 2013). Furthermore, camel milk has blood-clot-dissolving (thrombolytic) activity, which decreases the synthesis of fibrin, thus decreasing the growth of tumour cells (Mohammadabadi, 2020).
Pathogenicity and Virulence
Published in Julius P. Kreier, Infection, Resistance, and Immunity, 2022
Free ionic iron is present in the body fluids of animals, but only in very low concentrations. Most of the iron is either sequestered inside host cells, in association with functional molecules such as hemoglobin or myoglobin, or captured extracellularly by the glycoproteins lactoferrin and transferrin, which have a high iron-binding affinity. Lactoferrin is found primarily in mucosal secretions and milk, while transferrin is found mainly in blood and lymph. In response to a microbial infection, the host reduces the amount of iron bound to transferrin by transferring it to iron stores. Bacteria and fungi, however, require iron for their metabolism; the survival of the invading microorganism therefore depends upon its ability to scavenge iron from its environment.
Iron in Formulas and Baby Foods
Published in Bo Lönnerdal, Iron Metabolism in Infants, 2020
Sean R. Lynch, Richard F. Hurrell
The role of lactoferrin which is present in high concentrations in human milk but not in cow’s milk is uncertain. McMillan et al.26 reported that the addition of a human lactoferrin to cow’s milk depressed absorption. However, recent studies in infant Rhesus monkeys by Davidson and Lönnerdal demonstrate that lactoferrin is resistant to proteolysis in the infant gastrointestinal tract and shows specific binding to the brush border of the small intestine, suggesting that it may play an important role in facilitating iron absorption from primate milk.12
Targeting stearoyl-coa desaturase enhances radiation induced ferroptosis and immunogenic cell death in esophageal squamous cell carcinoma
Published in OncoImmunology, 2022
Hui Luo, Xiaohui Wang, Shuai Song, Yunhan Wang, Qinfu Dan, Hong Ge
Since difficulty swallowing and unintended weight loss were the most common symptoms of esophageal cancer, iron deficiency anemia may exist in the affected individuals.40 Besides, tumor cells themselves exhibit an increased iron uptake to support survival .41 Anemia was an unfavorable factor with regards to treatment response and survival in cancer patients.6 In a mouse glioma model, administration of iron-containing water prior to RT stimulated ferroptotic cell death and decreased tumor size. Moreover, there was significant difference in tumor volume between mice treated with RT alone and mice treated with RT followed by the iron-containing water.42,43 Tumor cells containing high iron levels caused increased hydrogen peroxide generation, an early and crucial step for ferroptosis.44 In addition, lactoferrin was an iron-binding multifunctional cationic glycoprotein that capable of treating iron deficiency anemia.45 Holo-lactoferricin – a protein incorporated in food supplements to increase iron levels – exhibited anticancer properties via reactive oxygen species generation and GPX4 downregulation, resulting in tumor cell ferroptosis and enhanced radiation response in triple-negative breast cancer.46 Consequently, the efficacy of RT combined with MF-438 may be improved with an increased cellular iron, especially in gastrointestinal tract tumors, and further study is warranted.
Development of an enzymatic method for the evaluation of protein deposition on contact lenses
Published in Biofouling, 2022
The amount of lactoferrin on the surface of all lenses was similar to the total amount extracted, indicating the majority would have been surface-bound. The concentration of extracted lactoferrin as measured in the current study is similar to a previous report (Chow et al. 2009). No difference was found between the concentration of surface lactoferrin across the lens types. The concentration of total lactoferrin between the lens types was also the same except for Balafilcon A and Senofilcon A or Comfilcon A, with more being in the bulk of Balafilcon A. Even though, Balafilcon A has smaller average pore size than Senofilcon A, the number of pores on Balafilcon A is more than Senofilcon A (504 vs. 32) (Green et al. 2012; Lewandowska et al. 2015). The number, size and distribution of pores on each lens might play a role in the penetration of lactoferrin into the bulk of contact lenses (Garrett et al. 1998).
Estimation of numbers of mature and immature neutrophils in blood by a novel, rapid and simple technology
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2021
Per Venge, Ann-Katrin Eriksson, Lena Moberg, Christer Peterson, Shengyuan Xu, Kerstin Hamberg, Martin Höglund
Myeloperoxidase is primarily contained in the primary, azurophil granules of neutrophils but also in monocytes [2,3]. The content in monocytes has been estimated to be about 50% of what is found in neutrophils. Thus, in rare cases with monocythemia the numbers of neutrophils may be overestimated by our novel technology. MPO deficiency is a rare genetic abnormality in which neutrophil counts may be underestimated [4]. Lactoferrin is not present in any other blood cell but neutrophils. However, as the name implies lactoferrin is found abundantly in breast milk and serves as an anti-bacterial principle in the milk [5]. Lactoferrin is present in the secondary, specific granules of neutrophils. The differences in the degree of correlations to neutrophil numbers with a much closer correlation for MPO than for Lactoferrin is probably a sign of two conditions. One is the fact that Lactoferrin is produced late in the myeloid cell development and subject to variable marrow transit times depending on the demand from the body [6]. Thus, in diseases such as bacterial infections, the transit time is shortened and the time to produce Lactoferrin goes down [7]. Myeloperoxidase on the other hand is produced already early during the myeloid development and much less affected by changes in marrow transit time. The second condition is the fact that secondary granules are secretory granules, meaning that mobilization of proteins from this class of granules is more responsive to external stimuli than from Myeloperoxidase containing primary granules [3].