Cloning of a pig homologue of the human lactoferrin receptor: Expression and localization during intestinal maturation in piglets

Liao, Yin; López, Verónica; Shafizadeh, Tracy B.; Halsted, Charles H.; Lönnerdal, Bo

doi:10.1016/j.cbpa.2007.08.001

Cited by 38 publications

(30 citation statements)

References 30 publications

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“…This protein also represents a promising candidate for an alternative iron source in the absence of a functional DMT1 pathway. The identification of a specific receptor for lactoferrin (LfR) in the small intestine of newborn infants [115] and suckling piglets [116] is evidence that the Lf-LfR pathway plays a role in iron absorption during early life. However, a comparison of the iron status of suckling progeny from mothers with a disrupted Lf gene and those from wild-type mothers showed that lactoferrin is not essential for iron absorption during the early postnatal period and does not play a major role in the regulation of this process [117].…”

Section: Iron Metabolism In Early Postnatal Lifementioning

confidence: 99%

Molecular insights into the regulation of iron metabolism during the prenatal and early postnatal periods

Lipiński

Styś

Starzyński

2012

Cell. Mol. Life Sci.

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Molecular iron metabolism and its regulation are least well understood in the fetal and early postnatal periods of mammalian ontogenic development. The scope of this review is to summarize recent progress in uncovering the molecular mechanisms of fetal iron homeostasis, introduce the molecules involved in iron transfer across the placenta, and briefly explain the role of iron transporters in the absorption of this microelement during early postnatal life. These issues are discussed and parallels are drawn with the relatively well-established system for elemental and heme iron regulation in adult mammals. We conclude that detailed investigations into the regulatory mechanisms of iron metabolism at early stages of development are required in order to optimize strategies to prevent neonatal iron deficiency. We propose that newborn piglets represent a suitable animal model for studies on iron deficiency anemia in neonates.

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Section: Iron Metabolism In Early Postnatal Lifementioning

confidence: 99%

Molecular insights into the regulation of iron metabolism during the prenatal and early postnatal periods

Lipiński

Styś

Starzyński

2012

Cell. Mol. Life Sci.

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“…During the first hours of life the gut is permeable to many immunologically relevant proteins such as IgA and growth factors necessary for gut development (Commare and Tappenden 2007). After the first few days of life the gut becomes impermeable to most proteins, however there is a 105 kDa lactoferrin receptor (also known as intelectin) that specializes in mediating uptake of lactoferrin into enterocytes and crypt cells (Kawakami and Lönnerdal 1991;Liao et al 2007Liao et al , 2012, so infants can transport lactoferrin past gut closure. Once lactoferrin is taken up by enterocytes at the brush border, is internalized into compartments in the apical cytoplasm, where it can have effects on cellular proliferation and directing immune responses (Nielsen et al 2010).…”

Section: Lactoferrinmentioning

confidence: 97%

Production of human lactoferrin and lysozyme in the milk of transgenic dairy animals: past, present, and future

2015

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Genetic engineering, which was first developed in the 1980s, allows for specific additions to animals' genomes that are not possible through conventional breeding. Using genetic engineering to improve agricultural animals was first suggested when the technology was in the early stages of development by Palmiter et al. (Nature 300:611-615, 1982). One of the first agricultural applications identified was generating transgenic dairy animals that could produce altered or novel proteins in their milk. Human milk contains high levels of antimicrobial proteins that are found in low concentrations in the milk of ruminants, including the antimicrobial proteins lactoferrin and lysozyme. Lactoferrin and lysozyme are both part of the innate immune system and are secreted in tears, mucus, and throughout the gastrointestinal (GI) tract. Due to their antimicrobial properties and abundance in human milk, multiple lines of transgenic dairy animals that produce either human lactoferrin or human lysozyme have been developed. The focus of this review is to catalogue the different lines of genetically engineered dairy animals that produce either recombinant lactoferrin or lysozyme that have been generated over the years as well as compare the wealth of research that has been done on the in vitro and in vivo effects of the milk they produce. While recent advances including the development of CRISPRs and TALENs have removed many of the technical barriers to predictable and efficient genetic engineering in agricultural species, there are still many political and regulatory hurdles before genetic engineering can be used in agriculture. It is important to consider the substantial amount of work that has been done thus far on well established lines of genetically engineered animals evaluating both the animals themselves and the products they yield to identify the most effective path forward for future research and acceptance of this technology.

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“…Recombinant human lactoferrin was also shown to resist digestion in vitro [35]. A receptor for lactoferrin was iso-lated and characterized [36], and it was subsequently cloned in the human [37], mouse [38], and pig [39], all species with milk having high concentrations of lactoferrin. The LfR is a homo-trimer of about 110 kDa in molecular weight, and it is glycosylated [37].…”

Section: Absorption Of Iron From Lactoferrinmentioning

confidence: 99%

“…Interestingly, the expression is similarly high in duodenum, jejunum, and ileum [39], possibly allowing lactoferrin-iron uptake throughout the small intestine, whereas the uptake of ferrous iron (mediated by DMT-1) only occurs in the duodenum. This may be one reason why iron absorption is lower from infant formula (where iron is added as ferrous sulfate) than from breast milk [44].…”

Section: Absorption Of Iron From Lactoferrinmentioning

confidence: 99%

Alternative pathways for absorption of iron from foods

Lönnerdal

2010

Pure and Applied Chemistry

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Iron is known to be absorbed from foods in two major forms, heme iron and nonheme iron. Iron status as well as dietary factors known to affect iron absorption has limited effect on heme iron absorption, whereas inhibitors and enhancers of iron absorption have pronounced effects on non-heme iron absorption. The enterocyte transporter for non-heme iron, DMT1, is strongly up-regulated during iron deficiency and down-regulated during iron overload. A transporter for heme iron, HCP1, was recently characterized and is present on the apical membrane of enterocytes. Two other pathways for iron absorption have been discovered and may serve to facilitate uptake of iron from two unique iron-binding proteins, lactoferrin and ferritin. Lactoferrin is an iron-binding protein in human milk and known to survive proteo lytic digestion. It mediates iron uptake in breast-fed infants through endocytosis via a specific lactoferrin receptor (LfR). Recently, lactoferrin has become popular as a food additive and may enhance iron status in several age groups. Ferritin is present in meat, but also in plants. The ferritin content of plants can be enhanced by conventional breeding or genetic engineering, and thereby increase iron intake of populations consuming plant-based diets. Ferritin is a bioavailable source of iron, as shown in recent human studies. Ferritin can be taken up by intestinal cells via endocytosis, suggesting a receptor-mediated mechanism.

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Cloning of a pig homologue of the human lactoferrin receptor: Expression and localization during intestinal maturation in piglets

Cited by 38 publications

References 30 publications

Molecular insights into the regulation of iron metabolism during the prenatal and early postnatal periods

Molecular insights into the regulation of iron metabolism during the prenatal and early postnatal periods

Production of human lactoferrin and lysozyme in the milk of transgenic dairy animals: past, present, and future

Alternative pathways for absorption of iron from foods

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