Purification of an iron‐binding peptide from scad ( Decapterus maruadsi ) processing by‐products and its effects on iron absorption by Caco‐2 cells

2019 ◽  
Vol 43 (7) ◽  
Author(s):  
Han Jiang ◽  
Wenting Zhang ◽  
Fangyuan Chen ◽  
Jiong Zou ◽  
Wenwei Chen ◽  
...  
Keyword(s):  
Iron Absorption ◽  
Iron Binding ◽  
Binding Peptide ◽  
By Products ◽  
Decapterus Maruadsi

Manufacturing of Iron Binding Peptide Using Sericin Hydrolysate and Its Bioavailability in Iron Deficient Rat

2010 ◽  
Vol 39 (10) ◽  
pp. 1446-1451 ◽  
Author(s):  
Hye-Jin Cho ◽  
Hyun-Sun Lee ◽  
Eun-Young Jung ◽  
So-Yeon Park ◽  
Woo-Taek Lim ◽  
...  
Keyword(s):  
Iron Binding ◽  
Binding Peptide ◽  
Iron Deficient

scholarly journals IRON METABOLISM

Blood ◽  
1950 ◽  
Vol 5 (11) ◽  
pp. 983-1008 ◽  
Author(s):  
CLEMENT A. FINCH ◽  
MARK HEGSTED ◽  
THOMAS D. KINNEY ◽  
E. D. THOMAS ◽  
CHARLES E. RATH ◽  
...  
Keyword(s):  
Iron Metabolism ◽  
Serum Iron ◽  
Iron Absorption ◽  
Binding Protein ◽  
The Body ◽  
Iron Binding ◽  
Body Iron ◽  
Iron Administration ◽  
Parenteral Iron ◽  
Iron Binding Protein

Abstract On the basis of experimental and clinical observations and a review of the literature, a concept of the behavior of storage iron in relation to body iron metabolism has been formulated. Storage iron is defined as tissue iron which is available for hemoglobin synthesis when the need arises. This iron is stored intracellularly in protein complex as ferritin and hemosiderin. It would appear that wherever the cell is functionally intact, such iron is available for general body needs. Iron is transported by a globulin of the serum to and from the various tissues of the body to satisfy their metabolism. Surplus iron carried by this iron-binding protein is deposited chiefly in the liver. Storage iron may be increased in two ways. The first mechanism results from the inability of the body to excrete significant amounts of iron. Because of this, any decrease in circulating red cell iron (any anemia other than blood loss or iron deficiency anemia) is accompanied by a shift of iron to the tissue compartment. The total amount of body iron remains constant and is merely redistributed. This is to be contrasted with the absolute increase in body iron and enlarged iron stores which follow excessive iron absorption or parenteral iron administration. Enlarged iron stores in either instance may be evaluated by examination of sternal marrow or determination of the serum iron and saturation of the iron binding protein In states of iron excess, differences in initial distribution are observed, depending on the route of administration and type of iron compound employed. Iron absorbed from the gastro-intestinal tract and soluble iron salts injected in small amounts are transported by the iron-binding protein of the serum and stored predominantly in the liver. Colloidal iron given intravenously is taken up by the reticulo-endothelial tissue. Erythrocytes appear to localize in greatest concentration in the spleen, while greater amounts of hemoglobin iron are found in the renal parenchyma. These latter differences in distribution reflect the capacity of various body tissues to assimilate different iron compounds, which while present in the plasma are not carried by the iron-binding protein. Over a period of time an internal redistribution of iron from these various sites occurs through the serum iron compartment. The liver becomes progressively loaded with iron. When the capacity of the liver to store iron is exceeded, the serum iron increases and secondary tissue receptors begin to fill with iron. That iron in large amounts is toxic to tissues is suggested by the occurrence of fibrosis in the organs most heavily laden with iron. This sequence of events, whether following excessive iron absorption or parenteral iron administration is believed to be responsible for the clinical and pathologic picture of hemochromatosis.

Alternative pathways for absorption of iron from foods

2010 ◽  
Vol 82 (2) ◽  
pp. 429-436 ◽  
Author(s):  
Bo Lönnerdal
Keyword(s):  
Iron Absorption ◽  
Iron Status ◽  
Age Groups ◽  
Heme Iron ◽  
Dietary Factors ◽  
Iron Binding ◽  
Alternative Pathways ◽  
Non Heme Iron ◽  
Lactoferrin Receptor ◽  
Iron Binding Proteins

Iron is known to be absorbed from foods in two major forms, heme iron and non-heme 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 proteolytic 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.

Lactoferrin – 50 years on

2012 ◽  
Vol 90 (3) ◽  
pp. 245-251 ◽  
Author(s):  
Jeremy H. Brock
Keyword(s):  
Gastrointestinal Tract ◽  
Antimicrobial Agent ◽  
Iron Transport ◽  
Iron Absorption ◽  
Structure And Function ◽  
Transport Protein ◽  
Future Research ◽  
Iron Binding ◽  
Plasma Iron ◽  
And Function

It is now some 50 years since iron-binding lactoferrin was first isolated and purified, an event that opened the way to subsequent extensive research on lactoferrin structure and function. The initial recognition that lactoferrin closely resembled the plasma iron-transport protein transferrin meant that lactoferrin was first thought to mediate intestinal iron absorption or to act as an antimicrobial agent. It was also suggested that it could mediate the hyposideraemia of inflammation. This paper will assess to what extent early proposals have stood the test of time and also suggest possible mechanisms by which lactoferrin can mediate the large number of potential functions that have subsequently been proposed. It will also review the ability of lactoferrin to resist digestion in the gastrointestinal tract and identify areas for future research.

scholarly journals Transferrin and the Absorption of Iron

Blood ◽  
1963 ◽  
Vol 21 (1) ◽  
pp. 33-38 ◽  
Author(s):  
SIMEON POLLACK ◽  
STANLEY P. BALCERZAK ◽  
WILLIAM H. CROSBY
Keyword(s):  
Iron Absorption ◽  
Binding Protein ◽  
Iron Binding ◽  
Iron Salt ◽  
Iron Binding Protein

Abstract A loop isolated in situ has been used to study iron absorption in the dog. An infusion of iron salt into the artery supplying the isolated loop fails to stop the absorption of iron from the lumen of the gut. Iron absorption appears to be independent of the relative saturation of iron-binding protein.

Kinetic analysis of the intestinal iron absorption process in situ. The potential of vascularly autoperfused intestinal loops

1997 ◽  
Vol 16 (8) ◽  
pp. 425-428 ◽  
Author(s):  
G. Hunder ◽  
K. Osterloh ◽  
K. Schümann
Keyword(s):  
Blood Flow ◽  
Small Intestine ◽  
Iron Absorption ◽  
Binding Capacity ◽  
Iron Binding ◽  
Absorption Kinetics ◽  
Flow Rates ◽  
Intestinal Iron Absorption ◽  
Iron Binding Capacity

1 Blood sampling from mesenteric venules during absorption in situ is a useful tool to analyse intestinal absorption kinetics and prehepatic metabolism in different sections of the rat small intestine. By use of a micromanipulator, the method can be applied to the duodenum. This part of the small intestine shows the strongest adaptation of non-haem iron absorption to the demand for iron. 2 Iron absorption kinetics was linear in duodenal and jejunal segments. In iron-deficient animals, intestinal iron absorption capacity was increased in the duode num, while simultaneously determined galactose absorption showed no change. 3 In situ perfusion and cannulation of mesenteric venules in duodenal segments are described. The use of a micromanipulator permits varying the blood volume collected by changing the vertical angle between the cannula and the mesenteric vessel. 4 Intestinal iron absorption rates remained close to constant when blood flow rates were varied by a factor of about ten. Plasma concentrations of absorbed iron vs mesenteric blood flow rates followed a hyperbolic function, as the plasma concentration of absorbed iron in mesenteric venules increased to the same extent as the blood flow decreased. 5 As the plasma transferrin concentration did not change over the experimental period, the concentra tion of absorbed iron in the mesenteric plasma exceeded the iron-binding capacity of plasma trans ferrin at low blood flow rates. This observation shows that enhancement of intestinal iron absorption does not require a corresponding increase in plasma iron- binding capacity in the intestinal tissue. 6 Vascularly perfused gut loops were also used to measure prehepatic metabolism, which may influence organotropism of carcinogenic metabolites. Therefore, this type of preparation is likely to find a variety of toxicological applications.

scholarly journals Isolated rat hepatocytes acquire iron from lactoferrin by endocytosis

1995 ◽  
Vol 311 (2) ◽  
pp. 603-609 ◽  
Author(s):  
D D McAbee
Keyword(s):  
Binding Sites ◽  
Rat Hepatocytes ◽  
Iron Binding ◽  
C Cells ◽  
Dextran Sulphate ◽  
Isolated Rat Hepatocytes ◽  
Iron Binding Protein ◽  
Diferric Transferrin ◽  
By Products ◽  
Isolated Rat

The iron-binding protein lactoferrin (Lf) present in blood is metabolized by the liver. Isolated rat hepatocytes vigorously endocytose bovine Lf via recycling Ca2(+)-dependent binding sites, but the uptake of iron from Lf by hepatocytes has not been examined. In this study, isolated rat hepatocytes were incubated with radiolabelled bovine Lf (125I-Lf, 59Fe-Lf or 125I-59Fe-Lf) at 37 degrees C, then washed at 4 degrees C in the presence of dextran sulphate with either Ca2+ or EGTA to distinguish between total bound and internal radioactivity respectively. Cells internalized 125I-Lf protein and Lf-bound 59Fe at maximal endocytic rates of 1700 and 480 mol.cell-1.s-1 respectively. When Lf was normalized for 59Fe content, these endocytic rates were equivalent and reflected an uptake potential of at least 3400 mol of iron.cell-1.s-1. Cells prebound with 125I-59Fe-Lf to Ca2+(-)dependent sites at 4 degrees C internalized more than 80% of both 125I-Lf protein and Lf-bound 59Fe approx. 6 min after warming to 37 degrees C at similar rates (125I-Lf: k(in) = 0.276 min-1, 59Fe: k(in) = 0.303 min-1). Within 4 h at 37 degrees C, cells had released 25% or less internalized Lf protein in the form of acid-soluble 125I-by-products but retained all the Lf-delivered 59Fe. Hyperosmotic disruption of clathrin-dependent endocytosis blocked the uptake of 125I-Lf and Lf-bound 59Fe. Incubation of cells with 125I-59Fe-Lf and a 100 molar excess of diferric transferrin reduced slightly the endocytosis of 125I-Lf protein and 59Fe accumulation. Treatment of cells with the ferric chelator desferrioxamine did not alter uptake of 125I-Lf protein or Lf-bound 59Fe, but the ferrous chelator bathophenanthroline disulphonate slightly elevated endocytosis of 125I-Lf protein and Lf-bound 59Fe. These findings indicate that Lf does not release its bound iron before endocytosis. It was concluded from this study that hepatocytes take up iron from Lf at high rates by a process that requires endocytosis of Lf-iron complexes.

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