Identification and functional analysis of an iron‐binding protein, ferritin heavy chain subunit, from the swallowtail butterfly, Papilio xuthus

2019 ◽  
Vol 102 (1) ◽  
Author(s):  
Zhan‐Jun Lu ◽  
Yan‐Xin Xie ◽  
Hai‐Zhong Yu ◽  
Shahzad Toufeeq ◽  
Jie Wang ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Heavy Chain ◽  
Binding Protein ◽  
Iron Binding ◽  
Swallowtail Butterfly ◽  
Ferritin Heavy Chain ◽  
Papilio Xuthus ◽  
Iron Binding Protein

scholarly journals Lactoferrin-an iron binding protein in synovial fluid

1973 ◽  
Vol 16 (2) ◽  
pp. 186-190 ◽  
Author(s):  
Robert M Bennett ◽  
A C Eddie-Quartey ◽  
P J L Holt
Keyword(s):  
Synovial Fluid ◽  
Binding Protein ◽  
Iron Binding ◽  
Iron Binding Protein

scholarly journals Iron-Binding Protein of Swine Serum.

1947 ◽  
Vol 1 ◽  
pp. 770-776 ◽  
Author(s):  
C.-B Laurell ◽  
B. Ingelman
Keyword(s):  
Binding Protein ◽  
Iron Binding ◽  
Iron Binding Protein ◽  
Swine Serum

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.

scholarly journals The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin

1988 ◽  
Vol 256 (3) ◽  
pp. 923-928 ◽  
Author(s):  
H P Monteiro ◽  
C C Winterbourn
Keyword(s):  
Lipid Peroxidation ◽  
Free Radicals ◽  
Xanthine Oxidase ◽  
Binding Protein ◽  
Gel Filtration ◽  
Iron Binding ◽  
Oxidase System ◽  
Oxidative Reactions ◽  
Phospholipid Liposomes ◽  
Iron Binding Protein

By the use of gel filtration and [59Fe]ferritin, apotransferrin and apolactoferrin were shown to take up iron released from ferritin by superoxide generated by hypoxanthine and xanthine oxidase. Apotransferrin also inhibited uptake of released iron by ferrozine. Ferritin and the xanthine oxidase system induced lipid peroxidation in phospholipid liposomes. This peroxidation was inhibited by apotransferrin or apolactoferrin. Thus, although superoxide and other free radicals can release iron from ferritin, either iron-binding protein, if present, should take up this iron and prevent its catalysing subsequent oxidative reactions.

The World Distribution of Transferrin Variants and some Unsolved Problems

1968 ◽  
Vol 17 (4) ◽  
pp. 613-640 ◽  
Author(s):  
R. L. Kirk
Keyword(s):  
Human Serum ◽  
World Literature ◽  
Binding Protein ◽  
Present Knowledge ◽  
Human Populations ◽  
Iron Binding ◽  
The World ◽  
Iron Binding Protein ◽  
World Distribution

SummaryNineteen variants of the iron-binding protein, transferrin, have been described in human serum. The world literature on the distribution of these variants in human populations is surveyed in comprehensive tables and attention is drawn to some of the outstanding deficiencies in our present knowledge of this distribution. It is pointed out that transferrin variants are important markers in anthropological studies.

scholarly journals Function of integrin in duodenal mucosal uptake of iron

Blood ◽  
1993 ◽  
Vol 81 (2) ◽  
pp. 517-521 ◽  
Author(s):  
ME Conrad ◽  
JN Umbreit ◽  
RD Peterson ◽  
EG Moore ◽  
KP Harper
Keyword(s):  
Monoclonal Antibodies ◽  
Small Intestine ◽  
Binding Protein ◽  
Iron Binding ◽  
Immunofluorescent Microscopy ◽  
Mucosal Surfaces ◽  
Iron Binding Protein ◽  
Mucosal Uptake

Abstract A mechanism for the absorption of inorganic iron in the small intestine is described in which integrins appear to play an important role in the passage of iron across microvillous membranes. Biochemical isolates from microvillous preparations of duodenum from rats dosed with radioiron showed radioactivity concentrated in integrins. The presence of integrins on mucosal surfaces of duodenal cells was confirmed by immunofluorescent microscopy using anti-integrin monoclonal antibodies. Immunoprecipitation methods were used to show that microvillous radioiron was precipitated with anti-integrin antibodies and that mobilferrin, a 56-Kd cytosol iron-binding protein, coprecipitated with integrins. We postulate from these data that the mucosal uptake of iron from the gut lumen is mediated via an integrin-mobilferrin pathway.

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