scholarly journals A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is required for binding to transferrin

1999 ◽  
Vol 341 (1) ◽  
pp. 11-14 ◽  
Author(s):  
Valentina DUBLJEVIC ◽  
Adnan SALI ◽  
James W. GODING
Keyword(s):  
Cell Adhesion ◽  
Transferrin Receptor ◽  
Iron Uptake ◽  
Terminal Region ◽  
Rgd Sequence

The transferrin receptor contains a highly conserved Arg-Gly-Asp (RGD) sequence in the C-terminal region where transferrin is thought to bind. RGD sequences are commonly involved in cell adhesion. This sequence is crucial for transferrin binding, suggesting possible evolutionary links between molecules mediating iron uptake and cell adhesion.

scholarly journals Transferrin receptor 1-mediated iron uptake plays an essential role in hematopoiesis

Haematologica ◽  
2019 ◽  
Vol 105 (8) ◽  
pp. 2071-2082 ◽  
Author(s):  
Shufen Wang ◽  
Xuyan He ◽  
Qian Wu ◽  
Li Jiang ◽  
Liyun Chen ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Iron Uptake ◽  
Essential Role ◽  
Transferrin Receptor 1

Role of vasostatin-1 C-terminal region in fibroblast cell adhesion

2010 ◽  
Vol 67 (12) ◽  
pp. 2107-2118 ◽  
Author(s):  
Eleonora Dondossola ◽  
Anna Gasparri ◽  
Angela Bachi ◽  
Renato Longhi ◽  
Marie-Hélène Metz-Boutigue ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Fibroblast Cell ◽  
Terminal Region

scholarly journals Understanding the Transferrin Receptor and Cellular Iron Deficiency Outside the Erythron

Blood ◽  
2017 ◽  
Vol 130 (Suppl_1) ◽  
pp. SCI-42-SCI-42
Author(s):  
Nancy C. Andrews
Keyword(s):  
Iron Deficiency ◽  
Missense Mutation ◽  
Transferrin Receptor ◽  
Iron Uptake ◽  
Clinical Manifestations ◽  
Cell Types ◽  
Conditional Knockout ◽  
Deficiency Anemia ◽  
Transferrin Receptor 1

Our laboratory showed that mouse embryos lacking the classical transferrin receptor, Tfrc, experienced anemia, pericardial effusion and a kinking of the neural tube, but otherwise appeared to be developing normally, suggesting that Tfrc was not needed by most tissues (Levy et al. 1999). Subsequently, we reported that Tfrc was essential for hematopoiesis but seemed to be dispensable in other tissues (Ned et al., 2003). A recent paper showing that a missense mutation in the TFRC internalization motif resulted in immunodeficiency without other clinical manifestations was consistent with this idea (Jabara et al., 2016). Nonetheless, we were not entirely convinced. More than thirty years ago, Larrick and Hyman described a patient with an anti-TFRC autoantibody who suffered from a broader range of clinical problems, suggesting that TFRC might have other roles (Larrick and Hyman, 1984). To help resolve the issue, we developed mice carrying an allele of Tfrc that can be conditionally inactivated, and used Cre/lox-mediated recombination to disrupt that allele in vivo, in several key cell types. We asked two questions: (1) is Tfrc important in those cell types and, if so, (2) what are the cellular consequences of Tfrc loss? We found that some cell types do not need Tfrc but others are highly dependent upon it. Those cell types that depend upon Tfrc generally need it for iron uptake, as expected, with one exception. Tfrc is critically important for normal development of the intestinal epithelium, but our data indicate that its essential role does not involve iron uptake. While surprising in view of our earlier results, the roles of Tfrc that we have unmasked through conditional knockout experiments would not have been apparent prior to the death of global Tfrc knockout embryos in mid-gestation. Nonetheless those roles are important, and our results give insight into why iron deficiency exacerbates heart failure, how muscle iron deficiency leads to disruption of systemic carbon metabolism, and how iron deficiency, rather than iron excess, may play a role in the pathogenesis of neurodegenerative disorders. Levy JE, Jin O, Fujiwara Y, Kuo F, Andrews NC. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat Genet. 1999;21:396-9. Ned RM, Swat W, Andrews NC. Transferrin receptor 1 is differentially required in lymphocyte development. Blood. 2003;102:3711-8. Jabara HH, Boyden SE, Chou J et al. A missense mutation in TFRC, encoding transferrin receptor 1, causes combined immunodeficiency. Nat Genet. 2016;48:74-8. Larrick JW, Hyman ES. Acquired iron-deficiency anemia caused by an antibody against the transferrin receptor. N Engl J Med. 1984;311:214-8. Disclosures Andrews: Novartis: Membership on an entity's Board of Directors or advisory committees.

scholarly journals Temporal manipulation of transferrin-receptor-1-dependent iron uptake identifies a sensitive period in mouse hippocampal neurodevelopment

Hippocampus ◽  
2012 ◽  
Vol 22 (8) ◽  
pp. 1691-1702 ◽  
Author(s):  
S.J.B. Fretham ◽  
E.S. Carlson ◽  
J. Wobken ◽  
P.V. Tran ◽  
A. Petryk ◽  
...  
Keyword(s):  
Transferrin Receptor ◽  
Iron Uptake ◽  
Sensitive Period ◽  
Transferrin Receptor 1

scholarly journals The C-terminal region of NELL1 mediates osteoblastic cell adhesion through integrin α3β1

FEBS Letters ◽  
2012 ◽  
Vol 586 (16) ◽  
pp. 2500-2506 ◽  
Author(s):  
Ai Hasebe ◽  
Yoko Nakamura ◽  
Hiroki Tashima ◽  
Kaneyoshi Takahashi ◽  
Masumi Iijima ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Terminal Region ◽  
Osteoblastic Cell ◽  
Integrin Α3β1

Preferential hepatic uptake of iron from rat asialotransferrin: possible engagement of two receptors

1986 ◽  
Vol 251 (3) ◽  
pp. G398-G404
Author(s):  
J. R. Rudolph ◽  
E. Regoeczi ◽  
P. A. Chindemi ◽  
M. T. Debanne
Keyword(s):  
Transferrin Receptor ◽  
Iron Uptake ◽  
Rat Hepatocytes ◽  
Hepatic Uptake ◽  
Hepatic Iron ◽  
Transferrin Receptors ◽  
Binding Studies ◽  
Human Transferrin ◽  
Homologous Protein ◽  
Intact Rats

Hepatic iron uptake from and degradation of rat asialotransferrin prepared from the least anionic (major) component of rat transferrin were studied in intact rats. In experiments lasting 60-90 min, rat asialotransferrin delivered a three to four times larger fraction of the Fe dose to the liver than rat transferrin. Variations in the concentration of endogenous circulating rat 2Fe-transferrin by up to 300% failed to affect the enhanced hepatic delivery of Fe from rat asialotransferrin. However, pretreating the animals with a large dose of asialomucin, or fully sialylated human transferrin, or a combination of both did affect the delivery. In all cases, rat asialotransferrin delivered Fe to the liver at rates comparable with those seen with rat transferrin. The reason for the efficacy of human transferrin was clarified in competitive binding studies on rat hepatocytes and reticulocytes, which showed that human transferrin possessed an approximately sevenfold higher affinity for rat transferrin receptors than the homologous protein. These findings suggest that the enhanced hepatic uptake of Fe from rat asialotransferrin is mediated by simultaneous binding of the ligand both through its glycan and transferrin receptor affinity site. Pretreatment with asialomucin and human transferrin had no suppressing effect on basal hepatic delivery of iron from rat 2Fe-transferrin. The data suggest that deposition of a significant fraction of Fe in rat liver from rat transferrin is likely to take place by a mechanism not involving transferrin receptors. Desialylation shortened the metabolic half-life of rat transferrin from 33 to 24 h.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Solid-phase von Willebrand factor contains a conformationally active RGD motif that mediates endothelial cell adhesion through the alpha v beta 3 receptor

Blood ◽  
1993 ◽  
Vol 82 (12) ◽  
pp. 3622-3630 ◽  
Author(s):  
C Denis ◽  
JA Williams ◽  
X Lu ◽  
D Meyer ◽  
D Baruch
Keyword(s):  
Monoclonal Antibody ◽  
Cell Adhesion ◽  
Endothelial Cell ◽  
Von Willebrand Factor ◽  
Solid Phase ◽  
Rgd Sequence ◽  
Alpha V Beta 3 ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Endothelial Cell Adhesion

Abstract The interaction of von Willebrand factor (vWF) with the alpha v beta 3 integrin of human umbilical vein endothelial cells is dependent on the RGD sequence present at residues 1744–1746 of the mature vWF subunit. We compared vWF and its two dimeric fragments, SpIII (residues 1–1365) and SpII (residues 1366–2050), as adhesion substrates. Solid-phase vWF and SpII supported endothelial cell adhesion, whereas SpIII, which contains the glycoprotein (GP) Ib binding domain, did not. Soluble SpII inhibited adhesion to immobilized ligands, whereas soluble vWF did not, suggesting that exposure of the cell attachment domain involves a conformational modification of vWF. Dendroaspin and albolabrin, two RGD- containing peptides of the disintegrin family, were potent inhibitors of cell adhesion to vWF (IC50 approximately 15 nmol/L). Complete inhibition of endothelial cell adhesion to vWF was obtained in the presence of F(ab')2 of monoclonal antibody 9 to vWF, which blocks vWF binding to platelet GPIIb/IIIa. In contrast, monoclonal antibody 713 to vWF, which blocks its binding to platelet GPIb, did not inhibit cell adhesion to vWF. These results indicate that endothelial cell adhesion to vWF is mediated by an RGD-dependent interaction with alpha v beta 3, but does not seem to involve a GPIb-like receptor, and show the importance of the conformation of the RGD sequence.

scholarly journals Transferrin receptor expression and the regulation of placental iron uptake

1991 ◽  
Vol 100 (1) ◽  
pp. 31-38 ◽  
Author(s):  
M. B. Bierings ◽  
M. R. M. Baert ◽  
H. G. van Eijk ◽  
J. P. van Dijk
Keyword(s):  
Transferrin Receptor ◽  
Iron Uptake ◽  
Receptor Expression ◽  
Transferrin Receptor Expression
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