The membrane‐bound transferrin homologue melanotransferrin: roles other than iron transport?

Sekyere, Eric; Richardson, Des R.

doi:10.1016/s0014-5793(00)02079-2

Cited by 51 publications

(44 citation statements)

References 46 publications

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“…These CHO cells expressed 1.2 Â 10 6 MTf molecules per cell, a level three-to four-fold higher than that of the most highly expressing, naturally-derived melanoma cell line, SK-MEL-28 (300-380 000 sites/cell; Brown et al, 1981a;Sekyere and Richardson, 2000). However, after an incubation of 240 min, the Fe uptake from 59 Fe-citrate was only 2.4 times greater than the control CHO cells not expressing MTf (Kennard et al, 1995).…”

Section: Functional Role Of Mtf: Melanoma Iron Transport and Metabolismmentioning

confidence: 98%

“…An MTf-like gene has been identified in the fruit fly, Drosophila melanogaster, and also in the mosquito, Anopheles gambiae (Adams et al, 2000). However, unlike other members of the MTf family, these insect molecules show far lower homology to other MTf family members and the single Fe-binding site is not conserved (Sekyere and Richardson, 2000). Hence, the role of these MTf-like proteins in insect Fe metabolism is unclear.…”

Section: Genomic and Molecular Organization Of Mtfmentioning

confidence: 99%

“…As found in Tf, the critical Fe-binding ligands in the N-terminal of MTf consists of the DYRYH motif (Table 2), which is composed of Asp78, Tyr107, Arg136, Tyr210 and His279 . In contrast to Tf, the C-terminal of MTf consists of SYSYH, in which Asp-421 and Arg-482 are replaced by serine resulting in a general disruption of H-bonding and loss of the Fe-binding motif (Bailey et al, 1988;Baker and Lindley, 1992;Nakamasu et al, 1999;Sekyere and Richardson, 2000). Analysis of the protein sequence encoded by the hDMTf transcript suggests that the potential protein product does not bind Fe, as the His279 residue has been replaced by valine (Sekyere et al, 2005).…”

Section: Mtf Gene Transcriptionmentioning

confidence: 99%

“…If metalloprotease activity is an important function of MTf, one may expect the motif to be conserved across species. However, this motif is absent in the mouse, chicken and rabbit, suggesting that at least in these organisms, MTf probably has no significant metalloprotease activity (Sekyere and Richardson, 2000).…”

Section: Mtf Gene Transcriptionmentioning

confidence: 99%

“…A general hypothesis initially existed that MTf may be overexpressed on melanoma cells to assist with their increased Fe requirements for proliferation (Brown et al, 1982;Richardson and Baker, 1990;Sekyere and Richardson, 2000).…”

Section: Functional Role Of Mtf: Melanoma Iron Transport and Metabolismmentioning

confidence: 99%

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The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark – from iron metabolism to tumorigenesis

2007

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Melanotransferrin (MTf) or melanoma tumor antigen p97 is a transferrin (Tf) homolog that is found predominantly bound to the cell membrane via a glycosyl phosphatidylinositol anchor. The molecule is a member of the Tf superfamily and binds iron through a single high-affinity iron(III)-binding site. Since its discovery on the plasma membrane of melanoma cells, the function of MTf has remained intriguing, particularly in relation to its role in cancer cell iron transport. In fact, considering the crucial role of iron in many metabolic pathways, e.g., DNA synthesis, it was important to understand the function of MTf in the transport of this vital nutrient. MTf has also been implicated in diverse physiological processes, such as plasminogen activation, angiogenesis and cell migration. However, recent studies using a knockout mouse and posttranscriptional gene silencing have demonstrated that MTf is not involved in iron metabolism, but plays a vital role in melanoma cell proliferation and tumorigenesis. In this review, we discuss the possible biological functions of MTf, particularly in relation to cancer.

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Section: Functional Role Of Mtf: Melanoma Iron Transport and Metabolismmentioning

confidence: 98%

Section: Genomic and Molecular Organization Of Mtfmentioning

confidence: 99%

Section: Mtf Gene Transcriptionmentioning

confidence: 99%

Section: Mtf Gene Transcriptionmentioning

confidence: 99%

Section: Functional Role Of Mtf: Melanoma Iron Transport and Metabolismmentioning

confidence: 99%

See 3 more Smart Citations

The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark – from iron metabolism to tumorigenesis

2007

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Conjugation of melanotransferrin antibody on solid lipid nanoparticles for mediating brain cancer malignancy

Kuo

Chao

2015

Biotechnology Progress

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Solid lipid nanoparticles (SLNs) comprising complex internal lipids were conjugated with melanotransferrin antibody (MA) to carry anticancer etoposide across the blood-brain barrier (BBB) for managing glioblastoma multiforme (GBM). MA was crosslinked on the surface of etoposide-loaded SLNs (ETP-SLNs) to target human brain-microvascular endothelial cells (HBMECs) and U87MG cells. The experimental evidences showed that an increase in the tripalmitin weight percentage in lipids enhanced the particle size and viability of U87MG cells, however decreased the etoposide loading efficiency, MA conjugation efficiency, and permeability coefficient for etoposide across the BBB. A high level of MA on the particle surface increased the atomic ratio of nitrogen to phosphorus and permeability coefficient for propidium iodide and etoposide across the BBB, however reduced the MA conjugation efficiency, transendothelial electrical resistance, and viability of U87MG cells. Based on immunochemical staining, we found that MA on ETP-SLNs triggered the melanotransferrin-mediated transcytosis and promoted the growth-inhibitory efficacy to U87MG cells. MA-conjugated ETP-SLNs can be a promising colloidal delivery system for malignant GBM pharmacotherapy. © 2015 American Institute of Chemical Engineers Biotechnol. Prog., 32:480-490, 2016.

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The structure and evolution of the murine inhibitor of carbonic anhydrase: A member of the transferrin superfamily

et al. 2010

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The original signature of the transferrin (TF) family of proteins was the ability to bind ferric iron with high affinity in the cleft of each of two homologous lobes. However, in recent years, new family members that do not bind iron have been discovered. One new member is the inhibitor of carbonic anhydrase (ICA), which as its name indicates, binds to and strongly inhibits certain isoforms of carbonic anhydrase. Recently, mouse ICA has been expressed as a recombinant protein in a mammalian cell system. Here, we describe the 2.4 Å structure of mouse ICA from a pseudomerohedral twinned crystal. As predicted, the structure is bilobal, comprised of two a-b domains per lobe typical of the other family members. As with all but insect TFs, the structure includes the unusual reverse c-turn in each lobe. The structure is consistent with the fact that introduction of two mutations in the N-lobe of murine ICA (mICA) (W124R and S188Y) allowed it to bind iron with high affinity. Unexpectedly, both lobes of the mICA were found in the closed conformation usually associated with presence of iron in the cleft, and making the structure most similar to diferric pig TF. Two new ICA family members (guinea pig and horse) were identified from genomic sequences and used in evolutionary comparisons. Additionally, a comparison of selection pressure (dN/dS) on functional residues reveals some interesting insights into the evolution of the TF family including that the N-lobe of lactoferrin may be in the process of eliminating its iron binding function.

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The membrane‐bound transferrin homologue melanotransferrin: roles other than iron transport?

Cited by 51 publications

References 46 publications

The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark – from iron metabolism to tumorigenesis

The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark – from iron metabolism to tumorigenesis

Conjugation of melanotransferrin antibody on solid lipid nanoparticles for mediating brain cancer malignancy

The structure and evolution of the murine inhibitor of carbonic anhydrase: A member of the transferrin superfamily

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