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Mohamed Ismail Nounou, Chris E Adkins, Evelina Rubinchik, Tori B Terrell-Hall, Mohamed Afroz, Tim Vitalis, Reinhard Gabathuler, Mei Mei Tian, Paul R Lockman
PURPOSE: The ability of human melanotransferrin (hMTf) to carry a therapeutic concentration of trastuzumab (BTA) in the brain after conjugation (in the form of trastuzumab-melanotransferrin conjugate, BT2111 conjugate) was investigated by measuring the reduction of the number and size of metastatic human HER(2+) breast cancer tumors in a preclinical model of brain metastases of breast cancer. METHODS: Human metastatic brain seeking breast cancer cells were injected in NuNu mice (n = 6-12 per group) which then developed experimental brain metastases...
August 15, 2016: Pharmaceutical Research
Jasmina Paluncic, Zaklina Kovacevic, Patric J Jansson, Danuta Kalinowski, Angelika M Merlot, Michael L-H Huang, Hiu Chuen Lok, Sumit Sahni, Darius J R Lane, Des R Richardson
Melanoma has markedly increased worldwide during the past several decades in the Caucasian population and is responsible for 80% of skin cancer deaths. Considering that metastatic melanoma is almost completely resistant to most current therapies and is linked with a poor patient prognosis, it is crucial to further investigate potential molecular targets. Major cell-autonomous drivers in the pathogenesis of this disease include the classical MAPK (i.e., RAS-RAF-MEK-ERK), WNT, and PI3K signaling pathways. These pathways play a major role in defining the progression of melanoma, and some have been the subject of recent pharmacological strategies to treat this belligerent disease...
April 2016: Biochimica et Biophysica Acta
Yung-Chih Kuo, I-Hsin Wang
Melanotransferrin antibody (MA) and tamoxifen (TX) were conjugated on etoposide (ETP)-entrapped solid lipid nanoparticles (ETP-SLNs) to target the blood-brain barrier (BBB) and glioblastom multiforme (GBM). MA- and TX-conjugated ETP-SLNs (MA-TX-ETP-SLNs) were used to infiltrate the BBB comprising a monolayer of human astrocyte-regulated human brain-microvascular endothelial cells (HBMECs) and to restrain the proliferation of malignant U87MG cells. TX-grafted ETP-SLNs (TX-ETP-SLNs) significantly enhanced the BBB permeability coefficient for ETP and raised the fluorescent intensity of calcein-AM when compared with ETP-SLNs...
August 2016: Journal of Drug Targeting
Yung-Chih Kuo, In-Wei Chao
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...
March 2016: Biotechnology Progress
Lina Bai, Mu Qiao, Rong Zheng, Changyan Deng, Shuqi Mei, Wanping Chen
Transferrins have been identified in animals and green algae, and they consist of a family of evolutionarily related proteins that play a central role in iron transport, immunity, growth and differentiation. This study assessed the transferrin genes among 100 genomes from a wide range of animal and plant kingdoms. The results showed that putative transferrins were widespread in animals, but their gene quantity and type differ greatly between animal groups. Generally, Mammalia possess abundant transferrin genes, whereas Trematoda contain few ones...
March 2016: Comparative Biochemistry and Physiology. Part D, Genomics & Proteomics
Kamila Duś-Szachniewicz, Paweł Ostasiewicz, Marta Woźniak, Paweł Kołodziej, Jacek R Wiśniewski, Piotr Ziółkowski
BACKGROUND: Our previous liquid chromatography-tandem mass spectrometry (LC-MS/MS) study on colorectal cancer proteome resulted in identification of 10,000 differentially expressed proteins. We observed a significantly changed expression of 25% of all identified proteins between patient and matched adjacent normal mucosa, carcinoma and colorectal adenoma, including melanotransferrin. Herein, we consider this protein as a potential biomarker of colorectal cancer. MATERIALS AND METHODS: Immunohistochemical detection of melanotransferrin was carried-out to localize its expression pattern within the colorectal tissues by tissue microarray...
December 2015: Anticancer Research
Jihye Shin, Hye-Jung Kim, Gamin Kim, Meiying Song, Se Joon Woo, Seung-Taek Lee, Hoguen Kim, Cheolju Lee
To discover serological colorectal cancer (CRC) markers, we analyzed cell line secretome to gather proteins of higher potential to be secreted from tissues into circulation. A total of 898 human proteins were identified, of which 62.2% were predicted to be released or shed from cells. The identified proteins were compared with tissue proteomes to find candidate proteins whose expressions were elevated in tumor tissues compared with normal tissues as revealed by (i) quantitative proteomic analysis based on cICAT and mTRAQ or (ii) data mining of immunohistochemical images piled in Human Protein Atlas database...
November 7, 2014: Journal of Proteome Research
Austin L Hughes, Robert Friedman
In a phylogenetic analysis of vertebrate transferrins (TFs), six major clades (subfamilies) were identified: (a) S, the mammalian serotransferrins; (b) ICA, the mammalian inhibitor of carbonic anhydrase (ICA) homologs; (c) L, the mammalian lactoferrins; (d) O, the ovotransferrins of birds and reptiles; (e) M, the melanotransferrins of bony fishes, amphibians, reptiles, birds, and mammals; and (f) M-like, a newly identified TF subfamily found in bony fishes, amphibians, reptiles, and birds. A phylogenetic tree based on the joint alignment of N-lobes and C-lobes supported the hypothesis that three separate events of internal duplication occurred in vertebrate TFs: (a) in the common ancestor of the M subfamily, (b) in the common ancestor of the M-like subfamily, and (c) in the common ancestor of other vertebrate TFs...
November 2014: Immunogenetics
Xuemei Qiu, Dong Li, Jun Cui, Yang Liu, Xiuli Wang
Melanotransferrin (MTf), a member of the transferrin families, plays an important role in immune response. But the research about MTf in sea cucumber is limited till now. In this study, the Melanotransferrin (Aj-MTf) gene was firstly cloned and characterized from the sea cucumber Apostichoupus japonicus by reverse transcriptase polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends. The full-length cDNA of Aj-MTf is 2,840 bp in length and contains a 2,184 bp open reading frame that encodes a polypeptide of 727 amino acids...
June 2014: Molecular Biology Reports
Hirzahida Mohd-Padil, Adura Mohd-Adnan, Toni Gabaldón
Transferrin is a protein super-family involved in iron transport, a central process in cellular homeostasis. Throughout the evolution of vertebrates, transferrin members have diversified into distinct subfamilies including serotransferrin, ovotransferrin, lactoferrin, melanotransferrin, the inhibitor of carbonic anhydrase, pacifastin, and the major yolk protein in sea urchin. Previous phylogenetic analyses have established the branching order of the diverse transferrin subfamilies but were mostly focused on the transferrin repertoire present in mammals...
April 2013: Molecular Biology and Evolution
Reinhard Gabathuler
The central nervous system is a sanctuary protected by barriers, among which the blood-brain barrier (BBB). The BBB is formed by the specific nature of the endothelial cells of the brain capillaries, that allow brain access only to nutrients necessary for brain cell survival and function. These properties of the BBB result in the incapacity of therapeutic compounds, both small and large, to reach the brain at therapeutic concentrations. Various strategies are now being developed to enhance the amount and concentration of these compounds in the brain parenchyma...
2012: Biologie Aujourd'hui
Minglin Lang, Caroline L Braun, Michael R Kanost, Maureen J Gorman
Multicopper ferroxidases catalyze the oxidation of ferrous iron to ferric iron. In yeast and algae, they participate in cellular uptake of iron; in mammals, they facilitate cellular efflux. The mechanisms of iron metabolism in insects are still poorly understood, and insect multicopper ferroxidases have not been identified. In this paper, we present evidence that Drosophila melanogaster multicopper oxidase-1 (MCO1) is a functional ferroxidase. We identified candidate iron-binding residues in the MCO1 sequence and found that purified recombinant MCO1 oxidizes ferrous iron...
August 14, 2012: Proceedings of the National Academy of Sciences of the United States of America
Yohan Suryo Rahmanto, Sumeet Bal, Kim H Loh, Yu Yu, Des R Richardson
BACKGROUND: Melanotransferrin was discovered in the 1980s as one of the first melanoma tumour antigens. The molecule is a transferrin homologue that is found predominantly bound to the cell membrane by a glycosyl-phosphatidylinositol anchor. MTf was described as an oncofoetal antigen expressed in only small quantities in normal tissues, but in much larger amounts in neoplastic cells. Several diseases are associated with expression of melanotransferrin, including melanoma and Alzheimer's disease, although the significance of the protein to the pathogenesis of these conditions remains unclear...
March 2012: Biochimica et Biophysica Acta
Lisa A Lambert
BACKGROUND: In vertebrates, serum transferrins are essential iron transporters that have bind and release Fe(III) in response to receptor binding and changes in pH. Some family members such as lactoferrin and melanotransferrin can also bind iron while others have lost this ability and have gained other functions, e.g., inhibitor of carbonic anhydrase (mammals), saxiphilin (frogs) and otolith matrix protein 1 (fish). SCOPE OF REVIEW: This article provides an overview of the known transferrin family members and their associated receptors and interacting partners...
March 2012: Biochimica et Biophysica Acta
Øivind Andersen, Maria Cristina De Rosa, Davide Pirolli, Ave Tooming-Klunderud, Petra E Petersen, Carl André
BACKGROUND: The two homologous iron-binding lobes of transferrins are thought to have evolved by gene duplication of an ancestral monolobal form, but any conserved synteny between bilobal and monolobal transferrin loci remains unexplored. The important role played by transferrin in the resistance to invading pathogens makes this polymorphic gene a highly valuable candidate for studying adaptive divergence among local populations. RESULTS: The Atlantic cod genome was shown to harbour two tandem duplicated serum transferrin genes (Tf1, Tf2), a melanotransferrin gene (MTf), and a monolobal transferrin gene (Omp)...
2011: BMC Genetics
Katarína Tiklová, Kirsten-André Senti, Shenqiu Wang, Astrid Gräslund, Christos Samakovlis
Iron is an essential element in many biological processes. In vertebrates, serum transferrin is the major supplier of iron to tissues, but the function of additional transferrin-like proteins remains poorly understood. Melanotransferrin (MTf) is a phylogenetically conserved, iron-binding epithelial protein. Elevated MTf levels have been implicated in melanoma pathogenesis. Here, we present a functional analysis of MTf in Drosophila melanogaster. Similarly to its human homologue, Drosophila MTf is a lipid-modified, iron-binding protein attached to epithelial cell membranes, and is a component of the septate junctions that form the paracellular permeability barrier in epithelial tissues...
November 2010: Nature Cell Biology
Jia Liu, Shicui Zhang, Lei Li
Previous studies have shown the universal presence of transferrin (Tf) in both invertebrates and vertebrates, but little information is available regarding Tf in amphioxus, a protochordate on the evolutionary boundary between invertebrates and vertebrates. Here we isolated a Tf-like homolog from Branchiostoma belcheri, which encodes a deduced protein, BbTfl, of 1256 amino acids containing a N-terminal signal peptide, a conserved transferrin domain in its N-terminal lobe, with a putative iron-binding site consisting of Asp63 and Try188 and another transferrin domain in its C-terminal lobe with an long intervening sequence of 305 amino acids...
September 2009: Molecular Immunology
Yohan Suryo Rahmanto, Des R Richardson
Melanotransferrin (MTf) is a transferrin homologue that binds iron (Fe) through a high affinity Fe-binding site. MTf has been implicated in diverse processes, e.g., iron metabolism, plasminogen activation, eosinophil differentiation and cancer cell migration, proliferation and tumourigenesis. Our previous studies using a knockout mouse demonstrated that MTf does not have an essential function in Fe metabolism (E.O. Sekyere, L.L. Dunn, Y.S. Rahmanto, D.R. Richardson, Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo, Blood 107 (2006) 2599-2601)...
July 2009: Biochimica et Biophysica Acta
Wei-Yi Ong, Andrew M Jenner, Ning Pan, Choon-Nam Ong, Barry Halliwell
Rabbits were fed a diet containing 1% cholesterol for 8 weeks and the levels of iron and oxidized lipids in liver analysed using atomic absorption spectroscopy and gas chromatography-mass spectrometry. A non-significant trend to an increase in iron level, but significant increases in the lipid peroxidation products, F(2)-isoprostanes and the cholesterol oxidation products 7 beta hydroxycholesterol, 7 ketocholesterol and cholesterol 5,6-alpha epoxide were detected in the liver of the cholesterol-fed rabbits...
March 2009: Free Radical Research
Yannève Rolland, Michel Demeule, Laurence Fenart, Richard Béliveau
Brain metastases are a common feature of malignant melanoma and are associated with poor prognosis. Melanotransferrin (MTf), one of several antigens associated with the surface of melanoma cells, has been demonstrated to promote cell invasion. In this study, we investigated the role of membrane-bound MTf in several of the steps leading to the development of melanoma brain metastasis. Our results indicated that MTf-positive cells were detected in the brains of nude mice injected intravenously with human melanoma SK-Mel 28 cells...
February 2009: Pigment Cell & Melanoma Research
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