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Journal articles on the topic 'Melanotransferrin'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

DESROSIERS, Richard R., Yanick BERTRAND, Quynh-Tran NGUYEN, Michel DEMEULE, Reinhard GABATHULER, Malcolm L. KENNARD, Serge GAUTHIER, and Richard BÉLIVEAU. "Expression of melanotransferrin isoforms in human serum: relevance to Alzheimer's disease." Biochemical Journal 374, no. 2 (September 1, 2003): 463–71. http://dx.doi.org/10.1042/bj20030240.

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Levels of soluble melanotransferrin in serum have been reported to be higher in patients with Alzheimer's disease than in control subjects. The present study investigated melanotransferrin in human body fluids in the light of these findings. To clarify the correlation between melanotransferrin and Alzheimer's disease, the melanotransferrin content was determined by non-reducing, denaturing SDS/PAGE and Western blotting. Under these conditions, serum melanotransferrin migrated at 79 and 82 kDa. Melanotransferrin antigenicity and the relative proportions of the two forms were very sensitive to factors that altered its conformation, including disulphide bridges, pH and bivalent cations. Serum melanotransferrin levels were not significantly different between control subjects and patients with Alzheimer's disease using whole serum, EDTA-supplemented serum or serum immunoglobulin-depleted by Protein G–Sepharose and enriched by affinity precipitation with the lectin from Asparagus pea. Glycosylated forms of serum melanotransferrin bound to Asparagus lectin manifested similar patterns on two-dimensional gel electrophoresis in samples from controls and Alzheimer's disease subjects. Melanotransferrin was also present in saliva and at a high level in urine, but contents were similar in controls and patients with Alzheimer's disease. Together, these results demonstrate that serum melanotransferrin exists in various conformations depending on the binding of bivalent cations or following post-translational modification. These data also indicate that human serum melanotransferrin levels are unchanged in subjects with Alzheimer's disease.

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2

Rahmanto, Yohan Suryo, Sumeet Bal, Kim H. Loh, Yu Yu, and Des R. Richardson. "Melanotransferrin: Search for a function." Biochimica et Biophysica Acta (BBA) - General Subjects 1820, no. 3 (March 2012): 237–43. http://dx.doi.org/10.1016/j.bbagen.2011.09.003.

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3

Nitta, Taizo, Toshitaka Endo, Akira Tsunoda, Yoshiaki Kadota, Toshiharu Matsumoto, and Kiyoshi Sato. "Melanotic neuroectodermal tumor of infancy: a molecular approach to diagnosis." Journal of Neurosurgery 83, no. 1 (July 1995): 145–48. http://dx.doi.org/10.3171/jns.1995.83.1.0145.

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✓ A case of melanotic neuroectodermal tumor of infancy arising from the transverse sinus is presented. The tumor was located on the outer surface of the dura and extended extracranially through the occipitomastoid suture. Two cell populations were observed: pigmented melanocyte-like cells and small neuroblast-like cells. Ultrastructural analysis revealed epithelial tumor cells and melanosomes at various stages. Expression of melanotransferrin messenger RNA transcripts within the tumor tissue was observed using a reverse transcriptase—polymerase chain reaction method in addition to immunohistological studies. The positive expression of melanotransferrin confirmed that this melanotic neuroectodermal tumor was derived from neural crest cells.

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4

McNagny, KM, F. Rossi, G. Smith, and T. Graf. "The eosinophil-specific cell surface antigen, EOS47, is a chicken homologue of the oncofetal antigen melanotransferrin." Blood 87, no. 4 (February 15, 1996): 1343–52. http://dx.doi.org/10.1182/blood.v87.4.1343.bloodjournal8741343.

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The EOS47 antigen is a 100-kD cell surface glycoprotein selectively expressed by avian retrovirus-transformed eosinophils and their precursors. We have purified the EOS47 protein to homogeneity and used peptide sequence information to clone EOS47-encoding cDNAs. The open reading frames from these cDNAs predict a 738 amino acid protein with homology to human melanotransferrin, a membrane-found, transferrin-like protein that is expressed at high levels by a subset of melanomas, tumor cell lines, fetal intestine, and liver, but not by most normal adult tissues. The predicted protein sequence of EOS47 displays a 61% sequence identity with melanotransferrin and conservation of all 28 cysteine residues, indicating a similar tertiary structure. The finding that EOS47 lacks several of the iron-coordinating amino acids present in all transferrins suggests that it may be impaired in its ability to bind iron. In nonhematopoietic tissues, EOS47 is expressed at high levels by epithelial brush borders of small intestine and kidney and at lower levels by cells lining the sinusoids of the liver. Within hematopoietic tissues, EOS47 is restricted to a subpopulation of cells (1% to 5%) in bone marrow and early spleen and fluorescence-activated cell sorting of EOS47+ cells leads to a dramatic ( > 30-fold) enrichment of peroxidase+ eosinophils. In contrast, peripheral blood eosinophils are EOS47-, suggesting that the antigen is expressed by newly formed eosinophils and that expression ceases shortly before these cells emigrate from the bone marrow into the peripheral blood. Our results show that melanotransferrin is a stage-specific marker of eosinophils and should be useful for their isolation and further characterization.

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5

Sekyere, Eric, Michael R. Food, and Des R. Richardson. "A second melanotransferrin gene (MTf2) and a novel protein isoform: explanation for the membrane-bound and soluble forms of melanotransferrin?" FEBS Letters 512, no. 1-3 (January 18, 2002): 350–52. http://dx.doi.org/10.1016/s0014-5793(02)02248-2.

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6

Demeule, Michel, Julie Poirier, Julie Jodoin, Yanick Bertrand, Richard R. Desrosiers, Claude Dagenais, Tran Nguyen, et al. "High transcytosis of melanotransferrin (P97) across the blood-brain barrier." Journal of Neurochemistry 83, no. 4 (November 4, 2002): 924–33. http://dx.doi.org/10.1046/j.1471-4159.2002.01201.x.

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7

Chen, Qingqi, and Reinhard Gabathuler. "Efficient Synthesis of Doxorubicin Melanotransferrin p97 Conjugates Through SMCC Linker." Synthetic Communications 34, no. 13 (January 1, 2004): 2407–14. http://dx.doi.org/10.1081/scc-120039494.

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8

Creagh, A. Louise, Jacqueline W. C. Tiong, Mei Mei Tian, Charles A. Haynes, and Wilfred A. Jefferies. "Calorimetric Studies of Melanotransferrin (p97) and Its Interaction with Iron." Journal of Biological Chemistry 280, no. 16 (February 9, 2005): 15735–41. http://dx.doi.org/10.1074/jbc.m414650200.

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The mammalian molecule melanotransferrin (mTf), also called p97, is a member of the transferrin family of molecules. It exists in both secreted and glycosylphosphatidylinositol-anchored forms and is thought to play a role in angiogenesis and in transporting iron across the blood brain barrier. The binding affinity of iron to this molecule has not been formally established. Here, the binding of ferric ion (chelated with a 2-fold molar ratio of nitrilotriacetate) to mTf has been studied using isothermal titration calorimetry and differential scanning calorimetry. One iron-binding site was determined for mTf with similar binding characteristics to other transferrins. In the absence of bicarbonate, binding occurs quickly with an apparent association constant of 2.6 × 107m–1at 25 °C. The presence of bicarbonate introduces kinetic effects that prevent direct determination of the apparent binding constant by isothermal titration calorimetry. Differential scanning calorimetry thermograms of mTf unfolding in the presence and absence of iron were therefore used to determine the apparent binding constant in the bicarbonate-containing system; at pH 7.5 and 25 °C, iron binding occurs in a 1:1 ratio with aKappof 4.4 × 1017m–1. This affinity is intermediate between the high and low affinity lobes of transferrin and suggests that mTf is likely to play a significant role in iron transport where the high affinity lobe of transferrin is occupied or where transferrin is in proportionally low concentrations.

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9

Baker, Edward N., Heather M. Baker, Clyde A. Smith, Mark R. Stebbins, Maria Kahn, Karl Erik Hellström, and Ingegerd Hellström. "Human melanotransferrin (p97) has only one functional iron-binding site." FEBS Letters 298, no. 2-3 (February 24, 1992): 215–18. http://dx.doi.org/10.1016/0014-5793(92)80060-t.

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10

Kim, D. "Serum Melanotransferrin, p97 as a Biochemical Marker of Alzheimer's Disease." Neuropsychopharmacology 25, no. 1 (July 2001): 84–90. http://dx.doi.org/10.1016/s0893-133x(00)00230-x.

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11

Chen, Qingqi, Damian A. Sowa, Jianlin Cai, and Reinhard Gabathuler. "Synthesis of Doxorubicin Conjugates Through Hydrazone Bonds to Melanotransferrin P97." Synthetic Communications 33, no. 14 (January 8, 2003): 2377–90. http://dx.doi.org/10.1081/scc-120021827.

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12

Sekyere, Eric, Michael R. Food, and Des R. Richardson. "Corrigendum to: A second melanotransferrin gene (MTf2) and a novel protein isoform: explanation for the membrane-bound and soluble forms of melanotransferrin? (FEBS 25737)." FEBS Letters 547, no. 1-3 (June 17, 2003): 234. http://dx.doi.org/10.1016/s0014-5793(03)00657-4.

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13

Sekyere, Eric, and Des R. Richardson. "The membrane-bound transferrin homologue melanotransferrin: roles other than iron transport?" FEBS Letters 483, no. 1 (October 9, 2000): 11–16. http://dx.doi.org/10.1016/s0014-5793(00)02079-2.

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14

Rolland, Y., M. Demeule, J. Michaud-Levesque, J. Leclerc, and R. Béliveau. "42 POSTER Potent inhibition of glioblastoma growth and angiogenesis by melanotransferrin." European Journal of Cancer Supplements 4, no. 12 (November 2006): 17. http://dx.doi.org/10.1016/s1359-6349(06)70048-9.

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15

Bertrand, Yanick, Michel Demeule, Jonathan Michaud-Levesque, and Richard Béliveau. "Melanotransferrin induces human melanoma SK-Mel-28 cell invasion in vivo." Biochemical and Biophysical Research Communications 353, no. 2 (February 2007): 418–23. http://dx.doi.org/10.1016/j.bbrc.2006.12.034.

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16

Michaud-Levesque, J., M. Demeule, and R. Beliveau. "In vivo inhibition of angiogenesis by a soluble form of melanotransferrin." Carcinogenesis 28, no. 2 (July 8, 2006): 280–88. http://dx.doi.org/10.1093/carcin/bgl123.

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17

Chen, Qingqi, Damian A. Sowa, and Reinhard Gabathuler. "Synthesis of Doxorubicin Conjugates Through 14-Hydroxy Group to Melanotransferrin P97." Synthetic Communications 33, no. 14 (January 8, 2003): 2391–400. http://dx.doi.org/10.1081/scc-120021828.

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18

Rolland, Yannève, Michel Demeule, Laurence Fenart, and Richard Béliveau. "Inhibition of melanoma brain metastasis by targeting melanotransferrin at the cell surface." Pigment Cell & Melanoma Research 22, no. 1 (February 2009): 86–98. http://dx.doi.org/10.1111/j.1755-148x.2008.00525.x.

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19

Demeule, Michel, Yanick Bertrand, Jonathan Michaud-Levesque, Julie Jodoin, Yannève Rolland, Reinhard Gabathuler, and Richard Béliveau. "Regulation of plasminogen activation: a role for melanotransferrin (p97) in cell migration." Blood 102, no. 5 (September 1, 2003): 1723–31. http://dx.doi.org/10.1182/blood-2003-01-0166.

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AbstractWe recently reported that human recombinant melanotransferrin (p97) presents a high transport rate across the blood-brain barrier that might involve the low-density lipoprotein receptor–related protein (LRP). We now report new interactions between p97 and another LRP ligand, the urokinase plasminogen activator (uPA) complex. By using biospecific interaction analysis, both pro-uPA and plasminogen are shown to interact with immobilized p97. Moreover, the activation of plasminogen by pro-uPA is increased by soluble p97. Because the uPA system plays a crucial role in cell migration, both in cancer and in angiogenesis, we also measured the impact of both endogenous membrane-bound and exogenous p97 on cell migration. The monoclonal antibody L235 (which recognizes a conformational epitope on p97) inhibited the migration of human microvascular endothelial cells (HMECs-1) and of human melanoma SK-MEL-28 cells, indicating that endogenous membrane-bound p97 could be associated with this process. In addition, low concentrations of exogenous p97 (10 and 100 nM) inhibited HMEC-1 and SK-MEL28 cell migration by more than 50%. These results indicate that membrane-bound and soluble p97 affect the migration capacity of endothelial and melanoma cells and suggest that p97 could be involved in the regulation of plasminogen activation by interacting with pro-uPA and plasminogen.

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20

Rolland, Yannève, Michel Demeule, Jonathan Michaud-Levesque, and Richard Béliveau. "Inhibition of tumor growth by a truncated and soluble form of melanotransferrin." Experimental Cell Research 313, no. 13 (August 2007): 2910–19. http://dx.doi.org/10.1016/j.yexcr.2007.04.013.

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21

Sekyere, Eric, Louise L. Dunn, and Des R. Richardson. "The double-edged nature of using genetic databases: melanotransferrin genes and transcripts." FEBS Letters 547, no. 1-3 (June 17, 2003): 233. http://dx.doi.org/10.1016/s0014-5793(03)00658-6.

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22

Barresi, Gaetano, and Giovanni Tuccari. "Immunocytochemical demonstration of melanotransferrin (p97) in thyroid tumors of follicular cell origin." Pathology 26, no. 2 (1994): 127–29. http://dx.doi.org/10.1080/00313029400169341.

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23

Yamada, T., Y. Tsujioka, J. Taguchi, M. Takahashi, Y. Tsuboi, I. Moroo, J. Yang, and Wilfred A. Jefferies. "Melanotransferrin is produced by senile plaque-associated reactive microglia in Alzheimer's disease." Brain Research 845, no. 1 (October 1999): 1–5. http://dx.doi.org/10.1016/s0006-8993(99)01767-9.

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24

Dunn, L. L., E. O. Sekyere, Y. Suryo Rahmanto, and D. R. Richardson. "The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis." Carcinogenesis 27, no. 11 (May 16, 2006): 2157–69. http://dx.doi.org/10.1093/carcin/bgl045.

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25

Rozé, Anne, Mario M. Zakin, and Nathalie Duchange. "Regulation of melanotransferrin gene in melanoma cells. Analysis of the enhancer region." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1260, no. 3 (February 1995): 301–7. http://dx.doi.org/10.1016/0167-4781(94)00208-k.

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26

Furukawa, K. S., K. Furukawa, F. X. Real, L. J. Old, and K. O. Lloyd. "A unique antigenic epitope of human melanoma is carried on the common melanoma glycoprotein gp95/p97." Journal of Experimental Medicine 169, no. 2 (February 1, 1989): 585–90. http://dx.doi.org/10.1084/jem.169.2.585.

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Analysis of antibodies present in the serum of melanoma patient FD has shown that they detect a unique tumor epitope present only on the autologous melanoma cell line SK-MEL-131. Previous results had shown that the unique FD epitope is carried on a common glycoprotein of approximately 90 kD, widely expressed on melanoma and a few other cell types. We now show by sequential radioimmunoprecipitation and partial amino acid sequencing that this common molecule is a previously recognized melanoma antigen, originally identified by mouse mAbs, designated gp95 or p97 (and also known as melanotransferrin). Thus, FD is the first of the class I (unique) melanoma antigens that has been characterized and related to a known cell surface molecule.

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27

Alemany, R., M. R. Vila, C. Franci, G. Egea, F. X. Real, and T. M. Thomson. "Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): apical compartmentalization in intestinal epithelial cells." Journal of Cell Science 104, no. 4 (April 1, 1993): 1155–62. http://dx.doi.org/10.1242/jcs.104.4.1155.

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Melanotransferrin (p97) is an iron-binding membrane glycoprotein with 40% homology to transferrin and lactoferrin. It was first identified on the basis of its high level of expression in melanoma cells, as compared to normal melanocytes. It is also present in many cultured cell types. In normal tissues, p97 is expressed in fetal intestine, umbilical cord, sweat gland ducts and liver sinusoidal lining cells. Kinetic studies in melanoma cells have suggested that p97 plays a role in iron metabolism. We have examined expression of p97 in cell lines derived from human colorectal carcinomas which express a differentiated phenotype. When polarized, these cells showed a preferred apical distribution of p97, as demonstrated by immunohistochemistry, immune electron microscopy and domain-selective biotinylation. Correspondingly, p97 was only found on the apical brush border of epithelial cells in the fetal intestine. p97 was shown to be anchored to the membrane through a glycosyl phosphatidylinositol moiety by treatment with phophatidylinositol-specific phospholipase C (PI-PLC) and labeling with [14C]ethanolamine. These observations provide a basis for the elucidation of the physiological role of p97 in iron metabolism and its possible role in cell proliferation and malignant cell transformation.

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28

Béliveau, R. "Vectorization of proteins across the blood-brain barrier: high transcytosis of melanotransferrin (P97)." Journal of Neurochemistry 85 (May 8, 2003): 7. http://dx.doi.org/10.1046/j.1471-4159.85.s2.7_4.x.

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29

Sekyere, Eric O., Louise L. Dunn, Yohan Suryo Rahmanto, and Des R. Richardson. "Role of melanotransferrin in iron metabolism: studies using targeted gene disruption in vivo." Blood 107, no. 7 (April 1, 2006): 2599–601. http://dx.doi.org/10.1182/blood-2005-10-4174.

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AbstractMelanotransferrin (MTf) or tumor antigen p97 is a transferrin homolog that binds one iron (Fe) atom and has been suggested to play roles in a variety of processes, including Fe metabolism, eosinophil differentiation, and plasminogen activation. Considering the vital role of Fe in many metabolic pathways, such as DNA and heme synthesis, it is important to understand the function of MTf. To define this, a MTf knockout (MTf–/–) mouse was generated through targeted disruption of the MTf gene. The MTf–/– mice were viable and fertile and developed normally, with no morphologic or histologic abnormalities. Assessment of Fe indices, tissue Fe levels, hematology, and serum chemistry parameters demonstrated no differences between MTf–/– and wild-type (MTf+/+) mice, suggesting MTf was not essential for Fe metabolism.

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30

Tiklová, Katarína, Kirsten-André Senti, Shenqiu Wang, Astrid Gräslund, and Christos Samakovlis. "Epithelial septate junction assembly relies on melanotransferrin iron binding and endocytosis in Drosophila." Nature Cell Biology 12, no. 11 (October 10, 2010): 1071–77. http://dx.doi.org/10.1038/ncb2111.

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31

Kuo, Yung-Chih, and In-Wei Chao. "Conjugation of melanotransferrin antibody on solid lipid nanoparticles for mediating brain cancer malignancy." Biotechnology Progress 32, no. 2 (December 31, 2015): 480–90. http://dx.doi.org/10.1002/btpr.2214.

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32

Food, Michael R., and Des R. Richardson. "Iron uptake by melanoma cells from the soluble form of the transferrin homologue, melanotransferrin." Redox Report 7, no. 5 (October 2002): 279–82. http://dx.doi.org/10.1179/135100002125000794.

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33

Bertrand, Y., M. Demeule, G. E. Rivard, and R. Béliveau. "Stimulation of tPA-dependent provisional extracellular fibrin matrix degradation by human recombinant soluble melanotransferrin." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1763, no. 10 (October 2006): 1024–30. http://dx.doi.org/10.1016/j.bbamcr.2006.08.006.

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34

Qiu, Xuemei, Dong Li, Jun Cui, Yang Liu, and Xiuli Wang. "Molecular cloning, characterization and expression analysis of Melanotransferrin from the sea cucumber Apostichopus japonicus." Molecular Biology Reports 41, no. 6 (February 18, 2014): 3781–91. http://dx.doi.org/10.1007/s11033-014-3243-1.

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35

Sala, Roberta, Wilfred A. Jefferies, Brandie Walker, Joseph Yang, Jacqueline Tiong, S. K. Alex Law, Mariella F. Carlevaro, et al. "The human melanoma associated protein melanotransferrin promotes endothelial cell migration and angiogenesis in vivo." European Journal of Cell Biology 81, no. 11 (November 2002): 599–607. http://dx.doi.org/10.1078/0171-9335-00280.

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36

Chen, Qingqi, Damian A. Sowa, Jianlin Cai, and Reinhard Gabathuler. "Efficient One-Pot Synthesis of Doxorubicin Conjugates Through Its Amino Group to Melanotransferrin P97." Synthetic Communications 33, no. 14 (January 8, 2003): 2401–21. http://dx.doi.org/10.1081/scc-120021829.

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37

Jefferies, Wilfred A., Michael R. Food, Reinhard Gabathuler, Sylvia Rothenberger, Tatsuo Yamada, Osamu Yasuhara, and Patrick L. McGeer. "Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin." Brain Research 712, no. 1 (March 1996): 122–26. http://dx.doi.org/10.1016/0006-8993(95)01407-1.

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38

Rothenberger, Sylvia, Michael R. Food, Reinhard Gabathuler, Malcolm L. Kennard, Tatsuo Yamada, Osamu Yasuhara, Patrick L. McGeer, and Wilfred A. Jefferies. "Coincident expression and distribution of melanotransferrin and transferrin receptor in human brain capillary endothelium." Brain Research 712, no. 1 (March 1996): 117–21. http://dx.doi.org/10.1016/0006-8993(96)88505-2.

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39

SAWAKI, KOICHI, MITSURO KANDA, SHINICHI UMEDA, TAKASHI MIWA, CHIE TANAKA, DAISUKE KOBAYASHI, MASAMICHI HAYASHI, et al. "Level of Melanotransferrin in Tissue and Sera Serves as a Prognostic Marker of Gastric Cancer." Anticancer Research 39, no. 11 (November 2019): 6125–33. http://dx.doi.org/10.21873/anticanres.13820.

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40

Rose, T. M., G. D. Plowman, D. B. Teplow, W. J. Dreyer, K. E. Hellstrom, and J. P. Brown. "Primary structure of the human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence." Proceedings of the National Academy of Sciences 83, no. 5 (March 1, 1986): 1261–65. http://dx.doi.org/10.1073/pnas.83.5.1261.

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41

Smith, Leia M., Albina Nesterova, Stephen C. Alley, Michael Y. Torgov, and Paul J. Carter. "Potent cytotoxicity of an auristatin-containing antibody-drug conjugate targeting melanoma cells expressing melanotransferrin/p97." Molecular Cancer Therapeutics 5, no. 6 (June 2006): 1474–82. http://dx.doi.org/10.1158/1535-7163.mct-06-0026.

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42

Rolland, Yannève, Michel Demeule, and Richard Béliveau. "Melanotransferrin stimulates t-PA-dependent activation of plasminogen in endothelial cells leading to cell detachment." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1763, no. 4 (April 2006): 393–401. http://dx.doi.org/10.1016/j.bbamcr.2006.03.006.

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43

Suryo Rahmanto, Y., L. L. Dunn, and D. R. Richardson. "The melanoma tumor antigen, melanotransferrin (p97): a 25-year hallmark – from iron metabolism to tumorigenesis." Oncogene 26, no. 42 (April 23, 2007): 6113–24. http://dx.doi.org/10.1038/sj.onc.1210442.

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44

Xin, Vechtova, Shaliutina-Kolesova, Fussy, Loginov, Dzyuba, Linhart, et al. "Transferrin Identification in Sterlet (Acipenser ruthenus) Reproductive System." Animals 9, no. 10 (September 30, 2019): 753. http://dx.doi.org/10.3390/ani9100753.

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Transferrins are a superfamily of iron-binding proteins and are recognized as multifunctional proteins. In the present study, transcriptomic and proteomic methods were used to identify transferrins in the reproductive organs and sperm of out-of-spawning and spermiating sterlet (Acipenser ruthenus) males. The results showed that seven transferrin transcripts were identified in the transcriptome of sterlet, and these transcripts were qualified as two different transferrin genes, serotransferrin and melanotransferrin, with several isoforms present for serotransferrin. The relative abundance of serotransferrin isoforms was higher in the kidneys and Wolffian ducts in the spermiating males compared to out-of-spawning males. In addition, transferrin was immunodetected in sterlet seminal plasma, but not in sterlet spermatozoa extract. Mass spectrometry identification of transferrin in seminal plasma but not in spermatozoa corroborates immunodetection. The identification of transferrin in the reproductive organs and seminal plasma of sterlet in this study provides the potential function of transferrin during sturgeon male reproduction.

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45

Shin, Jihye, Hye-Jung Kim, Gamin Kim, Meiying Song, Se Joon Woo, Seung-Taek Lee, Hoguen Kim, and Cheolju Lee. "Discovery of Melanotransferrin as a Serological Marker of Colorectal Cancer by Secretome Analysis and Quantitative Proteomics." Journal of Proteome Research 13, no. 11 (September 23, 2014): 4919–31. http://dx.doi.org/10.1021/pr500790f.

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46

Duchange, Nathalie, Alberto Ochoa, Gregory D. Plowman, Anne Rozé, Mardjan Amdjadi, and Mario M. Zakin. "Identification of an enhancer involved in the melanoma-specific expression of the tumor antigen melanotransferrin gene." Nucleic Acids Research 20, no. 11 (1992): 2853–59. http://dx.doi.org/10.1093/nar/20.11.2853.

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47

Michaud-Levesque, Jonathan, Michel Demeule, and Richard Béliveau. "Stimulation of cell surface plasminogen activation by membrane-bound melanotransferrin: A key phenomenon for cell invasion." Experimental Cell Research 308, no. 2 (August 2005): 479–90. http://dx.doi.org/10.1016/j.yexcr.2005.05.004.

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48

SEKYERE, E., L. DUNN, and D. RICHARDSON. "Examination of the distribution of the transferrin homologue, melanotransferrin (tumour antigen p97), in mouse and human." Biochimica et Biophysica Acta (BBA) - General Subjects 1722, no. 2 (March 11, 2005): 131–42. http://dx.doi.org/10.1016/j.bbagen.2004.12.002.

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Hegedus, Dwayne D., Tom A. Pfeifer, David A. Theilmann, Malcolm L. Kennard, Reinhard Gabathuler, Wilfred A. Jefferies, and Thomas A. Grigliatti. "Differences in the Expression and Localization of Human Melanotransferrin in Lepidopteran and Dipteran Insect Cell Lines." Protein Expression and Purification 15, no. 3 (April 1999): 296–307. http://dx.doi.org/10.1006/prep.1998.1021.

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Hernández-Pasos, Josué, Griselle Valentín-Tirado, and José E. García-Arrarás. "Melanotransferrin: New Homolog Genes and Their Differential Expression during Intestinal Regeneration in the Sea CucumberHolothuria glaberrima." Journal of Experimental Zoology Part B: Molecular and Developmental Evolution 328, no. 3 (February 23, 2017): 259–74. http://dx.doi.org/10.1002/jez.b.22731.

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