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Melanotransferrin is a serological marker of colorectal cancer by secretome analysis and quantitative proteomics.
PC3 tumors are sustained by a small number of tumor-initiating cells with stem-like characteristics, including strong self-renewal and pro-angiogenic capability and marked by the expression pattern FAM65Bhigh/MFI2low/LEF1low.
The human genome contains a second melanotransferrin gene (MTf2). There are two isoforms of melanotransferrin.
its ability to donate 59Fe to SK-Mel-28 melanoma cells and other cell types
This melanoma-associated marker was detected in melanoma cell lines.
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.
Serum melanotransferrin exists in various conformations depending on the binding of bivalent cations or following post-translational modification; serum melanotransferrin levels are unchanged in subjects with Alzheimer's disease.
The distribution of MTf and its splice variants may provide clues to their possible biological roles in melanoma and other tumors.
melanotransferrin has a role in cell proliferation and tumorigenesis
Anti-angiogenic properties of soluble melanotransferrin may result from local overstimulation of plasminogen activation by tissue plasminogen activator, thus leading to subsequent degradation of the fibronectin matrix and endothelial cell detachment.
Altogether, these findings strongly suggest that MTf overexpression in melanoma cells contributes to tumor progression by stimulating plasmin generation as well as cell migration and invasion.
HMB-45 (melanoma-associated antigen p97) and Melan-A combined were positive in 100% of the renal angiomyolipomas
Novel molecular targets directly or indirectly regulated by MTf and the potential pathways involved in its function, including modulation of proliferation.
this review discusses the studies that have demonstrated that melanotransferrin is not involved in iron metabolism, but plays a vital role in melanoma cell proliferation and tumorigenesis.
results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP
Biochemical and spectroscopic studies of MTF1 are reported.
MTf represents the first identification of a plant lectin receptor involved in cell-shape changes and the differentiation of animal cells
Iron indices, tissue levels, hematology, and serum chemistry parameters demonstrated no differences between metallototransferrin deficient and wild-type mice, suggesting MTf was not essential for iron metabolism.
The protein encoded by this gene is a cell-surface glycoprotein found on melanoma cells. The protein shares sequence similarity and iron-binding properties with members of the transferrin superfamily. The importance of the iron binding function has not yet been identified. This gene resides in the same region of chromosome 3 as members of the transferrin superfamily. Alternative splicing results in two transcript variants.
melanoma-associated antigen p97
, membrane-bound transferrin-like protein
, membrane-bound transferrin-like protein p97
, LOW QUALITY PROTEIN: melanotransferrin