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Related Concept Videos

The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
The Significance of Membrane Transport01:44

The Significance of Membrane Transport

The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.

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Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
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Published on: May 10, 2022

Melanotransferrin: search for a function.

Yohan Suryo Rahmanto1, Sumeet Bal, Kim H Loh

  • 1Department of Pathology and Bosch Institute, Blackburn Building (D06), University of Sydney, Sydney, New South Wales, 2006 Australia.

Biochimica Et Biophysica Acta
|September 22, 2011
PubMed
Summary
This summary is machine-generated.

Melanotransferrin (MTf), a transferrin homologue, is highly expressed in cancers like melanoma. Its roles in iron transport, angiogenesis, and tumor growth suggest potential as an immunotherapy target.

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Last Updated: May 29, 2026

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Published on: May 10, 2022

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Area of Science:

  • Biochemistry
  • Oncology
  • Immunology

Background:

  • Melanotransferrin (MTf) is a cell membrane-bound transferrin homologue discovered as a melanoma tumor antigen.
  • MTf is an oncofoetal antigen, with low expression in normal tissues but high levels in neoplastic cells.
  • Associated diseases include melanoma and Alzheimer's, though MTf's role in pathogenesis is unclear.

Purpose of the Study:

  • To review the physiological and pathological roles of melanotransferrin.
  • To explore the potential of melanotransferrin as an immunotherapy target.

Main Methods:

  • Literature review of studies on melanotransferrin's biological functions and clinical associations.
  • Analysis of melanotransferrin's involvement in various disease states.

Main Results:

  • Melanotransferrin is implicated in iron transport, angiogenesis, cell proliferation, migration, and tumorigenesis.
  • High expression of MTf in malignant melanoma and other diseases suggests clinical significance.

Conclusions:

  • While MTf's precise biological functions are still being elucidated, its roles in key cellular processes are increasingly recognized.
  • Further research into melanotransferrin biology may unveil novel therapeutic strategies for cancer treatment.