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Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
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Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Redox state influence on human galectin-1 function.

Xing Yu1, Stacy A Scott1, Rhys Pritchard2

  • 1Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.

Biochimie
|June 28, 2015
PubMed
Summary
This summary is machine-generated.

Human galectin-1

Keywords:
FarnesylGalectin-1RasRedox

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Human galectin-1's functions are redox-sensitive due to its cysteine residues.
  • Galectin-1 interacts with Ras proteins, crucial for signal transduction.
  • Mutated Ras proteins drive tumor growth, angiogenesis, and metastasis.

Purpose of the Study:

  • To investigate the impact of redox state on galectin-1's interaction with farnesyl analogues.
  • To explore galectin-1's independent growth inhibitory activity.
  • To examine the redox effect on galectin-1's extracellular functions.

Main Methods:

  • Exploration of galectin-1's interaction with farnesyl analogues under different redox conditions.
  • Site-directed mutagenesis (K28T) to assess specific binding regions.
  • Assessment of galectin-1's protective effect on leukemia cells against oxidative stress.

Main Results:

  • Reduced galectin-1 directly binds farnesyl independently of carbohydrate binding.
  • A K28T mutation abolishes farnesyl recognition by reduced galectin-1, indicating a separate binding site.
  • Oxidized galectin-1 also recognizes farnesyl and protects acute lymphoblastic leukemia cells from oxidative stress.

Conclusions:

  • Redox state significantly modulates galectin-1's interaction with H-Ras farnesyl moiety.
  • Galectin-1 possesses a distinct region for farnesyl binding, separate from its carbohydrate-binding domain.
  • Oxidized galectin-1 exhibits a protective role in leukemia cells under oxidative stress.