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Oxidative modification of serum proteins in multiple sclerosis
Izabela Sadowska-Bartosz1, Monika Adamczyk-Sowa, Sabina Galiniak
1Department of Biochemistry and Cell Biology, University of Rzeszow, ul. Zelwerowicza 4, 35-601 Rzeszów, Poland.
Neurochemistry International
|September 17, 2013
Summary
Oxidative and glycoxidative damage are present in multiple sclerosis (MS). Markers like advanced protein oxidation products (AOPP) can help monitor oxidative stress during MS therapy.
Area of Science:
- Neuroimmunology
- Biochemistry
- Oxidative Stress Research
Background:
- Multiple sclerosis (MS) is associated with oxidative stress and increased glycoxidation.
- Protein modifications due to oxidative and glycoxidative damage are implicated in MS pathogenesis.
Purpose of the Study:
- To compare markers of protein oxidative damage and glycoxidation in different MS patient groups and healthy controls.
- To assess the utility of these markers in monitoring MS and its therapies.
Main Methods:
- Spectrophotometric and fluorimetric analysis of protein oxidation and glycoxidation markers.
- Comparison of marker levels in relapsing-remitting MS patients (untreated, in relapse, treated with interferon β1a, interferon β1b, or glatiramer acetate) and healthy subjects.
Main Results:
- Elevated glycophore content in untreated RRMS patients and those treated with glatiramer acetate.
- Increased advanced protein oxidation products (AOPP) in untreated RRMS patients and those in clinical relapse.
- Correlation of protein modification markers with C-reactive protein and white blood cell count, indicating a link to inflammation.
Conclusions:
- Protein oxidative and glycoxidative damage are confirmed in MS.
- Markers, particularly AOPP, show potential for monitoring oxidative stress during MS treatment.
- Oxidative protein modifications are linked to inflammatory processes in MS.
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Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.

