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Degradation of basic protein and Wolfgram protein in central nervous system by soluble enzymes of human peripheral
Abstract:
The present communication describes the ability of soluble enzymes (SE) of peripheral polymorphonuclear leucocytes of control and multiple sclerosis (MS) patients to degrade major myelin proteins of MS and control myelin. MS and control SE degraded in situ both Wolfgram protein (WP) and basic protein (BP) of isolated myelin. No differences were found between the action of control and MS patients SE on myelin. However, significantly less degradation of BP and WP in control myelin compared to that in MS myelin was found. Only 30% of SE samples (both control and MS) degraded significant amounts of proteolipid protein in myelin. It is postulated that SE associated demyelination in MS may be a factor contributing to the demyelinating process.
Insights
Soluble enzymes from white blood cells can break down myelin proteins in multiple sclerosis (MS) patients and controls. This enzyme activity may contribute to demyelination in MS.
Area of Science:
- Neuroimmunology
- Biochemistry
- Cellular Biology
Background:
- Multiple Sclerosis (MS) is a demyelinating disease of the central nervous system.
- The role of soluble enzymes (SE) from peripheral polymorphonuclear leucocytes (PMNs) in myelin degradation is not fully understood.
Purpose of the Study:
- To investigate the capacity of SE from PMNs of control and MS patients to degrade major myelin proteins.
- To compare the myelin-degrading activity of SE between MS patients and healthy controls.
Main Methods:
- Isolation of myelin from control and MS brain tissue.
- Incubation of isolated myelin with SE derived from peripheral PMNs of control and MS subjects.
- Quantification of myelin protein degradation, including Wolfgram protein (WP), basic protein (BP), and proteolipid protein (PLP).
Main Results:
- Both control and MS SE degraded WP and BP in isolated myelin.
- No significant difference was observed in the SE's ability to degrade myelin proteins between control and MS groups.
- Control myelin showed significantly less degradation of BP and WP compared to MS myelin when acted upon by SE.
- Approximately 30% of SE samples, from both control and MS groups, degraded significant amounts of PLP.
Conclusions:
- SE associated with PMNs possess the capability to degrade key myelin proteins.
- The observed differences in myelin degradation susceptibility suggest MS myelin may be more vulnerable to SE action.
- SE-mediated myelin degradation is postulated as a potential contributing factor to the demyelination process in MS.