Proteomics in Human Parkinson’s Disease: Present Scenario and Future Directions
Parkinson’s disease (PD) is an age-related, threatening neurodegenerative disorder with no reliable treatment till date. Identification of specific and reliable biomarker is a major challenge for disease diagnosis and designing effective therapeutic strategy against it. PD pathology at molecular level involves abnormal expression and function of several proteins, including alpha-synuclein. These proteins affect the normal functioning of neurons through various post-translational modifications and interaction with other cellular components. The role of protein anomalies during PD pathogenesis can be better understood by the application of proteomics approach. A number of proteomic studies conducted on brain tissue, blood, and cerebrospinal fluid of PD patients have identified a wide array of protein alterations underlying disease pathogenesis. However, these studies are limited by the types of brain regions or biofluids utilized in the research. For a complete understanding of PD mechanism and discovery of reliable protein biomarkers, it is essential to analyze the proteome of different PD-associated brain regions and easily accessible biofluids such as saliva and urine. The present review summarizes the major advances in the field of PD research in humans utilizing proteomic techniques. Moreover, potential samples for proteomic analysis and limitations associated with the analyses of different types of samples have also been discussed.
KeywordsBiomarker Human Parkinson’s disease Proteomics
Ubiquitin carboxy-terminal hydrolase L1
Leucine-rich repeat kinase 2
PTEN-induced kinase 1
Gamma glutamyl hydrolase
Metalloproteinase inhibitor 1
Amyloid-like protein 1
Prolow-density lipoprotein receptor-related protein 1
Macrophage colony-stimulating factor 1 receptor
Ephrin type-A receptor 4
Major prion protein
Heparan sulfate proteoglycan 2
Multiple EGF-like domains 8
Neural cell adhesion molecule 1
Two-dimensional gel electrophoresis
- 2-D DIGE
Two-dimensional difference gel electrophoresis
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
MALDI imaging mass spectrometry
Liquid chromatography-electrospray ionization tandem mass spectrometry
- ESI-Q-TOF MS/MS
Electrospray-quadrupole-time-of-flight tandem mass spectrometry
Electrospray ionization mass spectrometry
Dr. M. P. Singh and CSIR-Indian Institute of Toxicology Research, Lucknow, India are acknowledged for providing guidance and research facilities to AD.
AD-Review design, literature collection, data interpretation, and manuscript preparation. RM-Review design and manuscript preparation. AKS-Review design and manuscript preparation.
Compliance with Ethical Standards
Conflict of interest
The authors declare that they do not have any conflict of interest.
All reported studies involving human participants/animals have been previously published and procedures performed in studies were in accordance with applicable ethical standards of the institution and/or national research committee, international, national, and/or institutional guidelines, and 1964 Helsinki Declaration and its later amendments or comparable ethical standards.
Informed consent was obtained from all individual participants included in the reported studies.
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