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Proteomics in Human Parkinson’s Disease: Present Scenario and Future Directions

  • Anubhuti DixitEmail author
  • Rachna Mehta
  • Abhishek Kumar Singh
Review Paper

Abstract

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.

Keywords

Biomarker Human Parkinson’s disease Proteomics 

Abbreviations

PD

Parkinson’s disease

UCHL1

Ubiquitin carboxy-terminal hydrolase L1

LRRK2

Leucine-rich repeat kinase 2

PINK1

PTEN-induced kinase 1

LNs

Lewy neurites

LBs

Lewy bodies

LC

Locus coeruleus

SN

Substantia nigra

Prx

Peroxiredoxin

CSF

Cerebrospinal fluid

GGH

Gamma glutamyl hydrolase

SOD

Superoxide dismutase

AD

Alzheimer’s disease

Apo

Apolipoprotein

TIMP1

Metalloproteinase inhibitor 1

APLP1

Amyloid-like protein 1

LRP1

Prolow-density lipoprotein receptor-related protein 1

CSF1R

Macrophage colony-stimulating factor 1 receptor

EPHA4

Ephrin type-A receptor 4

PRNP

Major prion protein

HSPG2

Heparan sulfate proteoglycan 2

MEGF8

Multiple EGF-like domains 8

NCAM1

Neural cell adhesion molecule 1

2-DE

Two-dimensional gel electrophoresis

2-D DIGE

Two-dimensional difference gel electrophoresis

MALDI-TOF/TOF-MS

Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

MALDI-IMS

MALDI imaging mass spectrometry

LC-ESI-MS/MS

Liquid chromatography-electrospray ionization tandem mass spectrometry

ESI-Q-TOF MS/MS

Electrospray-quadrupole-time-of-flight tandem mass spectrometry

ESI-MS

Electrospray ionization mass spectrometry

Notes

Acknowledgements

Dr. M. P. Singh and CSIR-Indian Institute of Toxicology Research, Lucknow, India are acknowledged for providing guidance and research facilities to AD.

Author Contributions

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.

Ethical Approval

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

Informed consent was obtained from all individual participants included in the reported studies.

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Authors and Affiliations

  1. 1.Amity Institute of Neuropsychology and NeurosciencesAmity UniversityNoidaIndia

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