title: The methodology of neuroproteomics.
abstract: The human central nervous system (CNS) is the most complex organ in nature, composed of ten trillion cells forming complex neural networks using a quadrillion synaptic connections. Proteins, their modifications, and their interactions are integral to CNS function. The emerging field of neuroproteomics provides us with a wide-scope view of posttranslation protein dynamics within the CNS to better our understanding of its function, and more often, its dysfunction consequent to neurodegenerative disorders. This chapter reviews methodology employed in the neurosciences to study the neuroproteome in health and disease. The chapter layout parallels this volume's four parts. Part I focuses on modeling human neuropathology in animals as surrogate, accessible, and controllable platforms in our research. Part II discusses methodology used to focus analysis onto a subneuroproteome. Part III reviews analytical and bioinformatic technologies applied in neuroproteomics. Part IV discusses clinical neuroproteomics, from processing of human biofluids to translation in biomarkers research. Neuroproteomics continues to mature as a discipline, confronting the extreme complexity of the CNS proteome and its dynamics, and providing insight into the molecular mechanisms underlying how our nervous system works and how it is compromised by injury and disease.
authors.affiliation: Department of Anatomy & Neurobiology, Virginia Commonwealth University, Richmond, VA, USA. akottens@vcu.edu
authors.forename: Andrew K
authors.initials: AK
authors.lastname: Ottens
mesh_terms: D000818:Animals; D019295:Computational Biology / Q000379:methods; D006801:Humans; D008953:Models, Anatomic; D009419:Nerve Tissue Proteins / Q000032:analysis*; D009420:Nervous System; D009422:Nervous System Diseases / Q000503:physiopathology; D019636:Neurodegenerative Diseases / Q000503:physiopathology; D009488:Neurosciences / Q000379:methods*; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D039781:PubMed; D013572:Synaptic Vesicles / Q000737:chemistry / Q000648:ultrastructure; D057170:Translational Research, Biomedical
chemical_list: D009419:Nerve Tissue Proteins