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Title: Degradomics in Neurotrauma : Profiling Traumatic Brain Injury
Authors: Abou El Hassan, Hadi
Sukhon, Fares
Assaf, Edwyn Jeremy
Bahmad, Hisham
Abou-Abbass, Hussein
Jourdi, Hussam 
Kobeissy, Firas H.
Affiliations: Department of Biology 
Keywords: Degradomics
Degradation (C)
Subjects: Big data
Issue Date: 2017
Part of: J. Walker, J. Pollard & E. Murray (Eds.), Methods in Molecular Biology. Humana Press.
Start page: 65
End page: 99
Degradomics has recently emerged as a subdiscipline in the omics era with a focus on characterizing signature breakdown products implicated in various disease processes. Driven by promising experimental findings in cancer, neuroscience, and metabolomic disorders, degradomics has significantly promoted the notion of disease-specific "degradome." A degradome arises from the activation of several proteases that target specific substrates and generate signature protein fragments. Several proteases such as calpains, caspases, cathepsins, and matrix metalloproteinases (MMPs) are involved in the pathogenesis of numerous diseases that disturb the physiologic balance between protein synthesis and protein degradation. While regulated proteolytic activities are needed for development, growth, and regeneration, uncontrolled proteolysis initiated under pathological conditions ultimately culminates into apoptotic and necrotic processes. In this chapter, we aim to review the protease-substrate repertoires in neural injury concentrating on traumatic brain injury. A striking diversity of protease substrates, essential for neuronal and brain structural and functional integrity, namely, encryptic biomarker neoproteins, have been characterized in brain injury. These include cytoskeletal proteins, transcription factors, cell cycle regulatory proteins, synaptic proteins, and cell junction proteins. As these substrates are subject to proteolytic fragmentation, they are ceaselessly exposed to activated proteases. Characterization of these molecules allows for a surge of "possible" therapeutic approaches of intervention at various levels of the proteolytic cascade.
Ezproxy URL: Link to full text
Type: Book Chapter
Appears in Collections:Department of Biology

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