Chemokine Proteolytic Processing in HIV Infection: Neurotoxic and Neuroimmune Consequences

  • David Vergote
  • Christopher M. Overall
  • Christopher Power
Chapter

Abstract

Together with transcriptional and translational regulation, posttranslational modification is a pivotal mechanism regulating protein abundance and function. Proteolysis has been suggested to be the most important posttranslational modification of proteins – it affects every protein and can result in marked changes in activity and eventual clearance (Doucet et al. 2008). Not only do protein degradation and processing modulate protein stability, permitting extra- or misfolded protein recycling, but they are also important evolutionary strategies for generating bioactive molecules that affect cell function and survival. Two major enzymatic mechanisms are known to be involved in protein degradation and processing: (1) ubiquitin-dependent degradation of proteins by the proteasome and (2) protease-dependent maturation and processing of proteins with ensuing effects on their biological functions. Indeed, the maturation of numerous neuropeptides involves sequential proteolytic cleavages of a precursor protein by different proteases leading to peptide products with pleiotropic effects (see (Hallberg and Nyberg 2003) for review). Requisite maturation by proteolysis has also been reported for molecules involved in immune response including inflammatory proteins (pro-IL-1β by caspase-1/ICE and MMP-9 (Cerretti et al. 1992; Schonbeck et al. 1998), pro-TNF-α by ADAM17/TACE (Moss et al. 1997), TGFβ by plasmin (Yee et al. 1993), receptors (protease-activated receptors by their ligands) (Noorbakhsh et al. 2003), or elements of the complement cascade (Gasque 2004) to reveal their full activity. Several proteins acquire neuropathogenic properties following a proteolytic processing; one of the best examples occurs in Alzheimer’s disease in which the pathogenicity of amyloid peptides depends on proteases, namely secretases, involved in amyloid precursor protein (APP) maturation. This chapter will describe how the proteolysis of chemokines might participate in the neuropathogenesis of HIV infection, thus contributing to the development of the central nervous system disorder termed HIV-associated dementia (HAD).

Keywords

Depression Dementia Cysteine Serine Trypsin 

Notes

Acknowledgments

The authors thank Leah DeBlock for assistance with manuscript preparation. D.V. was supported by a Toupin Chair Fellowship. C.P. and C.M.O. hold Canada Research Chairs (T1) in Neurological Infection and Immunity, and Metalloproteinase Proteomics and Systems Biology, respectively. This research was supported by the Canadian Institutes for Health Research (CIHR), the Canadian Foundation for AIDS Research (CANFAR), National Institutes of Health (NIMH), and an Infrastructure Grant from the Michael Smith Research Foundation (University of British Columbia Centre for Blood Research). The authors have no conflicting financial interests.

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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • David Vergote
    • 1
  • Christopher M. Overall
    • 2
  • Christopher Power
    • 1
  1. 1.Department of Medicine (Neurology), 6-11 Heritage Medical Research CentreUniversity of AlbertaEdmontonCanada
  2. 2.Molecular Biology and Biochemistry and Oral Biological and Medical SciencesUniversity of British ColumbiaVancouverCanada

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