| Abstrakt: |
Intracellular protein degradation is prevalently carried out by the nonlysosomal ubiquitin proteolytic system; to enter this pathway, the protein has to be tagged by oligomers of ubiquitin, because in this form it becomes a selective target of the proteasome, the central protease of the pathway. The repertoire of proteins degraded by the proteasome is continually growing, and it has been elucidated that the proteasome activity is essential in a wide range of vital cellular processes extending from cell division and differentiation, DNA repair, transcription factor and regulatory protein processing, and membrane receptor internalization to inflammatory response and antigen presentation. However, from the beginning the proteasome has emerged as an important determinant in the defense against oxidative stress by providing the degradation of oxidized, damaged, misfolded, or unfolded proteins, thereby preventing their accumulation. Furthermore, the considerable progress made in the proteasome characterization in various cell and tissue types has uncovered that the proteasome has great structural and functional plasticity, which constitutes a prerequisite for its selective and efficient targeting by different challenges. However, the characterization of proteasome expression, activity, function, and structural properties in the central nervous tissue is not entirely defined and is very poor with regard to neurodegenerative diseases. This chapter focuses on what is known about the proteasome properties in the central nervous system in health and degenerative conditions. [ABSTRACT FROM AUTHOR] |
