Page 12 - T. Protein modification and regulation
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[T. Protein modification and regulation-6]
Misfolded human Z-type α₁-antitrypsin makes the host
vulnerable to the oxidative stress
Jaeyeon Lim¹, Hana Im¹
¹Integrative Bioscience and Biotechnology, Sejong University, Seoul 05006, Republic of Korea
Protein folding of human α₁-antitrypsin Z-type variant is extremely retarded, and thus accumulates folding
intermediates prone to aggregation in endoplasmic reticulum. Several misfolded proteins, such as in Parkinson’s
and Alzheimer diseases, are known to increase oxidative stress and lead to subsequent cell death. Accumulation of
misfolded Z-type α₁-antitrypsin provoked oxidative stress, and made the cells more vulnerable to further oxidative
challenges. Deletions of yeast genes involved in the oxidative response pathway exacerbated the slow growth
phenotype of Z-type α₁-antitrypsin-expression. Antioxidant treatment mitigated Z-type α₁-antitrypsin-induced
oxidative stress. Our results might provide further information on therapeutic strategies to deal with protein folding
diseases.
