緑膿菌におけるD - アミノ酸脱水素酵素

京都大学0048新制・課程博士医学博士医博第121号新制||医||41(附属図書館)479京都大学大学院医学研究科生理系専攻(主査)教授 早石 修, 教授 山田 肇, 教授 島本 暉朗学位規則第5条第1項該当Kyoto UniversityDA

CPP32/Yama/apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme

AbstractDNA-dependent protein kinase (DNA-PK) is composed of a 460-kDa catalytic component (p460) and a DNA-binding component Ku protein. Immunoblot analysis after treatment of Jurkat cells with anti-Fas antibody demonstrated the cleavage of p460 concomitantly with an increase in CPP32/Yama/apopain activity. Recombinant CPP32/Yama/apopain specifically cleaved p460 in the DNA-PK preparation that had been purified from Raji cells into 230- and 160-kDa polypeptides, the latter of which was detected in anti-Fas-treated Jurkat cells. The regulatory component Ku protein was not significantly affected by CPP32/Yama/apopain. DNA-PK activity was decreased with the disappearance of p460 in the incubation of DNA-PK with CPP32/Yama/apopain. These results suggest that the catalytic component of DNA-PK is one of the target proteins for CPP32/Yama/apopain in Fas-mediated apoptosis