Details

Autor(en) / Beteiligte

• Neil A. Munday
• John P. Vaillancourt
• Ambereen Ali
• Francesca J. Casano
• Douglas K. Miller
• Susan M. Molineaux
• Ting-Ting Yamin
• Violeta L. Yu
• Donald W. Nicholson

Titel

Molecular Cloning and Pro-apoptotic Activity of ICEII and ICEIII, Members of the ICE/CED-3 Family of Cysteine Proteases

Ist Teil von

• The Journal of biological chemistry, 1995-06, Vol.270 (26), p.15870

Ort / Verlag

American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1995

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• Cysteine proteases related to mammalian interleukin-1β-converting enzyme (ICE) and the nematode cell death abnormal ced-3 gene product have been implicated in the effector mechanism of apoptotic cell death. Two novel members of this new family of ICE/CED-3-related proteases, designated ICE -II and ICE -III, were cloned from human monocytic cells. Both were highly homologous to human ICE (52% identical) and CED-3 (25% identical) and both contained the absolutely conserved pentapeptide sequence Gln-Ala-Cys-Arg-Asp containing the catalytic cysteine residue. Other structural motifs that were comparable with ICE suggest that ICE -II and ICE -III are also synthesized as larger proenzymes which are proteolytically processed to form heterodimeric active enzymes. Pro-interleukin-1β processing activity could not be detected in cells transfected with ICE -II or ICE -III, but pro-domain-less truncated forms of ICE -II and ICE -III were capable of effectively inducing fibroblast apoptosis. ICE -II and ICE -III may, therefore, participate in proteolytic events culminating in the apoptotic death of human cells.