Efficient cleavage of Bid and procaspase-7 by caspase-2 at lower pH.
The activity of caspase-2 was examined under varying biochemical conditions with the synthetic and protein substrates, Bid and procaspase-7. The results indicate that it was largely influenced by pH which might be one reason behind the inconsistency for the cleavage of its established substrates during caspase-2-induced apoptosis.
Karki
Pratap
P
Research Center for Proteineous Materials (RCPM), Department of Bio-Materials Engineering, School of Medicine, College of Natural Sciences, Chosun University, Gwangju, 501-759, Republic of Korea.
Dahal
Giri Raj
GR
Shin
Song Yub
SY
Lee
Jung Sup
JS
Cho
Byungyun
B
Park
Il-Seon
IS
D000818:Animals; D051023:BH3 Interacting Domain Death Agonist Protein / Q000378:metabolism*; D053143:Caspase 2 / Q000378:metabolism*; D053179:Caspase 7 / Q000378:metabolism*; D053181:Caspase 8 / Q000378:metabolism; D061945:Caspase Inhibitors; D002417:Cattle; D045744:Cell Line, Tumor; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011485:Protein Binding / Q000187:drug effects; D011499:Protein Processing, Post-Translational; D012965:Sodium Chloride / Q000494:pharmacology
D051023:BH3 Interacting Domain Death Agonist Protein; D061945:Caspase Inhibitors; D012965:Sodium Chloride; D053143:Caspase 2; D053179:Caspase 7; D053181:Caspase 8