נגישות
menu      
חיפוש מתקדם
תחביר
חפש...
הספר "אוצר וולקני"
אודות
תנאי שימוש
ניהול
קהילה:
אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Activation pathways and signal-mediated upregulation of the insect Spodoptera frugiperda caspase-1
Year:
2006
Source of publication :
apoptosis (source)
Authors :
צ'חנובסקי, נור
;
.
Volume :
11
Co-Authors:
Liu, Q., Entomology Department, Institute of Plant Protection, Volcani Center, POB 6, Bet Dagan 50250, Israel, State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, China, State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, 430072, China
Chejanovsky, N., Entomology Department, Institute of Plant Protection, Volcani Center, POB 6, Bet Dagan 50250, Israel
Facilitators :
From page:
487
To page:
496
(
Total pages:
10
)
Abstract:
Sf-caspase-1 is the most studied effector caspase of Lepidoptera. Its activation is believed to follow a two-step mechanism: The first step requires cleavage by an initiator caspase at D195 (between the large and small subunits) releasing the C-terminal small subunit. This is blocked by the baculovirus caspase inhibitor P49. The second step removes the N-terminal prodomain by cleavage at D28 to generate the large subunit that is blocked by the baculovirus caspase inhibitor P35. In this study, we identified an alternative mechanism of Sf-caspase-1 activation. This additional two-step mechanism involves first cleavage of pro-Sf-caspase-1 at D28 to remove the N-terminal prodomain and subsequently cleavage at D195 to generate the large and small subunits. Both mechanisms are triggered by apoptotic stimuli following a distinct pattern. We also showed that expression of Sf-caspase-1 was upregulated upon reception of apoptotic stimuli. Different from all published data, this upregulation occurred as a post-transcriptional event. Moreover, we proved that the stronger the stimuli, the higher the upregulation. And we demonstrated that P49 and P35 inhibited the cleavage at D28 and D195 respectively, independently of wether the first cleavage was at D195 or at D28. © 2006 Springer Science + Business Media, LLC.
Note:
Related Files :
animal cell
Animals
apoptosis
carboxy terminal sequence
Insecta
Lepidoptera
protein p49
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1007/s10495-006-5059-5
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23304
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:58
You may also be interested in
Scientific Publication
Activation pathways and signal-mediated upregulation of the insect Spodoptera frugiperda caspase-1
11
Liu, Q., Entomology Department, Institute of Plant Protection, Volcani Center, POB 6, Bet Dagan 50250, Israel, State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, China, State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, 430072, China
Chejanovsky, N., Entomology Department, Institute of Plant Protection, Volcani Center, POB 6, Bet Dagan 50250, Israel
Activation pathways and signal-mediated upregulation of the insect Spodoptera frugiperda caspase-1
Sf-caspase-1 is the most studied effector caspase of Lepidoptera. Its activation is believed to follow a two-step mechanism: The first step requires cleavage by an initiator caspase at D195 (between the large and small subunits) releasing the C-terminal small subunit. This is blocked by the baculovirus caspase inhibitor P49. The second step removes the N-terminal prodomain by cleavage at D28 to generate the large subunit that is blocked by the baculovirus caspase inhibitor P35. In this study, we identified an alternative mechanism of Sf-caspase-1 activation. This additional two-step mechanism involves first cleavage of pro-Sf-caspase-1 at D28 to remove the N-terminal prodomain and subsequently cleavage at D195 to generate the large and small subunits. Both mechanisms are triggered by apoptotic stimuli following a distinct pattern. We also showed that expression of Sf-caspase-1 was upregulated upon reception of apoptotic stimuli. Different from all published data, this upregulation occurred as a post-transcriptional event. Moreover, we proved that the stronger the stimuli, the higher the upregulation. And we demonstrated that P49 and P35 inhibited the cleavage at D28 and D195 respectively, independently of wether the first cleavage was at D195 or at D28. © 2006 Springer Science + Business Media, LLC.
Scientific Publication
You may also be interested in