scholarly journals Localized serine protease activity and the establishment ofDrosophilaembryonic dorsoventral polarity

Fly ◽  
2013 ◽  
Vol 7 (3) ◽  
pp. 161-167 ◽  
Author(s):  
David Stein ◽  
Yong Suk Cho ◽  
Leslie M Stevens
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Dorsoventral Polarity ◽  
Serine Protease Activity

A novel mechanism for imatinib mesylate–induced cell death of BCR-ABL–positive human leukemic cells: caspase-independent, necrosis-like programmed cell death mediated by serine protease activity

Blood ◽  
2004 ◽  
Vol 103 (6) ◽  
pp. 2299-2307 ◽  
Author(s):  
Masayuki Okada ◽  
Souichi Adachi ◽  
Tsuyoshi Imai ◽  
Ken-ichiro Watanabe ◽  
Shin-ya Toyokuni ◽  
...  
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Serine Protease ◽  
Imatinib Mesylate ◽  
Protease Activity ◽  
Kinase Inhibitor ◽  
Leukemic Cells ◽  
Endonuclease G ◽  
Serine Protease Activity ◽  
Human Leukemic Cells

Abstract Caspase-independent programmed cell death can exhibit either an apoptosis-like or a necrosis-like morphology. The ABL kinase inhibitor, imatinib mesylate, has been reported to induce apoptosis of BCR-ABL–positive cells in a caspase-dependent fashion. We investigated whether caspases alone were the mediators of imatinib mesylate–induced cell death. In contrast to previous reports, we found that a broad caspase inhibitor, zVAD-fmk, failed to prevent the death of imatinib mesylate–treated BCR-ABL–positive human leukemic cells. Moreover, zVAD-fmk–preincubated, imatinib mesylate–treated cells exhibited a necrosis-like morphology characterized by cellular pyknosis, cytoplasmic vacuolization, and the absence of nuclear signs of apoptosis. These cells manifested a loss of the mitochondrial transmembrane potential, indicating the mitochondrial involvement in this caspase-independent necrosis. We excluded the participation of several mitochondrial factors possibly involved in caspase-independent cell death such as apoptosis-inducing factor, endonuclease G, and reactive oxygen species. However, we observed the mitochondrial release of the serine protease Omi/HtrA2 into the cytosol of the cells treated with imatinib mesylate or zVAD-fmk plus imatinib mesylate. Furthermore, serine protease inhibitors prevented the caspase-independent necrosis. Taken together, our results suggest that imatinib mesylate induces a caspase-independent, necrosis-like programmed cell death mediated by the serine protease activity of Omi/HtrA2.

Acute myocardial infarction elevates serine protease activity in saliva of patients with periodontitis

2011 ◽  
Vol 47 (3) ◽  
pp. 345-353 ◽  
Author(s):  
P. Mäntylä ◽  
E. Buduneli ◽  
G. Emingil ◽  
T. Tervahartiala ◽  
P. J. Pussinen ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity

Human Monocytes Possess a Serine Protease Activity Capable of Degrading HIV-1 Reverse Transcriptase in Vitro

2001 ◽  
Vol 285 (4) ◽  
pp. 863-872 ◽  
Author(s):  
Marie-Thérèse Château ◽  
Véronique Robert-Hebmann ◽  
Christian Devaux ◽  
Jean-Bernard Lazaro ◽  
Bruno Canard ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Serine Protease ◽  
Protease Activity ◽  
Human Monocytes ◽  
Serine Protease Activity ◽  
Hiv 1

scholarly journals The homotrimeric structure of HtrA2 is indispensable for executing its serine protease activity

2006 ◽  
Vol 38 (1) ◽  
pp. 36-43 ◽  
Author(s):  
Min-Kyung Nam ◽  
Young-Mo Seong ◽  
Hyo-Jin Park ◽  
Ju-Youn Choi ◽  
Seongman Kang ◽  
...  
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity

scholarly journals NS3 protein of Hepatitis C virus associates with the tumour suppressor p53 and inhibits its function in an NS3 sequence-dependent manner

2006 ◽  
Vol 87 (6) ◽  
pp. 1703-1713 ◽  
Author(s):  
Lin Deng ◽  
Motoko Nagano-Fujii ◽  
Motofumi Tanaka ◽  
Yuki Nomura-Takigawa ◽  
Masanori Ikeda ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Subcellular Localization ◽  
Serine Protease ◽  
Protease Activity ◽  
Hcv Rna ◽  
Dependent Manner ◽  
Diffuse Type ◽  
Serine Protease Activity ◽  
Tumour Suppressor P53

The N-terminal 198 residues of NS3 (NS3-N) of Hepatitis C virus (HCV) subtype 1b obtained from 29 patients, as well as full-length NS3 (NS3-Full), were analysed for their subcellular localization, interaction with the tumour suppressor p53 and serine protease activity in the presence and absence of the viral cofactor NS4A. Based on the subcellular-localization patterns in the absence of NS4A, NS3-N sequences were classified into three groups, with each group exhibiting either dot-like, diffuse or a mixed type of localization. Chimeric NS3-Full sequences, each consisting of an individual NS3-N and a shared C-terminal sequence, showed the same localization patterns as those of the respective NS3-N. Site-directed mutagenesis experiments revealed that a single or a few amino acid substitutions at a particular position(s) of NS3-N altered the localization pattern. Interestingly, NS3 of the dot-like type, either NS3-N or NS3-Full, interacted with p53 more strongly than that of the diffuse type, in both the presence and the absence of NS4A. Moreover, NS3-N of the dot-like type suppressed trans-activating activity of p53 more strongly than that of the diffuse type. Serine protease activity did not differ significantly between the two types of NS3. In HCV RNA replicon-harbouring cells, physical interaction between NS3 and p53 was observed consistently and p53-mediated transcriptional activation was suppressed significantly compared with HCV RNA-negative control cells. Our results collectively suggest the possibility that NS3 plays an important role in the hepatocarcinogenesis of HCV by interacting differentially with p53 in an NS3 sequence-dependent manner.

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