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

A desquamation paradox of atopic dermatitis–Markedly remaining corneodesmosomes despite the increased serine protease activity in vitro

2013 ◽  
Vol 69 (2) ◽  
pp. e41
Author(s):  
Satomi Igawa ◽  
Shin Iinuma ◽  
Mari Kishibe ◽  
Masako Minami-Hori ◽  
Masaru Honma ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity

Evidence that cell surface localization of serine protease activity facilitates cleavage of the protease activated receptor CDCP1

2018 ◽  
Vol 399 (9) ◽  
pp. 1091-1097
Author(s):  
Yaowu He ◽  
Janet C. Reid ◽  
Hui He ◽  
Brittney S. Harrington ◽  
Brittney Finlayson ◽  
...  
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Serine Proteases ◽  
Membrane Localization ◽  
Cub Domain ◽  
Serine Protease Activity ◽  
Surface Localization ◽  
Cell Surface Localization

Abstract The cellular receptor CUB domain containing protein 1 (CDCP1) is commonly elevated and functionally important in a range of cancers. CDCP1 is cleaved by serine proteases at adjacent sites, arginine 368 (R368) and lysine 369 (K369), which induces cell migration in vitro and metastasis in vivo. We demonstrate that membrane localization of serine protease activity increases efficacy of cleavage of CDCP1, and that both secreted and membrane anchored serine proteases can have distinct preferences for cleaving at CDCP1-R368 and CDCP1-K369. Approaches that disrupt membrane localization of CDCP1 cleaving serine proteases may interfere with the cancer promoting effects of CDCP1 proteolysis.

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
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