scholarly journals Cathepsin B-like Cysteine Proteases Confer Intestinal Cysteine Protease Activity inHaemonchus contortus

2000 ◽  
Vol 276 (4) ◽  
pp. 2928-2934 ◽  
Author(s):  
Sankale Shompole ◽  
Douglas P. Jasmer
Keyword(s):  
Cysteine Protease ◽  
Cathepsin B ◽  
Protease Activity ◽  
Cysteine Proteases ◽  
Cysteine Protease Activity

Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease

2005 ◽  
Vol 386 (9) ◽  
Author(s):  
Vivian Hook ◽  
Thomas Toneff ◽  
Matthew Bogyo ◽  
Doron Greenbaum ◽  
Katalin F. Medzihradszky ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cysteine Protease ◽  
Cathepsin B ◽  
Protease Activity ◽  
Chromaffin Cells ◽  
Secretory Pathway ◽  
Secretory Vesicles ◽  
Cysteine Protease Activity ◽  
Regulated Secretory Pathway

AbstractThe regulated secretory pathway of neurons is the major source of extracellular Aβ that accumulates in Alzheimer's disease (AD). Extracellular Aβ secreted from that pathway is generated by β-secretase processing of amyloid precursor protein (APP). Previously, cysteine protease activity was demonstrated as the major β-secretase activity in regulated secretory vesicles of neuronal chromaffin cells. In this study, the representative cysteine protease activity in these secretory vesicles was purified and identified as cathepsin B by peptide sequencing. Immunoelectron microscopy demonstrated colocalization of cathepsin B with Aβ in these vesicles. The selective cathepsin B inhibitor, CA074, blocked the conversion of endogenous APP to Aβ in isolated regulated secretory vesicles. In chromaffin cells, CA074Me (a cell permeable form of CA074) reduced by about 50% the extracellular Aβ released by the regulated secretory pathway, but CA074Me had no effect on Aβ released by the constitutive pathway. Furthermore, CA074Me inhibited processing of APP into the COOH-terminal β-secretase-like cleavage product. These results provide evidence for cathepsin B as a candidate β-secretase in regulated secretory vesicles of neuronal chromaffin cells. These findings implicate cathepsin B as β-secretase in the regulated secretory pathway of brain neurons, suggesting that inhibitors of cathepsin B may be considered as therapeutic agents to reduce Aβ in AD.

scholarly journals Cysteine protease activity in the wall of abdominal aortic aneurysms

2007 ◽  
Vol 46 (6) ◽  
pp. 1260-1266 ◽  
Author(s):  
Said Abisi ◽  
Kevin G. Burnand ◽  
Matthew Waltham ◽  
Julia Humphries ◽  
Peter R. Taylor ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Abdominal Aortic Aneurysms ◽  
Aortic Aneurysms ◽  
Cysteine Protease Activity ◽  
Abdominal Aortic

scholarly journals The M Protein Is Dispensable for Maturation of Streptococcal Cysteine Protease SpeB

2005 ◽  
Vol 73 (2) ◽  
pp. 859-864 ◽  
Author(s):  
Björn Zimmerlein ◽  
Hae-Sun Park ◽  
Shaoying Li ◽  
Andreas Podbielski ◽  
P. Patrick Cleary
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Active Form ◽  
Surface Protein ◽  
M Protein ◽  
Cysteine Protease Activity ◽  
Group A ◽  
Streptococcal Pyrogenic Exotoxin B ◽  
Major Surface ◽  
Culture Supernatants

ABSTRACT The streptococcal pyrogenic exotoxin B (SpeB) is an important virulence factor of group A streptococci (GAS) with cysteine protease activity. Maturation of SpeB to a proteolytically active form was suggested to be dependent on cell-wall-anchored M1 protein, the major surface protein of GAS (M. Collin and A. Olsén, Mol. Microbiol. 36:1306-1318, 2000). Collin and Olsén showed that mutant GAS strains expressing truncated M protein secrete a conformationally different form of unprocessed SpeB with no proteolytic activity. Alternatively, we hypothesized that a truncated M protein may interfere with processing of this secreted protease, and therefore we tested cysteine protease activity in genetically defined mutant strains that express either no M protein or membrane-anchored M protein with an in-frame deletion of the AB repeat region. Measurements of SpeB activity by cleavage of a substrate n-benzoyl-Pro-Phe-Arg-p-nitroanilide hydrochloride showed that the proteolytic activities in culture supernatants of both mutants were similar to those from the wild-type strain. In addition, Western blot analysis of culture supernatants showed that SpeB expression and processing to a mature form was unaffected by either deletion mutation. Therefore, we conclude that M protein is not required for maturation of the streptococcal cysteine protease SpeB.

scholarly journals Epicutaneous Administration of Papain Induces IgE and IgG Responses in a Cysteine Protease Activity-Dependent Manner

2014 ◽  
Vol 63 (2) ◽  
pp. 219-226 ◽  
Author(s):  
Hideo Iida ◽  
Toshiro Takai ◽  
Yusuke Hirasawa ◽  
Seiji Kamijo ◽  
Sakiko Shimura ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Dependent Manner ◽  
Cysteine Protease Activity ◽  
Activity Dependent

Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes

2007 ◽  
Vol 3 (10) ◽  
pp. 668-677 ◽  
Author(s):  
Galia Blum ◽  
Georges von Degenfeld ◽  
Milton J Merchant ◽  
Helen M Blau ◽  
Matthew Bogyo
Keyword(s):  
Optical Imaging ◽  
Cysteine Protease ◽  
Protease Activity ◽  
Cysteine Protease Activity
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