Cathepsin Q, a Novel Lysosomal Cysteine Protease Highly Expressed in Placenta

2000 ◽  
Vol 267 (3) ◽  
pp. 791-795 ◽  
Author(s):  
Katia Sol-Church ◽  
Jennifer Frenck ◽  
Robert W. Mason
Keyword(s):  
Cysteine Protease ◽  
Lysosomal Cysteine Protease

Immunohistochemical localization of lysosomal cysteine protease cathepsins B and L in monkey hippocampal neurons after transient ischemia

1999 ◽  
Vol 19 (3) ◽  
pp. 302-310
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Hippocampal Neurons ◽  
Immunohistochemical Localization ◽  
Transient Ischemia ◽  
Lysosomal Cysteine Protease

scholarly journals Mammalian legumain – A lysosomal cysteine protease with extracellular functions?

Biochimie ◽  
2019 ◽  
Vol 166 ◽  
pp. 77-83 ◽  
Author(s):  
Ngoc Nguyen Lunde ◽  
Tatjana Bosnjak ◽  
Rigmor Solberg ◽  
Harald Thidemann Johansen
Keyword(s):  
Cysteine Protease ◽  
Lysosomal Cysteine Protease

scholarly journals Lysosomal cysteine protease cathepsin S is involved in cancer cell motility by regulating store-operated Ca2+ entry

2019 ◽  
Vol 1866 (12) ◽  
pp. 118517 ◽  
Author(s):  
Hsiao-Han Lin ◽  
Szu-Jung Chen ◽  
Meng-Ru Shen ◽  
Yi-Ting Huang ◽  
Hsing-Pang Hsieh ◽  
...  
Keyword(s):  
Cell Motility ◽  
Cancer Cell ◽  
Cysteine Protease ◽  
Cathepsin S ◽  
Cancer Cell Motility ◽  
Lysosomal Cysteine Protease

scholarly journals Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2020 ◽  
Author(s):  
Patrick Johé ◽  
Elmar Jaenicke ◽  
Hannes Neuweiler ◽  
Tanja Schirmeister ◽  
Christian Kersten ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cysteine Protease ◽  
Cathepsin L ◽  
Salt Bridge ◽  
Correlation Spectroscopy ◽  
African Trypanosomes ◽  
Lysosomal Cysteine Protease ◽  
Control Switch ◽  
Α Helix ◽  
Dynamics Simulations

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease of T. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression of T. brucei rhodesiense pro-rhodesain in E. coli and determined its crystal structure. The trypanosomal pro-domain differs from non-parasitic pro-cathepsins by a unique, extended α-helix that blocks the active site and whose interactions resemble that of the antiprotozoal inhibitor K11777. Interdomain dynamics between pro- and core protease domain as observed by photoinduced electron transfer fluorescence correlation spectroscopy increase at low pH, where pro-rhodesain also undergoes autocleavage. Using the crystal structure, molecular dynamics simulations and mutagenesis, we identify a conserved interdomain salt bridge that prevents premature intramolecular cleavage at higher pH values and may thus present a control switch for the observed pH-sensitivity of pro-enzyme cleavage in (trypanosomal) CathL-like proteases.

Cathepsin B Stability, But Not Activity, Is Affected in Cysteine:Cystine Redox Buffers

2002 ◽  
Vol 383 (7-8) ◽  
pp. 1199-1204 ◽  
Author(s):  
C. S. Pillay ◽  
C. Dennison
Keyword(s):  
Redox Potential ◽  
Cysteine Protease ◽  
Cathepsin B ◽  
Reduction Potential ◽  
Potential Range ◽  
Neutral Ph ◽  
Lysosomal Cysteine Protease ◽  
The Stability ◽  
Redox Buffers

Abstract In order to test the hypothesis that the lysosomal cysteine protease cathepsin B may be redox regulated in vivo, cathepsin B activity and stability were measured in cysteine and/or cystinecontaining buffers. Cathepsin B activity in cysteinecontaining buffers was similar at pH 6.0 and pH 7.0, over all thiol concentrations tested. In contrast, the stability of the enzyme was greater at pH 6.0 than at pH 7.0. This suggests that the enzymes operational pH in vivo may be < pH 7.0. The activity of the enzyme was depressed in glutathionecontaining buffers. When assessed in cysteine:cystine redox buffers (pH 6.0 7.0) cathepsin B was active over a broad redox potential range, suggesting that cathepsin B activity may not be redox regulated. However, at pH 7.0, the stability of cathepsin B decreased with increasing reduction potential and ambient cystine concentration. This suggests that the stability of the enzyme at neutral pH is dependent on redox potential, and on the presence of oxidising agents.

Non-Lysosomal Cysteine Protease

2012 ◽  
pp. 1254-1254
Author(s):  
Rüdiger Horstkorte ◽  
Bettina Büttner ◽  
Kaya Bork ◽  
Navdeep Sahota ◽  
Sarah Sabir ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Lysosomal Cysteine Protease

Biosynthesis and Alternate Targeting of the Lysosomal Cysteine Protease Cathepsin L

2004 ◽  
pp. 1-51 ◽  
Author(s):  
John Collette ◽  
Jeffrey P. Bocock ◽  
Kyujeong Ahn ◽  
Richard L. Chapman ◽  
Gene Godbold ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Cathepsin L ◽  
Lysosomal Cysteine Protease
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