The reactive site loop of the serpin SCCA1 is essential for cysteine proteinase inhibition
Schick, Charles, Brömme, Dieter, Bartuski, Allison J., Uemura, Yoshiki, Schechter, Norman M., Silverman, Gary A.
The high-molecular-weight serine proteinase inhibitors (serpins) are restricted, generally, to inhibiting proteinases of the serine mechanistic class. However, the viral serpin, cytokine response...
Tolosa, Eva, Li, Weijie, Yasuda, Yoshiyuki, Wienhold, Wolfgang, Denzin, Lisa K., Lautwein, Alfred, ...
Stepwise degradation of the invariant chain (Ii) is required for the binding of antigenic peptides to MHC class II molecules. Cathepsin (Cat) L in the murine thymus and Cat S in peripheral APCs have...
NF-κB protects from the lysosomal pathway of cell death
Liu, Ni, Raja, Srikumar M., Zazzeroni, Francesca, Metkar, Sunil S., Shah, Ramila, Zhang, Manling, ...
The programme of gene expression induced by RelA/NF-κB transcription factors is critical to the control of cell survival. Ligation of ‘death receptors’ such as tumor necrosis factor receptor 1...
Hou, Wu-Shiun, Brömme, Dieter, Zhao, Yingming, Mehler, Ernest, Dushey, Craig, Weinstein, Harel, ...
Cathepsin K, a lysosomal cysteine protease critical for bone remodeling by osteoclasts, was recently identified as the deficient enzyme causing pycnodysostosis, an autosomal recessive osteosclerotic...
Cathepsin K: a cysteine protease with unique kinin-degrading properties
Godat, Emmanuel, Lecaille, Fabien, Desmazes, Claire, Duchêne, Sophie, Weidauer, Enrico, Saftig, Paul, ...
Taking into account a previous report of an unidentified enzyme from macrophages acting as a kininase, the ability of cysteine proteases to degrade kinins has been investigated. Wild-type fibroblast...
Alves, Marcio F M, Puzer, Luciano, Cotrin, Simone S, Juliano, Maria Aparecida, Juliano, Luiz, Brömme, Dieter, ...
We have systematically examined the S3 to S3' subsite substrate specificity requirements of cathepsin K using internally quenched fluorescent peptides derived from the lead sequence Abz-KLRFSKQ-EDDnp...
Probing cathepsin K activity with a selective substrate spanning its active site.
Lecaille, Fabien, Weidauer, Enrico, Juliano, Maria A, Brömme, Dieter, Lalmanach, Gilles
The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine...
The reactive site loop of the serpin SCCA1 is essential for cysteine proteinase inhibition
Schick, Charles, Brömme, Dieter, Bartuski, Allison J., Uemura, Yoshiki, Schechter, Norman M., Silverman, Gary A.
The high-molecular-weight serine proteinase inhibitors (serpins) are restricted, generally, to inhibiting proteinases of the serine mechanistic class. However, the viral serpin, cytokine response...
Tolosa, Eva, Li, Weijie, Yasuda, Yoshiyuki, Wienhold, Wolfgang, Denzin, Lisa K., Lautwein, Alfred, ...
Stepwise degradation of the invariant chain (Ii) is required for the binding of antigenic peptides to MHC class II molecules. Cathepsin (Cat) L in the murine thymus and Cat S in peripheral APCs have...
NF-κB protects from the lysosomal pathway of cell death
Liu, Ni, Raja, Srikumar M., Zazzeroni, Francesca, Metkar, Sunil S., Shah, Ramila, Zhang, Manling, ...
The programme of gene expression induced by RelA/NF-κB transcription factors is critical to the control of cell survival. Ligation of ‘death receptors’ such as tumor necrosis factor receptor 1...
Hou, Wu-Shiun, Brömme, Dieter, Zhao, Yingming, Mehler, Ernest, Dushey, Craig, Weinstein, Harel, ...
Cathepsin K, a lysosomal cysteine protease critical for bone remodeling by osteoclasts, was recently identified as the deficient enzyme causing pycnodysostosis, an autosomal recessive osteosclerotic...
Cathepsin K: a cysteine protease with unique kinin-degrading properties
Godat, Emmanuel, Lecaille, Fabien, Desmazes, Claire, Duchêne, Sophie, Weidauer, Enrico, Saftig, Paul, ...
Taking into account a previous report of an unidentified enzyme from macrophages acting as a kininase, the ability of cysteine proteases to degrade kinins has been investigated. Wild-type fibroblast...
Alves, Marcio F M, Puzer, Luciano, Cotrin, Simone S, Juliano, Maria Aparecida, Juliano, Luiz, Brömme, Dieter, ...
We have systematically examined the S3 to S3' subsite substrate specificity requirements of cathepsin K using internally quenched fluorescent peptides derived from the lead sequence Abz-KLRFSKQ-EDDnp...
Probing cathepsin K activity with a selective substrate spanning its active site.
Lecaille, Fabien, Weidauer, Enrico, Juliano, Maria A, Brömme, Dieter, Lalmanach, Gilles
The limited availability of highly selective cathepsin substrates seriously impairs studies designed to monitor individual cathepsin activities in biological samples. Among mammalian cysteine...
Pivotal Role of Cathepsin K in Lung Fibrosis
Bühling, Frank, Röcken, Christoph, Brasch, Frank, Hartig, Roland, Yasuda, Yoshiyuki, Saftig, Paul, ...
The paramount importance of the homeostasis of the extracellular matrix for pulmonary function is exemplified by two opposing extremes: emphysema and pulmonary fibrosis. This study examined the...
A Putative Role for Cathepsin K in Degradation of AA and AL Amyloidosis
Röcken, Christoph, Stix, Barbara, Brömme, Dieter, Ansorge, Siegfried, Roessner, Albert, Bühling, Frank
The aims of this study were to investigate the role of cathepsin K in the pathology of amyloidosis by demonstrating its presence in multinucleated giant cells (MGCs) adjacent to amyloid deposits, and...
Cathepsin K Is a Critical Protease in Synovial Fibroblast-Mediated Collagen Degradation
Hou, Wu-Shiun, Li, Zhenqiang, Gordon, Ronald E., Chan, Kyle, Klein, Michael J., Levy, Roger, ...
Synovial fibroblasts (SFs) play a critical role in the pathogenesis of rheumatoid arthritis (RA) and are directly involved in joint destruction. Both SF-resident matrix metalloproteases and...
The S2 subsites of cathepsins K and L and their contribution to collagen degradation
Lecaille, Fabien, Chowdhury, Shafinaz, Purisima, Enrico, Brömme, Dieter, Lalmanach, Gilles
The exchange of residues 67 and 205 of the S2 pocket of human cysteine cathepsins K and L induces a permutation of their substrate specificity toward fluorogenic peptide substrates. While the...