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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
Cathepsin L is a member of the papain superfamily of cysteine proteases and, like many other proteases, it is synthesized as an inactive proenzyme. Its prosegment shows little homology to that ofExpand
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Cathepsin B.
  • J. Mort, D. Buttle
  • Medicine
  • The international journal of biochemistry & cell…
  • 1997
Cathepsin B is a lysosomal cysteine protease of the papain family. It functions in intracellular protein catabolism and in certain situations may also be involved in other physiological processes,Expand
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Articular cartilage and changes in arthritis: Matrix degradation
While many proteases in articular cartilage have been described, current studies indicate that members of two families of metalloproteases – MMPs and the ADAMTSs – are responsible for the degradationExpand
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Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases.
The cathepsin L propeptide (phcl-2) was expressed in Saccharomyces cerevisiae using a human procathepsin L/alpha-factor fusion construct containing a stop codon at position -1 (the C-terminal aminoExpand
  • 185
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Role of the Occluding Loop in Cathepsin B Activity*
Within the lysosomal cysteine protease family, cathepsin B is unique due to its ability to act both as an endopeptidase and a peptidyldipeptidase. This latter capacity to remove C-terminal dipeptidesExpand
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Monoclonal antibodies that specifically recognize neoepitope sequences generated by 'aggrecanase' and matrix metalloproteinase cleavage of aggrecan: application to catabolism in situ and in vitro.
Monoclonal antibodies have been prepared that react specifically with the neoepitopes present on proteoglycan degradation products generated from the proteolytic cleavage of aggrecan in theExpand
  • 211
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Alarmins S100A8 and S100A9 elicit a catabolic effect in human osteoarthritic chondrocytes that is dependent on Toll-like receptor 4.
OBJECTIVE S100A8 and S100A9 are two Ca(2+) binding proteins classified as damage-associated molecular patterns or alarmins that are found in high amounts in the synovial fluid of osteoarthritis (OA)Expand
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The role of aggrecan in normal and osteoarthritic cartilage
Aggrecan is a large proteoglycan bearing numerous chondroitin sulfate and keratan sulfate chains that endow articular cartilage with its ability to withstand compressive loads. It is present in theExpand
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Cole-Carpenter syndrome is caused by a heterozygous missense mutation in P4HB.
Cole-Carpenter syndrome is a severe bone fragility disorder that is characterized by frequent fractures, craniosynostosis, ocular proptosis, hydrocephalus, and distinctive facial features. ToExpand
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MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein.
Aggrecan degradation in articular cartilage occurs predominantly through proteolysis and has been attributed to the action of members of the matrix metalloproteinase (MMP) and a disintegrin andExpand
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