Substrate specificity of recombinant osteoclast-specific cathepsin K from rabbits.

@article{Aibe1996SubstrateSO,
  title={Substrate specificity of recombinant osteoclast-specific cathepsin K from rabbits.},
  author={K. Aibe and H. Yazawa and K. Abe and K. Teramura and M. Kumegawa and H. Kawashima and K. Honda},
  journal={Biological \& pharmaceutical bulletin},
  year={1996},
  volume={19 8},
  pages={
          1026-31
        }
}
A cDNA clone encoding the rabbit cysteine proteinase cathepsin K, which is predominantly expressed in osteoclasts and is closely related to cathepsins L (EC 3.4.22.15) and S (EC 3.4.22.27) [Tezuka K., Tezuka Y., Maejima A., Sato T., Nemoto K., Kamioka H., Hakeda Y., Kumegawa M., J. Biol. Chem., 269, 1106 (1994)], was expressed at high levels in Escherichia coli in a T7 expression system. The insoluble recombinant enzyme was solubilized in urea and refolded at an alkaline pH. Cathepsin K (37-kDa… Expand
Preparation of active recombinant cathepsin K expressed in bacteria as inclusion body.
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Recombinant human procathepsin K expressed in Escherichia coli had type I and II collagenolytic activities which could be inhibited by E-64 and the presence of pepsin or cysteine in autocatalysis buffer did not have effect on the degree of conversion of nascent to mature cathepsins K. Expand
Detection of femtomole quantities of mature cathepsin K with zymography.
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This inexpensive, species-independent, antibody-free protocol describes a sensitive method with broad potential to elucidate previously undetectable cathepsin K activity. Expand
Biochemical properties and regulation of cathepsin K activity.
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This review focuses on the current knowledge of cathepsin K, the major bone cysteine protease, which is a drug target of clinical interest and the kinetic data of its inhibition by natural endogenous inhibitors, and its putative roles in physiological or pathophysiological processes. Expand
Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin.
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It is postulate that its localization enables cathepsin K to contribute to the extracellular proteolysis of thyroglobulin, i.e. thyroid hormone liberation, at the apical surface of thyroid epithelial cells in situ. Expand
Molecular cloning, expression analysis and enzymatic characterization of cathepsin K from olive flounder (Paralichthys olivaceus).
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  • Biology, Medicine
  • Comparative biochemistry and physiology. Part A, Molecular & integrative physiology
  • 2009
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The data indicate that cathepsin K may play a role in the immune system of fish skin and muscle, in addition to its principal bone-specific function as a collagenolytic enzyme. Expand
Human Osteoclast Cathepsin K Is Processed Intracellularly Prior to Attachment and Bone Resorption
  • R. Dodds, I. James, +9 authors M. Gowen
  • Medicine, Biology
  • Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research
  • 2001
TLDR
The results suggest that the in vivo activation of cathepsin K occurs intracellularly, before secretion into the resorption lacunae and the onset of bone resOrption, suggesting that local factors may regulate this process. Expand
Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis.
TLDR
These studies demonstrated the molecular heterogeneity of mutations causing pycnodysostosis, indicated that pro region conformation directs proper folding of the proenzyme, and suggested that the cathepsin K active site contains a critical collagen-binding domain. Expand
S3 to S3' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates.
TLDR
The results indicated that the S3-S1 subsite requirements are more restricted than those of S1'-S3' and cathepsin K preferentially accommodates hydrophobic amino acids with aliphatic side chains in the S2 site. Expand
Proteolysis of human bone collagen by cathepsin K: characterization of the cleavage sites generating by cross-linked N-telopeptide neoepitope.
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It is shown that recombinant human cathepsin K is highly active in releasing the NTx neoepitope in 100% yield from bone type I collagen. Expand
A cytochemical assay for osteoclast cathepsin K activity
  • R. Dodds
  • Chemistry, Medicine
  • Cell biochemistry and function
  • 2003
TLDR
A cytochemical assay is described that localizes osteoclast cathepsin K activity in unfixed, undecalcified cryostat sections of animal and human bone and could be used to identify and analyse osteoclasts at definitive stages of their lifespan. Expand
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