Cathepsin L Plays an Important Role in the Lysosomal Degradation of L-Lactate Dehydrogenase

  title={Cathepsin L Plays an Important Role in the Lysosomal Degradation of L-Lactate Dehydrogenase},
  author={Takeyuki Ohshita and Yuzo Hiroi},
  journal={Bioscience, Biotechnology, and Biochemistry},
  pages={2254 - 2261}
  • T. OhshitaY. Hiroi
  • Published 23 September 2006
  • Biology, Chemistry
  • Bioscience, Biotechnology, and Biochemistry
A cystatin α-sensitive cysteine proteinase that plays an important role in the lysosomal inactivation and degradation of L-lactate dehydrogenase (LDH) was purified by column chromatography from an ammonium sulfate precipitate of lysosome extract prepared from rat livers. It was eluted with marked delay from cathepsins B and H in a Sephacryl S-200 column by its specific interaction with the gel, and then effectively separated from cathepsins B and H and other proteins. It was eluted with 0.5 M… 

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Involvement of a cystatin-alpha-sensitive cysteine proteinase in the degradation of native L-lactate dehydrogenase and serum albumin by rat liver or kidney lysosomes.

It is concluded that a cystatin-alpha-sensitive cysteine proteinase, other than cathepsins B, H, L and J, is present in lysosomes and functions in the lysOSomal degradation of at least native L-lactate dehydrogenase and serum albumin.

Native and Acid-denatured L-Lactate Dehydrogenase Are Different in the Lysosomal Proteinases Involving in Their Overall Degradation

  • T. Ohshita
  • Biology, Chemistry
    Bioscience, biotechnology, and biochemistry
  • 2000
It was concluded that a role of a cystatin α-sensitive cysteine proteinase is critical in the lysosomal degradation of native LDH, but not in that of acid-denatured form.

Purification and properties of a new cathepsin from rat liver.

A lysosomal protease, a new cathepsin that inactivates glucose-6-phosphate dehydrogenase, was purified about 2,200-fold from crude extracts of rat liver by cell-fractionation, freezing and thawing, acetone treatment, gel filtration, and DEAE SephadeX and CM-Sephadex column chromatographies.

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Cathepsin J showed strong affinity for synthetic substrates such as N-benzyloxycarbonyl-phenylalanyl-arginine 4-methyl-coumaryl-7-amide and glycyl-argInine beta-naphthylamide and antiserum against rat liver cathepsins B and L reacted with rat livercathepsIn J, suggesting that cathePSin J is identical with cat hepsin C.

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Effects of selective inhibition of cathepsin B and general inhibition of cysteine proteinases on lysosomal proteolysis in rat liver in vivo and in vitro.

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