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Literature summary for 3.4.22.15 extracted from

  • Klein, D.M.; Felsenstein, K.M.; Brenneman, D.E.
    Cathepsins B and L differentially regulate amyloid precursor protein processing (2009), J. Pharmacol. Exp. Ther., 328, 813-821.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides ?
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
hippocampus in primary hippocampal neuron, pharmacological inhibition of cathepsin L selectively elevates amyloid precursor protein Abeta42 levels but not Abeta40 or total Abeta Mus musculus
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Neuro-2a cell neuroblastoma cell Mus musculus
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neuron in primary hippocampal neuron, pharmacological inhibition of cathepsin L selectively elevates amyloid precursor protein Abeta42 levels but not Abeta40 or total Abeta Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cathepsin L elevates alpha-secretase activity, thereby suppressing amyloid precursor protein Abeta42 level. Cathepsin L reduces the formation of Abeta42 peptides by cleaving amyloid precursor protein within the Abeta peptide sequence. In addition, both cathepsins B and L degrade Abeta42 into less toxic Abeta peptides Mus musculus ?
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