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Literature summary for 3.4.22.15 extracted from

  • Abboud-Jarrous, G.; Atzmon, R.; Peretz, T.; Palermo, C.; Gadea, B.B.; Joyce, J.A.; Vlodavsky, I.
    Cathepsin L is responsible for processing and activation of proheparanase through multiple cleavages of a linker segment (2008), J. Biol. Chem., 283, 18167-18176.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information knock-down of cathepsin L by siRNA results in a marked decrease in the level of the processed form of heparanase by 65%. Cathepsin L knock-out fibroblasts express high levels of the full-length 65-kDa proheparanase and display almost no heparanase enzymatic activity Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
proheparanase + H2O Bos taurus removal of the linker peptide and conversion of proheparanase into its active 8 + 50-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L active form of heparanase + ?
-
?
proheparanase + H2O Homo sapiens removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L active form of heparanase + ?
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
corneal endothelium
-
Bos taurus
-
JAR cell choriocarcinoma cell Homo sapiens
-
MCF-7 cell
-
Homo sapiens
-
MDA-MB-435 cell
-
Homo sapiens
-
RT-2 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
proheparanase + H2O removal of the linker peptide and conversion of proheparanase into its active 8 + 50-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L Bos taurus active form of heparanase + ?
-
?
proheparanase + H2O removal of the linker peptide and conversion of proheparanase into its active 850-kDa form is brought about predominantly by cathepsin L. Excision of a 10-amino acid peptide located at the C terminus of the linker segment between two functional cathepsin L cleavage sites at Y156Q and Y146Q is critical for activation of proheparanase. The entire linker segment of proheparanase is susceptible to multiple endocleavages by cathepsin L, generating small peptides. Processing and activation of proheparanase can be brought about solely by cathepsin L Homo sapiens active form of heparanase + ?
-
?