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cysteine protease, asparaginyl endopeptidase
This gene encodes a cysteine protease that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme may be involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Enzyme activation is triggered by acidic pH and appears to be autocatalytic. Protein expression occurs after monocytes differentiate into dendritic cells. A fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with the majority of solid tumor types. This gene has a pseudogene on chromosome 13. Several alternatively spliced transcript variants have been described, but the biological validity of only two has been determined. These two variants encode the same isoform. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on cysteine protease
Legumain: a biomarker for diagnosis and prognosis of human ovarian cancer.
Xiang et al., Tianjin, China. In J Cell Biochem, 2012
Increased legumain expression was validated by real-time PCR and Western blots, correlated positively with an increased malignancy of ovarian tumors.
Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile.
Brandstetter et al., Salzburg, Austria. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
Accepting asparagines and, to lesser extent, aspartic acid in P1, super-activated legumain exhibits a marked pH dependence that is governed by the P1 residue of its substrate and conformationally stabilizing factors such as temperature or ligands
RAC2, AEP, and ICAM1 expression are associated with CNS disease in a mouse model of pre-B childhood acute lymphoblastic leukemia.
Saha et al., Manchester, United Kingdom. In Blood, 2011
We identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion molecule 1 (ICAM1), and ras-related C3 botulinum toxin substrate 2 (RAC2), among others, in an invasive pre-B-cell line that produced leukemia in NOD-SCID mice
Asparagine endopeptidase is required for normal kidney physiology and homeostasis.
Watts et al., Dundee, United Kingdom. In Faseb J, 2011
AEP is required for normal protein catabolism by PTCs, and its loss induces proliferative and other abnormalities in the murine kidney, at least in part through defective regulation of the EGF receptor
Expression of phosphatidylserine-specific phospholipase A(1) mRNA in human THP-1-derived macrophages.
Kohda et al., Japan. In Cell Transplant, 2009
These results suggest that the expression of PS-PLA(1) mRNA in THP-1-derived macrophages is activated via TLR4.
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