Invariant Chain Controls the Activity of Extracellular Cathepsin L

@article{Fiebiger2002InvariantCC,
  title={Invariant Chain Controls the Activity of Extracellular Cathepsin L},
  author={Edda Fiebiger and Ren{\'e} Maehr and Jose A Villadangos and Ekkehard Weber and Ann E Erickson and Elizabeth K. Bikoff and Hidde L. Ploegh and Ana-Mar{\'i}a Lennon-Dum{\'e}nil},
  journal={The Journal of Experimental Medicine},
  year={2002},
  volume={196},
  pages={1263 - 1270}
}
Secretion of proteases is critical for degradation of the extracellular matrix during an inflammatory response. Cathepsin (Cat) S and L are the major elastinolytic cysteine proteases in mouse macrophages. A 65 amino acid segment of the p41 splice variant (p41(65aa)) of major histocompatibility complex class II-associated invariant chain (Ii) binds to the active site of CatL and permits the maintenance of a pool of mature enzyme in endosomal compartments of macro-phages and dendritic cells (DCs… CONTINUE READING

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