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Cathepsin V Is Involved in the Degradation of Invariant Chain in Human Thymus and Is Overexpressed in Myasthenia Gravis

Cathepsin V Is Involved in the Degradation of Invariant Chain in Human Thymus and Is Overexpressed in Myasthenia Gravis

Eva Tolosa, Weijie Li, Yoshiyuki Yasuda, Wolfgang Wienhold, Lisa K Denzin, Alfred Lautwein, Christoph Driessen, Petra Schnorrer, Ekkehard Weber, Stefan Stevanovic, Raffael Kurek, Arthur Melms, Dieter Bromme

J Clin Invest. 2003 Aug;112(4):517-26.

PMID: 12925692

Abstract:

Stepwise degradation of the invariant chain (Ii) is required for the binding of antigenic peptides to MHC class II molecules. Cathepsin (Cat) L in the murine thymus and Cat S in peripheral APCs have both been implicated in the last step of Ii degradation that gives rise to the class II-associated invariant chain peptides (CLIP). Cat V has been recently described as highly homologous to Cat L and exclusively expressed in human thymus and testis, but with no mouse orthologue. We report that Cat V is the dominant cysteine protease in cortical human thymic epithelial cells, while Cat L and Cat S seem to be restricted to dendritic and macrophage-like cells. Active Cat V in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant Cat V was capable of converting Ii into CLIP efficiently, suggesting that Cat V is the protease that controls the generation of alphabeta-CLIP complexes in the human thymus, in analogy to Cat L in mouse. Comparison of Cat V expression between thymi from patients with myasthenia gravis and healthy controls revealed a significantly higher expression level in the pathological samples, suggesting a potential involvement of this protease in the immunopathogenesis of myasthenia gravis, an autoimmune disease almost invariably associated with thymic pathology.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42412612	Cathepsin V Active human			Price

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