TITLE: Muscle-specific PPAR-gamma-deficient mice develop increased adiposity and insulin resistance but respond to thiazolidinediones
AUTHOR CONTACT:
C. Ronald Kahn
Joslin Diabetes Center, Boston, Massachusetts, USA.
Phone: (617) 732-2635
Fax: (617) 732-2487
E-mail: c.ronald.kahn@joslin.harvard.edu
View the PDF of this article at: https://www.the-jci.org/press/17305.pdf
A new cathepsin in the thymus
CD4 cells detect extracellular pathogens that have been processed and presented on the surface of MHC class II molecules. This presentation process requires the activity of lysosomal proteases such as the cathepsins, which degrade the MHC class II chaperone invariant chain to generate class IIassociated invariant chain peptides. Eva Tolosa and colleagues from Tbingen University Hospital, Germany, have now characterized the function of a new human cathepsin (Cathepsin V) exclusively expressed in the human thymus and testis. The authors show that Cathepsin V is the protease that mediates invariant chain release in the class II processing pathway in the human thymus. Comparison of Cathepsin V expression in thymi from myasthenia gravis patients and healthy controls revealed a significantly higher expression level in the pathological samples, suggesting a potential involvement of this protease in the immunopathogenesis of this disease.
TITLE: Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis
AUTHOR CONTACT:
Eva Tolosa
Tebingen University Hospital, Tebingen, Germany
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Contact: Brooke Grindlinger
science_editor@the-jci.org
212-342-9006
Journal of Clinical Investigation
15-Aug-2003