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Jobs E, Riserus U, Ingelsson E et al (2013) Serum cathepsin S is associated with decreased insulin sensitivity and the development of diabetes type 2 in a community-based cohort of elderly men. Liu J, Ma L, Yang J et al (2006) Increased serum cathepsin S in patients with atherosclerosis and diabetes. Jobs E, Ingelsson E, Riserus U et al (2011) Association between serum cathepsin S and mortality in older adults. Rodgers KJ, Watkins DJ, Miller AL et al (2006) Destabilizing role of cathepsin S in murine atherosclerotic plaques. Sukhova GK, Zhang Y, Pan JH et al (2003) Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice. Sukhova GK, Shi GP, Simon DI et al (1998) Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. Ward C, Kuehn D, Burden RE et al (2010) Antibody targeting of cathepsin S inhibits angiogenesis and synergistically enhances anti-VEGF. J Biol Chem 281:6020–6029īurden RE, Gormley JA, Jaquin TJ et al (2009) Antibody-mediated inhibition of cathepsin S blocks colorectal tumor invasion and angiogenesis. Wang B, Sun J, Kitamoto S et al (2006) Cathepsin S controls angiogenesis and tumor growth via matrix-derived angiogenic factors. J Autoimmun 36:201–209ĭeschamps K, Cromlish W, Weicker S et al (2011) Genetic and pharmacological evaluation of cathepsin s in a mouse model of asthma. Expert Opin Ther Pat 21:311–337īaugh M, Black D, Westwood P et al (2011) Therapeutic dosing of an orally active, selective cathepsin S inhibitor suppresses disease in models of autoimmunity. Lee-Dutra A, Wiener DK, Sun S (2011) Cathepsin S inhibitors: 2004–2010. Palermo C, Joyce JA (2008) Cysteine cathepsin proteases as pharmacological targets in cancer. Saegusa K, Ishimaru N, Yanagi K et al (2002) Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity.
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Nakagawa TY, Brissette WH, Lira PD et al (1999) Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice.
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Shi GP, Villadangos JA, Dranoff G et al (1999) Cathepsin S required for normal MHC class II peptide loading and germinal center development. Riese RJ, Wolf PR, Bromme D et al (1996) Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Naour N, Rouault C, Fellahi S et al (2010) Cathepsins in human obesity: changes in energy balance predominantly affect cathepsin s in adipose tissue and in circulation. Taleb S, Cancello R, Poitou C et al (2006) Weight loss reduces adipose tissue cathepsin S and its circulating levels in morbidly obese women. Reiser J, Adair B, Reinheckel T (2010) Specialized roles for cysteine cathepsins in health and disease. Lecaille F, Kaleta J, Bromme D (2002) Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Taleb S, Lacasa D, Bastard JP et al (2005) Cathepsin S, a novel biomarker of adiposity: relevance to atherogenesis. CatS inhibitors currently proposed for treatment of autoimmune diseases could help to lower hepatic glucose output in obese individuals at risk for type 2 diabetes. Our results revealed an unexpected metabolic effect of CatS in promoting pro-diabetic alterations in the liver. Mechanistically, we found that the protein ‘regulated in development and DNA damage response 1’ (REDD1), a factor potentially implicated in reduction of respiratory chain activity, was overexpressed in the liver of mice with CatS deficiency. This phenotype relied on downregulation of gluconeogenic gene expression in liver and a lower rate of hepatocellular respiration. In vivo testing of glucose tolerance, insulin sensitivity and glycaemic response to gluconeogenic substrates revealed that CatS suppression reduced hepatic glucose production despite there being no improvement in insulin sensitivity. ResultsĬatS deletion induced a robust reduction in blood glucose, which was preserved in diet-induced obesity and with ageing and was recapitulated with CatS inhibition in obese mice. MethodsĬatS knockout mice and wild-type mice treated with orally active small-molecule CatS inhibitors were fed chow or high-fat diets and explored for change in glycaemic status. This prompted us to test whether the protease contributes to the pathogenesis of type 2 diabetes using mouse models with CatS inactivation. We previously identified CatS as a protein that is markedly overexpressed in adipose tissue of obese individuals and downregulated after weight loss and amelioration of glycaemic status induced by gastric bypass surgery. Cathepsin S (CatS) belongs to a family of proteases that have been implicated in several disease processes.