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Title: Cysteine cathepsin S processes leptin, inactivating its biological activity
Authors: Oliveira, Marcela [UNIFESP]
Assis, Diego M. [UNIFESP]
Paschoalin, Thaysa [UNIFESP]
Miranda, Antonio [UNIFESP]
Ribeiro, Eliane B. [UNIFESP]
Juliano, Maria A. [UNIFESP]
Broemme, Dieter
Christoffolete, Marcelo Augusto
Barros, Nilana M. T. [UNIFESP]
Carmona, Adriana K. [UNIFESP]
Universidade Federal de São Paulo (UNIFESP)
Univ British Columbia
Universidade Federal do ABC (UFABC)
Issue Date: 1-Aug-2012
Publisher: Bioscientifica Ltd
Citation: Journal of Endocrinology. Bristol: Bioscientifica Ltd, v. 214, n. 2, p. 217-224, 2012.
Abstract: Leptin is a 16 kDa hormone mainly produced by adipocytes that plays an important role in many biological events including the regulation of appetite and energy balance, atherosclerosis, osteogenesis, angiogenesis, the immune response, and inflammation. the search for proteolytic enzymes capable of processing leptin prompted us to investigate the action of cysteine cathepsins on human leptin degradation. in this study, we observed high cysteine peptidase expression and hydrolytic activity in white adipose tissue (WAT), which was capable of degrading leptin. Considering these results, we investigated whether recombinant human cysteine cathepsins B, K, L, and S were able to degrade human leptin. Mass spectrometry analysis revealed that among the tested enzymes, cathepsin S exhibited the highest catalytic activity on leptin. Furthermore, using a Matrigel assay, we observed that the leptin fragments generated by cathepsin S digestion did not exhibit angiogenic action on endothelial cells and were unable to inhibit food intake in Wistar rats after intracerebroventricular administration. Taken together, these results suggest that cysteine cathepsins may be putative leptin activity regulators in WAT. Journal of Endocrinology (2012) 214, 217-224
ISSN: 0022-0795
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