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A 9-kDa matricellular SPARC fragment released by cathepsin D exhibits pro-tumor activity in the triple-negative breast cancer microenvironment

Lindsay B. Alcaraz, Aude Mallavialle, Timothée David, Danielle Derocq, Frédéric Delolme, Cindy Dieryckx, Caroline Mollévi, Florence Boissière‐Michot, Joëlle Simony-Lafontaine, Stanislas du Manoir, Pitter F. Huesgen, Christopher M. Overall, Sophie Tartare‐Deckert, William Jacot, Thierry Chardès, Séverine Guiu, Pascal Roger, Thomas Reinheckel, Catherine Moali, Emmanuelle Liaudet‐Coopman

2021Theranostics57 citationsDOIOpen Access PDF

Abstract

Our study establishes a novel crosstalk between proteases and matricellular proteins in the tumor microenvironment through limited SPARC proteolysis, revealing a novel targetable 9-kDa bioactive SPARC fragment for new TNBC treatments. Our study will pave the way for the development of strategies for targeting bioactive fragments from matricellular proteins in TNBC.

Topics & Concepts

Triple-negative breast cancerMatricellular proteinCathepsin DCancer researchCancerMedicineBreast cancerChemistryInternal medicineBiologyCell biologyExtracellular matrixBiochemistryEnzymeBone and Dental Protein StudiesOral and Maxillofacial PathologyOral microbiology and periodontitis research
A 9-kDa matricellular SPARC fragment released by cathepsin D exhibits pro-tumor activity in the triple-negative breast cancer microenvironment | Litcius