A5036595403- Protease and Inhibitor Mechanisms
- Cell Adhesion Molecules Research
- Fibroblast Growth Factor Research
- Glycosylation and Glycoproteins Research
- Peptidase Inhibition and Analysis
- Cell death mechanisms and regulation
- Monoclonal and Polyclonal Antibodies Research
- Bone and Dental Protein Studies
- Cancer, Hypoxia, and Metabolism
- Cellular transport and secretion
- Ubiquitin and proteasome pathways
- HER2/EGFR in Cancer Research
- Retinoids in leukemia and cellular processes
- Epigenetics and DNA Methylation
- Cancer Cells and Metastasis
- Calpain Protease Function and Regulation
- Oral microbiology and periodontitis research
- Chemokine receptors and signaling
- Immunotherapy and Immune Responses
- Adipokines, Inflammation, and Metabolic Diseases
- Kruppel-like factors research
- Angiogenesis and VEGF in Cancer
- Advanced biosensing and bioanalysis techniques
- NF-κB Signaling Pathways
- Bone health and treatments
Inserm
2012-2025
Université de Montpellier
2012-2025
Institut de Recherche en Cancérologie de Montpellier
2012-2025
Institut Regional du Cancer de Montpellier
2014-2015
Institut National de Recherche en Santé Publique
2014
CEA Valduc
2010-2011
Georgetown University
1996-2001
Georgetown University Medical Center
1996-2000
University of Washington
1998
Journal Article Processing of Human Cathepsin D Is Independent Its Catalytic Function and Auto-Activation: Involvement Cathepsins L B Get access Valérie Laurent-Matha, Laurent-Matha ‡To whom correspondence should be addressed. E Liaudet-Coopman, Inserm U540, 'Molecular Cellular Endocrinology Cancers,' 60 rue de Navacelles, 34090 Montpellier, France. Tel: +33 4 67 04 30 80, Fax: 54 05 98, E-mail:liaudet@montp.inserm.fr Search for other works by this author on: Oxford Academic PubMed Google...
Significance Autophagy allows the lysosomal degradation of intracellular material. It is a tightly regulated process controlled by tumor-suppressor gene p53, among others. Here we report unique regulator autophagy, BAT3, which modulates localization enzyme p300, an that adds some acetyl residues on targets proteins (acetylation) to modulate their activity. To stimulate BAT3 acetylation p53 p300 in nucleus, but limits p300-dependent ATG7, protein specific for cytosol. Thus, acts both cytosol...
Triple-negative breast cancer (TNBC) treatment is currently restricted to chemotherapy. Hence, tumor-specific molecular targets and/or alternative therapeutic strategies for TNBC are urgently needed. Immunotherapy emerging as an exciting option patients. The aspartic protease cathepsin D (cath-D), a marker of poor prognosis in (BC), overproduced and hypersecreted by human BC cells. This study explores whether cath-D tumor cell-associated extracellular biomarker potent target antibody-based...
The aspartyl-protease cathepsin D (cath-D) is overexpressed and hypersecreted by epithelial breast cancer cells stimulates their proliferation. As tumor epithelial–fibroblast cell interactions are important events in progression, we investigated whether cath-D overexpression affects also fibroblast behavior. We demonstrate a requirement of for invasive growth using three-dimensional (3D) coculture assay with secreting or not pro-cath-D. Ectopic expression cath-D–deficient fibroblasts 3D...
The aspartic protease cathepsin D, a poor prognostic indicator of breast cancer, is abundantly secreted as procathepsin D by human cancer cells and self-activates at low pH in vitro, giving rise to catalytically active D. Due lower extracellular tumor microenvironments compared normal tissues, may cleave pathophysiological substrates contributing progression. Here, we show yeast 2-hybrid degradomics analyses that cystatin C, the most potent natural inhibitor cysteine cathepsins, both binds...
Introduction Triple-negative breast cancer (TNBC) prognosis is poor. Immunotherapies to enhance the antibody-induced natural killer (NK) cell antitumor activity are emerging for TNBC that frequently immunogenic. The aspartic protease cathepsin D (cath-D), a tumor cell-associated extracellular protein with protumor and poor marker in TNBC, prime target antibody-based therapy induce NK cell-mediated antibody-dependent cellular cytotoxicity (ADCC). This study investigated whether Fc-engineered...
The cell surface low-density lipoprotein receptor-related protein 1, LRP1, plays a major role in lipid metabolism. question that remains open concerns the function of LRP1 adipogenesis. Here, we show is highly expressed murine preadipocytes as well primary culture human adipocytes. Moreover, abundantly synthesised during mouse and adipocyte differentiation. We demonstrate silencing 3T3F442A significantly inhibits expression PPARγ, HSL aP2 differentiation markers after adipogenesis induction,...
The aspartic protease cathepsin-D (cath-D) is overexpressed by human epithelial breast cancer cells and closely correlated with poor prognosis in cancer. adipocyte one of the most prominent cell types tumor-microenvironment cancer, clinical studies have shown that obesity increases incidence Here, we provide first evidence cath-D expression up-regulated adipose tissue from obese beings, as well adipocytes C57BI6/J mouse. Cath-D also increased during mouse differentiation. We show silencing...
Interactions between cancer cells and fibroblasts are crucial in progression. We have previously shown that the aspartic protease cathepsin D (cath-D), a marker of poor prognosis breast is overexpressed highly secreted by cells, triggers mouse embryonic fibroblast outgrowth via paracrine loop. Here, we show requirement cath-D for human mammary using three-dimensional co-culture assay with do or not secrete pro-cath-D. Interestingly, proteolytically-inactive pro-cath-D remains mitogenic,...
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The lysosomal protease cathepsin D (Cath-D) is overproduced in breast cancer cells (BCC) and supports tumor growth metastasis formation. Here, we describe the mechanism whereby Cath-D accumulated nucleus of ERα-positive (ER+) BCC. We identified TRPS1 (tricho-rhino-phalangeal-syndrome 1), a repressor GATA-mediated transcription, BAT3 (Scythe/BAG6), nucleo-cytoplasmic shuttling chaperone protein, as new Cath-D-interacting nuclear proteins. binds to ER+ BCC they partially co-localize at surface...