http://hdl.handle.net/2042/15655 2017-07-09T17:52:37Z 2017-07-09T17:52:37Z http://hdl.handle.net/2042/62329 2017-06-28T13:21:29Z 2017-06-28T00:00:00Z

Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2015, n°9 - Full issue

2017-06-28T00:00:00Z Francesco, Cappello de Macario Everly, Conway Alberto, JL. Macario http://hdl.handle.net/2042/62324 2017-06-29T09:19:21Z 2015-01-01T00:00:00Z

HSPD1 (Heat Shock 60kDa Protein 1) Francesco, Cappello; de Macario Everly, Conway; Alberto, JL. Macario The HSPD1 gene encodes a protein known as HSP60 or Hsp60, also commonly referred to as Cpn60. This protein is a molecular chaperone typically localized inside mitochondria where it forms a chaperoning machine with HSP10 (encoded by the HSPE1 gene), also called Cpn10, to assist protein folding inside the organelle. Hsp60 also occurs in the cytosol, plasma-cell membrane, intercellular space, and blood. Its functions in all these extramitochondrial locations are poorly understood. While the canonical functions of Hsp60 are considered to be cytoprotective, anti-stress and maintenance of protein homeostasis, other roles are currently being investigated. For example, Hsp60 participates in the pathogenesis of diseases in various ways in certain types of cancer, and chronic inflammatory and autoimmune pathological conditions. These are considered chaperonopathies by mistake, in which a normal chaperone (normal at least as far as it can be determined by current methods to study the structure of a molecule available only at extremely low concentrations and quantities) turns against the organism instead of protecting it, favouring the growth and dissemination of cancer cells, or the initiation-progression of inflammation, for instance. In addition, Hsp60 mutations cause at least two types of severe genetic chaperonopathies. All this knowledge is expanding nowadays clearly pointing to Hsp60 as a potential target for chaperonotherapy by replacement when it is defective or by inhibition when it is pathogenic.

2015-01-01T00:00:00Z Boudjadi, Salah Beaulieu, Jean-François http://hdl.handle.net/2042/62325 2017-06-29T09:22:11Z 2015-01-01T00:00:00Z

ITGA1 (integrin, alpha 1) Boudjadi, Salah; Beaulieu, Jean-François The α1 integrin subunit (SU) belongs to a large family of α and β subunits that are noncovalently linked to constitute αβ transmembrane units. To date, 18 α and 8 β subunits are known to form 24 αβ units (Takada et al., 2007; Barczyk et al., 2010) which are involved in cell-cell and cell-matrix attachment and can drive inside-out and outside-in cell signaling (Shattil et al., 2010). Integrins are known to participate in different cell processes including cell shape, differentiation, migration, survival and proliferation (Giancotti, 1997; Vachon, 2011; Beauséjour et al., 2012). The &alpha ;1 SU was discovered in 1986 as the Very Late Antigen 1 (VLA1) and is highly expressed in activated lymphocytes in the joints of patients with rheumatoid arthritis (Hemler et al., 1986). In fibroblasts, α1 is known to activate the RAS/ERK proliferative pathway and has a pro-invasive function in certain cancers. In megakaryocyte differentiation α1 is silenced by DNA methylation but not histone modification (Cheli et al., 2007). Different transcription factors involved in cancer progression can bind to the ITGA1 promoter. Integrin α1 transcriptional regulation remains to be further defined.

2015-01-01T00:00:00Z De Braekeleer, Etienne Douet-Guilbert, Nathalie Le Bris, Marie-José Basinko, Audrey Morel, Frédéric http://hdl.handle.net/2042/62326 2017-06-29T09:22:34Z 2015-01-01T00:00:00Z

inv(3)(q21q26) RPN1/MECOM De Braekeleer, Etienne; Douet-Guilbert, Nathalie; Le Bris, Marie-José; Basinko, Audrey; Morel, Frédéric review on inv(3)(q21q26) RPN1/MECOM

2015-01-01T00:00:00Z