Lipides, Nutrition, Cancer
Vendredi 8 Février 2013 à 14h00
Amphi Masson (faculté de médecine et de Pharmacie)
"Biological functions of HSP110 family members"
Heat shock proteins (HSPs) are the major components of molecular chaperones that facilitate the folding of newly synthesized proteins and prevent the aggregation of misfolded proteins. We are interested with biological functions of HSP110 family members, which act as a nucleotide exchange factor of HSP70 chaperone. In my seminar, I will represent our data about the targeted deletion of HSPA4, HSPA4L and HSPH1 gene in mice. Loss of HSPA4 resulted in development of cardiac hypertrophy and fibrosis. Our results suggest that the myocardial remodeling in Hspa4-deficient mice is due to accumulation of misfolded proteins resulting from impaired chaperone activity. Furthermore, I will illustrate the consequence of dual deletion of HSPA4 und HSPA4L on impaired maturation of alveolar epithelium in fetal lung.
Mohamed BA, Barakat AZ, Zimmermann WH, Bittner RE, Muhlfeld C, Hunlich M, Engel W, Maier LS, Adham IM. Targeted disruption of Hspa4 gene leads to cardiac hypertrophy and fibrosis. J Mol Cell Cardiol. 2012 Oct;53(4):459-68.
Yang K, Meinhardt A, Zhang B, Grzmil P, Adham IM, Hoyer-Fender S. The small heat shock protein ODF1/HSPB10 is essential for tight linkage of sperm head to tail and male fertility in mice. Mol Cell Biol. 2012 Jan;32(1):216-25.
Held T, Barakat AZ, Mohamed BA, Paprotta I, Meinhardt A, Engel W, Adham IM. Heat-shock protein HSPA4 is required for progression of spermatogenesis. Reproduction. 2011 Jul;142(1):133-44.
Held T, Paprotta I, Khulan J, Hemmerlein B, Binder L, Wolf S, Schubert S, Meinhardt A, Engel W, Adham IM. Hspa4l-deficient mice display increased incidence of male infertility and hydronephrosis development. Mol Cell Biol. 2006 Nov;26(21):8099-108.
Invitation: Carmen Garrido UMR866
Le séminaire aura lieu à la Faculté de Médecine Dijon
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