StarD7 knockdown leads to α5β1 integrin upregulation and Golgi fragmentation in HTR8/SVNEO cells

MARIANO CURZ DEL PUERTO; JÉSICA FLORES-MARTIN; LUCIANA REYNA; GRACIELA PANZETTA DE DUTARI; SUSANA GENTI-RAIMONDI

Córdoba

Congreso; LII Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2016

Cruz Del Puerto MM, Flores-Martín J, Reyna L; Panzetta-Dutari GM, Genti-Raimondi S.Dpto. Bioquímica Clínica, Facultad de Ciencias Químicas-UNC. CIBICI-CONICET. Argentina. E-mail: mdelpuertoi@fcq.unc.edu.ar.StarD7 belongs to START domain protein family, which is involved in lipid transport, metabolism and signaling. Preliminary resultsindicate that StarD7 silencing induces a decrease in HTR8/SVneo cell migration measured by wound healing assay. To address themechanism implicated in this process the levels of α5 and β1 integrin subunits, p-FAK as well as β-catenin proteins were measured inHTR8/SVneo transfected with StarD7 siRNA for 72 h. Surprisingly, a significant increase in the mRNA, and protein levels of α5integrin in silenced cells were determined by qRT-PCR, western blot and immunofluorescence assays. Also, a clear increase in thetranscript level of β1 integrin, as well as in the β1 mature protein was detected. In addition, StarD7 silencing leads to an increase in pFAKand β-catenin protein levels, whereas a decrease in the level of MMP2 secreted to the culture medium was established in StarD7siRNA cells. Since it is widely accepted that Golgi apparatus regulates directional cell migration we analyzed its integrity.Immunofluorescence assay usinganti-GM130 revealed that StarD7 knockdown induced Golgi apparatus fragmentation. In summary,our results suggest that StarD7 depletion causes a dysregulation in several molecules as well as in Golgi apparatus, which are involvedin maintaining cellular migration.