GENTI DE RAIMONDI SUSANA DEL VALLE
Congresos y reuniones científicas
Título:
StarD7 is a fusogenic protein that binds cardiolipin and phosphatidylserine
Autor/es:
ANGELETTI SOFÍA; CHEN Q; CHAMLEY L; RENA VIVIANA; PANZETTA-DUTARI GRACIELA; GENTI DE RAIMONDI SUSANA
Lugar:
San Miguel de Tucumán, Tucumán
Reunión:
Congreso; XLV Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2009
Institución organizadora:
SAIB
Resumen:
START lipid domain family. It was previously found that StarD7 is
able to interact in lipid monolayers with phosphatidylserine (PS).
Moreover, StarD7 is partially relocated from the cytoplasm to the
plasma membrane during in vitro cytotrophoblast differentiation
into syncytiotrophoblast (STB), a process characterized by an
enrichment of PS into the STB surface. This study further
investigates the function of StarD7 in trophoblasts. Here we
demonstrate an inhibition of BeWo cell proliferation by incubation
with recombinant StarD7 at 5, 10 and 20 mg/ml. Fluorescent
microscopy indicated that there were few intercellular desmosomes
between adjacent BeWo cells after treatment with StarD7 at 20
mg/ml. Similar results were found in control cultures treated with 5
mM forskolin. In addition, a protein-lipid overlay assay was
performed by an ELISA method using cardiolipin (CL), PS,
cholesterol (Chol), ceramide (Cer) and phosphatidylinosytol (PI).
The results indicate that StarD7 binds CL and PS, but no PI, Chol or
Cer. Altogether, these findings and previous data indicate that
StarD7 is a fusogenic protein leading us to conclude that StarD7 can
initiate/facilitate the syncytialization of BeWo cells through
transport of PS to the STB membrane surface