Camptothecin induces the transit of FasL trimers to the cell surface in apoptosis HEp-2 cells

• Autorzy: Meza-Lamas E , Bollain-Y-Goytia J.J. , Ramirez-Sandoval R. , Sanchez-Rodriguez S.H. , Lopez-Robles E. , Avaloz-Diaz E. , Herrera-Esparza R.
• Języki publikacji: EN

Abstrakty

EN

Fas ligand (L) is a membrane protein from the tumor necrosis factor (TNF) family. It induces apoptosis upon contact with its Fas/CD95/APO1 receptor. Trimerization of FasL on the surface of effector cells is essential in the binding of the Fas trimer of the target cells. The receptor then recruits an adaptor and caspase-like proteins which lead apoptosis. This paper reports on the fate of FasL in HEp-2 cells committed to apoptosis by induction with campthotecin. Our main results demonstrated that in non-apoptotic cells, FasL aggregates in the cytoplasm forming trimers of 120 kDa. Apoptosis increases the trimeric FasL species, but also induces its dissociation into monomers of 35 kDa. In conclusion, camptothecin appears to perturb the Fas and FasL segregation in the cytoplasm by promoting the transit of FasL to the cell surface, thus fostering a process of autocrine or paracrine apoptosis. FasL is trimerized prior to Fas/FasL complex formation, and after apoptosis, FasL undergoes an intense turnover.

Słowa kluczowe

EN

cell surface; cell; FasL segregation; Fas ligand; tumour necrosis factor family; oligomerization; Fas segregation; apoptosis; camptothecin; membrane protein

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2006
• Tom: 11
• Numer: 3
• Opis fizyczny: p.299-311,fig.,ref.

Twórcy

autor

Meza-Lamas E

• Universidad Autonoma de Zacatecas, Guadalupe, Zacatecas, Mexico

autor

Bollain-Y-Goytia J.J.

autor

Ramirez-Sandoval R.

autor

Sanchez-Rodriguez S.H.

autor

Lopez-Robles E.

autor

Avaloz-Diaz E.

autor

Herrera-Esparza R.

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