Al. Schwarzman et al., Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix, P NAS US, 96(14), 1999, pp. 7932-7937
Citations number
45
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Most familial early-onset Alzheimer's disease cases are caused by mutations
in the presenilin 1 (PS1) gene. Subcellular localization of the endogenous
PS1 is essential for understanding its function, interactions with protein
s, and role in Alzheimer's disease, Although numerous studies revealed pred
ominant localization of PSI to endoplasmic reticulum and Golgi, there are c
onflicting reports on the localization of PS1 to the cell surface. We found
that endogenous PS1 is highly expressed in T lymphocytes (Jurkat cells). U
sing a variety of methods, we present evidence that endogenous PSI is local
ized to the cell surface in addition to intracellular membrane compartments
. Moreover, PS1 appeared in high levels on the surface of lamellipodia upon
adhesion of the cells to a collagen matrix. The redistribution of PS1 in a
dhered cells was strikingly similar to that of the well characterized adhes
ion protein CD44, Cell surface-PS1 formed complexes in vivo with actin-bind
ing protein filamin (ABP-280), which is known to form bridges between cell
surface receptors and cytoskeleton and mediate cell adhesion and cell motil
ity. Taken together, our results suggest a role of PSI in cell adhesion and
/or cell-matrix interaction.