INVESTIGADORES
FERNANDEZ Maria Del Carmen
congresos y reuniones científicas
Título:
Specific DRM lipid composition is essential to maintain the integrity of epithelial cell adhesion structures in rat renal papilla.
Autor/es:
M.G. MARQUEZ, F. LEOCATA, N. FAVALE, M.C. FERNANDEZ- TOME, N. STERIN-SPEZIALE.; M. C. FERNANDEZ
Lugar:
Pecs, Hungary
Reunión:
Congreso; 47th International Conference on the Biochemistry of Lipids (ICBL).; 2006
Institución organizadora:
ICBL
Resumen:
PO 30
Speci.c DRM lipid composition is essential to maintain
the integrity of epithelial cell adhesion structures
in rat renal papilla
M.G. M´arquez, F. Leocata, N. Favale, M.C. Fern´andez-
Tom´e, N. Sterin-Speziale
School of Pharmacy and Biochemistry, University
of Buenos Aires, IQUIFIB-CONICET, Buenos Aires,
Argentina
Adherens junctions (AJ) and focal adhesions (FA)
mediate cell-cell and cell-extracellular matrix adhesion,
respectively. FA structure is associated with detergent
resistant microdomains (DRM), but lesser information
is available about AJ proteins. In previous work we
described, in rat renal papilla, a specific DRM enriched
in sphingomyelin and cholesterol that contained FA proteins.
Changes in DRM lipid composition provoked by
cyclodextrin (CD), neomycin (Neo) and LiCl induced
dissipation of FAstructures from cultured collecting duct
cells. Now, we show that this specific DRM also contains
AJ proteins E-cadherin and -catenin.Western blot
analysis shows that changes in DRM lipid composition
induced by CD provokes a 10 and 50% decrease in the
amount of E-cadherin and -catenin present in DRM,
respectively. Neo induces a more important decrease
in -catenin than in E-cadherin, while LiCl induces no
changes in E-cadherin and a decrease in almost 25% of
-catenin.Western blot
analysis shows that changes in DRM lipid composition
induced by CD provokes a 10 and 50% decrease in the
amount of E-cadherin and -catenin present in DRM,
respectively. Neo induces a more important decrease
in -catenin than in E-cadherin, while LiCl induces no
changes in E-cadherin and a decrease in almost 25% of
-catenin present in DRM,
respectively. Neo induces a more important decrease
in -catenin than in E-cadherin, while LiCl induces no
changes in E-cadherin and a decrease in almost 25% of
-catenin than in E-cadherin, while LiCl induces no
changes in E-cadherin and a decrease in almost 25% of
-catenin. Immunofluorescence analysis of control cultured
collecting duct cells shows continuous E-cadherin
and -catenin immunostaining at cell borders marking
the AJ. CD and Neo induce relocation of E-cadherin
and cells cannot adhere to each other, but minor changes
are observed after LiCl treatment. -catenin staining
localizes in a submembrane region after CD treatment,
suggesting delocalization from the plasma membrane,
becomes discontinuous after Neo treatment, and remains
along cell boundaries with a lesser intensity after LiCl
incubation. Our results provide evidence that changes in
the lipidic composition ofDRMmodulates the behaviour
of proteins involved in cell adhesion structures, essential
to maintain renal papillary tubular organization.
-catenin. Immunofluorescence analysis of control cultured
collecting duct cells shows continuous E-cadherin
and -catenin immunostaining at cell borders marking
the AJ. CD and Neo induce relocation of E-cadherin
and cells cannot adhere to each other, but minor changes
are observed after LiCl treatment. -catenin staining
localizes in a submembrane region after CD treatment,
suggesting delocalization from the plasma membrane,
becomes discontinuous after Neo treatment, and remains
along cell boundaries with a lesser intensity after LiCl
incubation. Our results provide evidence that changes in
the lipidic composition ofDRMmodulates the behaviour
of proteins involved in cell adhesion structures, essential
to maintain renal papillary tubular organization.
-catenin immunostaining at cell borders marking
the AJ. CD and Neo induce relocation of E-cadherin
and cells cannot adhere to each other, but minor changes
are observed after LiCl treatment. -catenin staining
localizes in a submembrane region after CD treatment,
suggesting delocalization from the plasma membrane,
becomes discontinuous after Neo treatment, and remains
along cell boundaries with a lesser intensity after LiCl
incubation. Our results provide evidence that changes in
the lipidic composition ofDRMmodulates the behaviour
of proteins involved in cell adhesion structures, essential
to maintain renal papillary tubular organization.
-catenin staining
localizes in a submembrane region after CD treatment,
suggesting delocalization from the plasma membrane,
becomes discontinuous after Neo treatment, and remains
along cell boundaries with a lesser intensity after LiCl
incubation. Our results provide evidence that changes in
the lipidic composition ofDRMmodulates the behaviour
of proteins involved in cell adhesion structures, essential
to maintain renal papillary tubular organization.