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2008 ; 12
(5A
): 1632-9
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Caveolin-1 is transported to multi-vesicular bodies after albumin-induced
endocytosis of caveolae in HepG2 cells
#MMPMID18053095
Botos E
; Klumperman J
; Oorschot V
; Igyártó B
; Magyar A
; Oláh M
; Kiss AL
J Cell Mol Med
2008[Sep]; 12
(5A
): 1632-9
PMID18053095
show ga
Caveolae-mediated endocytosis is a highly regulated endocytic pathway that exists
in parallel to other forms of clathrin-dependent and -independent endocytosis.
Internalized caveolae accumulate in intermediate organelles called caveosomes.
Here we addressed the further fate of internalized caveolae by inducing
caveolae-mediated uptake of albumin by HepG2 cells. We followed the route of
internalized caveolin-1 by immunogold labelling of ultrathin frozen sections and
by Western blot analyses of purified membrane fractions. Long-term (1 and 3 hrs)
albumin treatment resulted in the appearance of albumin-containing caveolae in
special multi-caveolar complexes (consisting of multiple caveolae clustered
together) connected to the plasma membrane and caveosome-like structures in the
cytoplasm. In addition, numerous CD63 (LIMP-1) positive late
endosomes/multi-vesicular bodies were found positive for caveolin-1, suggesting
that upon albumin incubation, caveolin-1 is endocytosed and enters the
degradative pathway. Surprisingly, the number of caveolae at the plasma membrane
increased after addition of albumin. This increase was blocked by cycloheximide
treatment, indicating that albumin internalization also stimulates de novo
protein synthesis, which is necessary for new caveolae formation. Together, our
results show that during long-term albumin uptake, caveolin-1 travels to late
endosomes and is replaced by newly synthesized caveolin-1 at the plasma membrane.
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