|
The Journal of Lipid Research, Vol. 39, 789-806, April 1998
Copyright © 1998 by Lipid Research, Inc.
Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells
Ricardo P. Casaroli-Maranoa,
Raquel Garcíaa,
Elisabet Vilellab,
Gunilla Olivecronac,
Manuel Reinaa, and
Senén Vilaróa
a Department of Cellular Biology, Faculty of Biology, University of Barcelona, Avda. Diagonal, 645, E-08028 Barcelona, Spain
b Centre de Recerca Biomèdica, Hospital de Sant Joan, E-43201 Reus, Spain
c Department of Medical Biochemistry and Biophysics, University of Umeå, S-901 87 Umeå, Sweden
Correspondence to:
Senén Vilaró.
The cellular mechanisms and pathways by which lipoprotein lipase (LPL) enhances the binding and uptake of lipoproteins remains unknown. Confocal and immunoelectron microscopy demonstrated that primary binding of bovine LPL (bLPL) occurs at the microvilli surface of HepG2 cells and hepatocytes. Internalized bLPL was associated with endocytic vesicles and multivesicular bodies. Quantitative immunofluorescence indicated that the presence of bLPL caused a marked increase in the cell-surface binding of DiI-conjugated triacylglycerol-rich lipoproteins (DiI-TRL). Confocal microscopy showed that when DiI-TRL was incubated with bLPL at 4°C, the distributions of bound LPL and DiI-TRL were totally coincident, and covered the apical surface of both HepG2 cells and hepatocytes. When incubated separately, the time-courses of the internalization of fluorescence associated with DiI-TRL and bLPL were different: DiI-TRL was quickly internalized by both HepG2 cells and hepatocytes, and reached a plateau at 30 min, whereas intracellular LPL increased continuously, but more slowly in the same period. In the presence of bLPL, DiI-TRL was internalized progressively by HepG2 and by cultured hepatocytes for up to 1 h and no saturation was reached. At this time the intensity of labeling of bLPL was lower than of DiI-TRL and a higher number of DiI spots did not colocalize with bLPL immunofluorescence, suggesting that the ligands follow a different pathway after internalization.
The data suggest that when lipoprotein lipase (LPL) is associated with the lipoproteins it directs them to specific endocytic pathways. A hypothetical model of the intracellular pathways followed by triacylglycerol-rich lipoproteins and LPL after internalization is proposed.Casaroli-Marano, R. P., R. García, E. Vilella, G. Olivecrona, M. Reina, and S. Vilaró. Binding and intracellular trafficking of lipoprotein lipase and triacylglycerol-rich lipoproteins by liver cells. J. Lipid Res. 1998. 39: 789806.
Supplementary key words:
immunofluorescence, immunoelectron microscopy, lipoprotein, heparan sulfate proteoglycans, confocal microscopy

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
Q. Deng, J.-w. Zhai, M.-L. Michel, J. Zhang, J. Qin, Y.-y. Kong, X.-x. Zhang, A. Budkowska, P. Tiollais, Y. Wang, et al.
Identification and Characterization of Peptides That Interact with Hepatitis B Virus via the Putative Receptor Binding Site
J. Virol.,
April 15, 2007;
81(8):
4244 - 4254.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. C. Nierman, B. H.C.M.T. Prinsen, J. Rip, R. J. Veldman, J. A. Kuivenhoven, J. J.P. Kastelein, M. G.M. de Sain-van der Velden, and E. S.G. Stroes
Enhanced Conversion of Triglyceride-Rich Lipoproteins and Increased Low-Density Lipoprotein Removal in LPLS447X Carriers
Arterioscler. Thromb. Vasc. Biol.,
November 1, 2005;
25(11):
2410 - 2415.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
H. Masuno, S. Okamoto, J. Iwanami, K. Honda, T. Shiosaka, T. Kidani, K. Sakayama, and H. Yamamoto
Effect of 4-Nonylphenol on Cell Proliferation and Adipocyte Formation in Cultures of Fully Differentiated 3T3-L1 Cells
Toxicol. Sci.,
October 1, 2003;
75(2):
314 - 320.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. Scholl, C Gamallo, S Vilar?o, and M Quintanilla
Identification of PA2.26 antigen as a novel cell-surface mucin-type glycoprotein that induces plasma membrane extensions and increased motility in keratinocytes
J. Cell Sci.,
January 12, 1999;
112(24):
4601 - 4613.
[Abstract]
[PDF]
|
 |
|
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|