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Hepatic lipase is abundant on both hepatocyte and endothelial cell surfaces in the liver

Sanan, D A, Fan, J, Bensadoun, A, Taylor, J M·1997·Journal of Lipid Research
DOI 10.1016/s0022-2275(20)37224-2
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Abstract

The cellular location of hepatic lipase was investigated in transgenic rabbits that expressed human hepatic lipase in the liver. The binding of monoclonal antibodies to human hepatic lipase, as detected by either fluorescence-tagged or gold-conjugated secondary antibodies, showed that hepatic lipase was concentrated at the surfaces of hepatic sinusoids. This distribution was the same as observed in the human liver. At the ultrastructural level, immunogold labeling of the space of Disse showed hepatic lipase on both lumenal and sublumenal surfaces of rabbit liver sinusoidal endothelial cells. An equivalent amount of hepatic lipase also was found on the external surfaces of hepatocyte microvilli in the space of Disse, as well as in the interhepatocyte spaces. The distribution suggests that a majority of the hepatic lipase produced by the liver is associated with hepatocyte surfaces, consistent with the functions of this enzyme in lipoprotein metabolism.

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  • Reduced sulfation of heparan chains could also decrease the pool of apoE/Lpl/HL associated with the hepatocyte plasma membrane, which may act as a reservoir for enriching TRLs with these ligands or as molecular bridges between lipoproteins and their receptors.

    “Reduced sulfation of heparan chains could also decrease the pool of apoE/Lpl/HL associated with the hepatocyte plasma membrane (9, 10, 59), which may act as a reservoir for enriching TRLs with these ligands or as molecular bridges between lipoproteins their receptors.”

    From Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members (2007) · cites this paper as [10]

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Metadata

Authors
Sanan, D. A., Fan, J., Bensadoun, A., & Taylor, J. M.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
1997-05
Volume
38
Issue
5
Pages
1002-1013
ISSN
0022-2275
DOI
10.1016/s0022-2275(20)37224-2
Cited by
72
References
0
Language
en
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