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 Research Article Open Access 
Hepatic Endosome Protein Profiling in Apolipoprotein E Deficient Mice Expressing Apolipoprotein B48 but not B100
Department of Comparative Biosciences, University of Illinois, 2001 S. Lincoln Avenue, Urbana, IL, USA
*Corresponding author: Dr. Hong Yang
Department of Physiology
Meharry Medical College, Nashville, TN
Tel: (615) 327-5772
Fax: (615) 3212949
E-mail:[email protected]
 
Received September 10, 2010; Accepted September 23, 2010; Published September 23, 2010
Citation: Chen A, Guo Z, Zhou L, Yang H (2010) Hepatic Endosome Protein Profiling in Apolipoprotein E Deficient Mice Expressing Apolipoprotein B48 but not B100. J Bioanal Biomed 2: 100-106. doi:10.4172/1948-593X.1000031
 
Copyright: © 2010 Chen A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 
Abstract
Liver cells absorb apolipoprotein (Apo) B48-carrying lipoproteins in ApoE's absence, albeit not as efficiently as the ApoE-mediated process. Our objective was to identify differentially expressed hepatic endosome proteins in mice expressing ApoB48 but lacking ApoE and ApoB100 expression (ApoE-/-/B48/48). We purified early and late endosomes from ApoE-/-/B48/48 and wild-type mouse's livers. In ApoE-/-/B48/48 mouse's hepatic endosomes, proteomic analysis revealed elevated protein levels of major urinary protein 6 (MUP), calreticulin, protein disulfide isomerases (PDI) A1, and A3. These proteins are capable of interacting with lipids/lipoproteins and triggering receptormediated endocytosis. In addition, hepatic endosomes from ApoE-/- /B48/48 mice exhibited significantly reduced protein levels of haptoglobin, hemopexin, late endosome/lysosome interacting protein, cell division control protein 2 homolog, γ-soluble Nethylmaleimide- sensitive factor attachment protein, vacuolar ATP synthase catalytic subunit A1, dipeptidyl peptidases II, cathepsin B, D, H, and Z. These proteins participate in plasma heme clearance, receptor-mediated signaling, membrane fusion, endosomal/lysosomal acidification, and protein degradation. The significance of increasing endosomal MUP, calreticulin and PDIs in ApoE-/-/B48/48 mouse liver cells is not clear; however, reducing endosomal/ lysosomal membrane proteins and hydrolases might be, at least partially, responsible for the retarded clearance of plasma ApoB-carrying lipoproteins in ApoE-/-/B48/48 mice.
 
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