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Proteomic profiling of the prechylomicron transport vesicle involved in the assembly and secretion of apoB‐48‐containing chylomicrons in the intestinal enterocytes
Author(s) -
Wong Diana M.,
Webb Jennifer P.,
Malinowski Paul M.,
Macri Joseph,
Adeli Khosrow
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800914
Subject(s) - vesicular transport protein , chylomicron , microbiology and biotechnology , secretion , transport protein , intracellular , golgi apparatus , copi , vesicle , biology , rab , vesicular transport proteins , biochemistry , microsomal triglyceride transfer protein , intracellular transport , secretory pathway , endosome , lipoprotein , endoplasmic reticulum , very low density lipoprotein , cholesterol , membrane , gtpase , vacuolar protein sorting
Intracellular assembly of chylomicrons (CM) occurs in intestinal enterocytes through a series of complex vesicular interactions. CM are transported from the ER to the Golgi using a specialized vesicular compartment called the prechylomicron transport vesicle (PCTV). In this study, PCTVs were isolated from the enteric ER of the Syrian Golden hamster, and characterized using 2‐DE and MS. Proteomic profiles of PCTV‐associated proteins were developed with the intention of identifying proteins involved in the formation, transport, lipidation, and assembly of CM particles. Positively identified proteins included those involved in lipoprotein assembly, namely microsomal triglyceride transfer protein and apolipoprotein B‐48, as well as proteins involved in vesicular transport, such as Sar1 and vesicle‐associated membrane protein 7. Other groups of proteins found were chaperones, intracellular vesicular trafficking proteins, fatty acid‐binding proteins, and lipid‐related proteins. These findings have increased our understanding of the transport vesicle involved in the intracellular assembly and transport of CM and can provide insight into potential cellular factors responsible for dysregulation of intestinal CM production.