Title

Proteomic Analysis of the Very Low Density Lipoprotein (VLDL) transport vesicles

Authors

Authors

A. Rahim; E. Nafi-valencia; S. Siddiqi; R. Basha; C. C. Runyon;S. A. Siddiqi

Comments

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Abbreviated Journal Title

J. Proteomics

Keywords

Very Low-Density Lipoprotein (VLDL); VLDL transport vesicle (VTV); Apolipoprotein B (apoB); Endoplasmic reticulum (ER); Triacylglycerol; (TAG); CHYLOMICRON RETENTION DISEASE; ROUGH ENDOPLASMIC-RETICULUM; B-CONTAINING; LIPOPROTEINS; APOLIPOPROTEIN-B; MEMBRANE-FUSION; CONFORMATIONAL-CHANGES; INTESTINAL ER; SAR1B GENE; COPII; PROTEIN; Biochemical Research Methods

Abstract

The VLDL transport vesicle (VTV) mediates the transport of nascent VLDL particles from the ER to the Golgi and plays a key role in VLDL-secretion from the liver. The functionality of VTV is controlled by specific proteins; however, full characterization and proteomic profiling of VTV remain to be carried out. Here, we report the first proteomic profile of VTVs. VTVs were purified to their homogeneity and characterized biochemically and morphologically. Thin section transmission electron microscopy suggests that the size of VTV ranges between 100 nm to 120 nm and each vesicle contains only one VLDL particle. Immunoblotting data indicate VTV concentrate apoB100, apoB48 and apoAIV but exclude apoAI. Proteomic analysis based on 2D-gel coupled with MALDI-TOF identified a number of vesicle-related proteins, however, many important VTV proteins could only be identified using LC-MS/MS methodology. Our data strongly indicate that VTVs greatly differ in their proteome with their counterparts of intestinal origin, the PCTVs. For example, VTV contains Sec22b, SVIP, ApoC-I, reticulon 3, cideB, LPCAT3 etc. which are not present in PCTV. The VTV proteome reported here will provide a basic tool to study the mechanisms underlying VLDL biogenesis, maturation, intracellular trafficking and secretion from the liver. Published by Elsevier B.V.

Journal Title

Journal of Proteomics

Volume

75

Issue/Number

7

Publication Date

1-1-2012

Document Type

Article

Language

English

First Page

2225

Last Page

2235

WOS Identifier

WOS:000303136600020

ISSN

1874-3919

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