Title

The Procession Of Identity And Ecology In Contemporary Literature

Keywords

Apolipoprotein B (apoB); Endoplasmic reticulum (ER); Triacylglycerol (TAG); Very Low-Density Lipoprotein (VLDL); VLDL transport vesicle (VTV)

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. © 2012.

Publication Date

4-3-2012

Publication Title

Sub-Stance

Volume

41

Issue

7

Number of Pages

77-91

Document Type

Review

Personal Identifier

scopus

DOI Link

https://doi.org/10.1353/sub.2012.0005

Socpus ID

84859124333 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84859124333

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