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Publication
Microsomal Triglyceride Transfer Protein (MTP) Associates with Cytosolic Lipid
Droplets in 3T3-L1 Adipocytes.
Authors Love JD, Suzuki T, Robinson DB, Harris CM, Johnson JE, Mohler PJ, Jerome WG,
Swift LL
Submitted By Submitted Externally on 11/3/2015
Status Published
Journal PLoS ONE
Year 2015
Date Published
Volume : Pages 10 : e0135598
PubMed Reference 26267806
Abstract Lipid droplets are intracellular energy storage organelles composed of a
hydrophobic core of neutral lipid, surrounded by a monolayer of phospholipid and
a diverse array of proteins. The function of the vast majority of these proteins
with regard to the formation and/or turnover of lipid droplets is unknown. Our
laboratory was the first to report that microsomal triglyceride transfer protein
(MTP), a lipid transfer protein essential for the assembly of triglyceride-rich
lipoproteins, was expressed in adipose tissue of humans and mice. In addition,
our studies suggested that MTP was associated with lipid droplets in both brown
and white fat. Our observations led us to hypothesize that MTP plays a key role
in lipid droplet formation and/or turnover. The objective of these studies was
to gain insight into the function of MTP in adipocytes. Using molecular,
biochemical, and morphologic approaches we have shown: 1) MTP protein levels
increase nearly five-fold as 3T3-L1 cells differentiate into adipocytes. 2) As
3T3-L1 cells undergo differentiation, MTP moves from the juxtanuclear region of
the cell to the surface of lipid droplets. MTP and perilipin 2, a major lipid
droplet surface protein, are found on the same droplets; however, MTP does not
co-localize with perilipin 2. 3) Inhibition of MTP activity has no effect on the
movement of triglyceride out of the cell either as a lipid complex or via
lipolysis. 4) MTP is found associated with lipid droplets within hepatocytes
from human fatty livers, suggesting that association of MTP with lipid droplets
is not restricted to adipocytes. In summary, our data demonstrate that MTP is a
lipid droplet-associated protein. Its location on the surface of the droplet in
adipocytes and hepatocytes, coupled with its known function as a lipid transfer
protein and its increased expression during adipocyte differentiation suggest a
role in lipid droplet biology.




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