Quantitative proteomic analysis of the adipocyte plasma membrane

Matthew J Prior; Mark Larance; Robert T Lawrence; Jamie Soul; Sean Humphrey; James Burchfield; Carol Kistler; Jonathon R Davey; Penelope J La-Borde; Michael Buckley; Hiroshi Kanazawa; Robert G Parton; Michael Guilhaus; David E James

doi:10.1021/pr200446r

Quantitative proteomic analysis of the adipocyte plasma membrane

Matthew J Prior, Mark Larance, Robert T Lawrence, Jamie Soul, Sean Humphrey, James Burchfield, Carol Kistler, Jonathon R Davey, Penelope J La-Borde, Michael Buckley, Hiroshi Kanazawa, Robert G Parton, Michael Guilhaus, David E James (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.

Original language	English
Pages (from-to)	4970-4982
Number of pages	13
Journal	Journal of Proteome Research
Volume	10
Issue number	11
DOIs	https://doi.org/10.1021/pr200446r
Publication status	Published - 4 Nov 2011

Keywords

Animals
Endoplasmic Reticulum
Caveolin 1
3T3-L1 Cells
Mice
Tandem Mass Spectrometry
Membrane Proteins
Cell Fractionation
Adipocytes
Calnexin
Proteomics
Cell Membrane
Syntaxin 16
Sodium-Hydrogen Antiporter
Qa-SNARE Proteins

Access to Document

10.1021/pr200446r

Cite this

@article{4f26c98694f6418f9e81c2b8557c87f2,

title = "Quantitative proteomic analysis of the adipocyte plasma membrane",

abstract = "The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.",

keywords = "Animals, Endoplasmic Reticulum, Caveolin 1, 3T3-L1 Cells, Mice, Tandem Mass Spectrometry, Membrane Proteins, Cell Fractionation, Adipocytes, Calnexin, Proteomics, Cell Membrane, Syntaxin 16, Sodium-Hydrogen Antiporter, Qa-SNARE Proteins",

author = "Prior, {Matthew J} and Mark Larance and Lawrence, {Robert T} and Jamie Soul and Sean Humphrey and James Burchfield and Carol Kistler and Davey, {Jonathon R} and La-Borde, {Penelope J} and Michael Buckley and Hiroshi Kanazawa and Parton, {Robert G} and Michael Guilhaus and James, {David E}",

year = "2011",

month = nov,

day = "4",

doi = "10.1021/pr200446r",

language = "English",

volume = "10",

pages = "4970--4982",

journal = "Journal of Proteome Research",

issn = "1535-3907",

publisher = "American Chemical Society",

number = "11",

}

TY - JOUR

T1 - Quantitative proteomic analysis of the adipocyte plasma membrane

AU - Prior, Matthew J

AU - Larance, Mark

AU - Lawrence, Robert T

AU - Soul, Jamie

AU - Humphrey, Sean

AU - Burchfield, James

AU - Kistler, Carol

AU - Davey, Jonathon R

AU - La-Borde, Penelope J

AU - Buckley, Michael

AU - Kanazawa, Hiroshi

AU - Parton, Robert G

AU - Guilhaus, Michael

AU - James, David E

PY - 2011/11/4

Y1 - 2011/11/4

N2 - The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.

AB - The adipocyte is a key regulator of mammalian metabolism. To advance our understanding of this important cell, we have used quantitative proteomics to define the protein composition of the adipocyte plasma membrane (PM) in the presence and absence of insulin. Using this approach, we have identified a high confidence list of 486 PM proteins, 52 of which potentially represent novel cell surface proteins, including a member of the adiponectin receptor family and an unusually high number of hydrolases with no known function. Several novel insulin-responsive proteins including the sodium/hydrogen exchanger, NHE6 and the collagens III and VI were also identified, and we provide evidence of PM-ER association suggestive of a unique functional association between these two organelles in the adipocyte. Together these studies provide a wealth of potential therapeutic targets for the manipulation of adipocyte function and a valuable resource for metabolic research and PM biology.

KW - Animals

KW - Endoplasmic Reticulum

KW - Caveolin 1

KW - 3T3-L1 Cells

KW - Mice

KW - Tandem Mass Spectrometry

KW - Membrane Proteins

KW - Cell Fractionation

KW - Adipocytes

KW - Calnexin

KW - Proteomics

KW - Cell Membrane

KW - Syntaxin 16

KW - Sodium-Hydrogen Antiporter

KW - Qa-SNARE Proteins

U2 - 10.1021/pr200446r

DO - 10.1021/pr200446r

M3 - Article

C2 - 21928809

SN - 1535-3907

VL - 10

SP - 4970

EP - 4982

JO - Journal of Proteome Research

JF - Journal of Proteome Research

IS - 11

ER -

Quantitative proteomic analysis of the adipocyte plasma membrane

Abstract

Keywords

Access to Document

Fingerprint

Cite this