ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway

Mairi Clarke, Marie Ann Ewart, Lorraine C. Santy, Rytis Prekeris, Gwyn W. Gould

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Adipocytes are now known to secrete a range of adipokines that exhibit distinct biological functions. Here, we sought to understand the secretory pathways utilised by ACRP30 to the surface of adipocytes. We find that ACRP30 overlaps with adipsin in intracellular compartments distinct from Glut4, but nonetheless exhibits insulin-stimulated secretion from cells. Both adipsin and ACRP30 overlap with transferrin receptor-positive membranes, implying that the pathway of secretion involves the transferrin receptor-positive endosomal system. Consistent with this, we show that ablation of endosomes significantly inhibited the secretion of ACRP30, as did treatment of cells with Brefeldin A. In order to further probe the role of recycling endosomes on the secretion of ACRP30, we over-expressed a mutant form of Rab11, Rab11-S25N, in 3T3-L1 adipocytes and found that expression of this mutant significantly reduced basal and insulin-stimulated secretion. We also demonstrate that Arf6 also plays a role in the secretion of ACRP30. Collectively, these data implicate both Arf6 and Rab11 as crucial mediators of constitutive and insulin-stimulated secretion of ACRP30 and further suggest that recycling endosomes may play a central role in this process.

Original languageEnglish (US)
Pages (from-to)1361-1367
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume342
Issue number4
DOIs
StatePublished - Apr 21 2006

Fingerprint

Endosomes
Adipocytes
Complement Factor D
Transferrin Receptors
Secretory Pathway
Insulin
Recycling
Brefeldin A
Adipokines
Ablation
Cells
Membranes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Clarke, Mairi ; Ewart, Marie Ann ; Santy, Lorraine C. ; Prekeris, Rytis ; Gould, Gwyn W. / ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway. In: Biochemical and Biophysical Research Communications. 2006 ; Vol. 342, No. 4. pp. 1361-1367.
@article{7f7f8a93de1040d4b57ff32e069abdd8,
title = "ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway",
abstract = "Adipocytes are now known to secrete a range of adipokines that exhibit distinct biological functions. Here, we sought to understand the secretory pathways utilised by ACRP30 to the surface of adipocytes. We find that ACRP30 overlaps with adipsin in intracellular compartments distinct from Glut4, but nonetheless exhibits insulin-stimulated secretion from cells. Both adipsin and ACRP30 overlap with transferrin receptor-positive membranes, implying that the pathway of secretion involves the transferrin receptor-positive endosomal system. Consistent with this, we show that ablation of endosomes significantly inhibited the secretion of ACRP30, as did treatment of cells with Brefeldin A. In order to further probe the role of recycling endosomes on the secretion of ACRP30, we over-expressed a mutant form of Rab11, Rab11-S25N, in 3T3-L1 adipocytes and found that expression of this mutant significantly reduced basal and insulin-stimulated secretion. We also demonstrate that Arf6 also plays a role in the secretion of ACRP30. Collectively, these data implicate both Arf6 and Rab11 as crucial mediators of constitutive and insulin-stimulated secretion of ACRP30 and further suggest that recycling endosomes may play a central role in this process.",
author = "Mairi Clarke and Ewart, {Marie Ann} and Santy, {Lorraine C.} and Rytis Prekeris and Gould, {Gwyn W.}",
year = "2006",
month = "4",
day = "21",
doi = "10.1016/j.bbrc.2006.02.102",
language = "English (US)",
volume = "342",
pages = "1361--1367",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway. / Clarke, Mairi; Ewart, Marie Ann; Santy, Lorraine C.; Prekeris, Rytis; Gould, Gwyn W.

In: Biochemical and Biophysical Research Communications, Vol. 342, No. 4, 21.04.2006, p. 1361-1367.

Research output: Contribution to journalArticle

TY - JOUR

T1 - ACRP30 is secreted from 3T3-L1 adipocytes via a Rab11-dependent pathway

AU - Clarke, Mairi

AU - Ewart, Marie Ann

AU - Santy, Lorraine C.

AU - Prekeris, Rytis

AU - Gould, Gwyn W.

PY - 2006/4/21

Y1 - 2006/4/21

N2 - Adipocytes are now known to secrete a range of adipokines that exhibit distinct biological functions. Here, we sought to understand the secretory pathways utilised by ACRP30 to the surface of adipocytes. We find that ACRP30 overlaps with adipsin in intracellular compartments distinct from Glut4, but nonetheless exhibits insulin-stimulated secretion from cells. Both adipsin and ACRP30 overlap with transferrin receptor-positive membranes, implying that the pathway of secretion involves the transferrin receptor-positive endosomal system. Consistent with this, we show that ablation of endosomes significantly inhibited the secretion of ACRP30, as did treatment of cells with Brefeldin A. In order to further probe the role of recycling endosomes on the secretion of ACRP30, we over-expressed a mutant form of Rab11, Rab11-S25N, in 3T3-L1 adipocytes and found that expression of this mutant significantly reduced basal and insulin-stimulated secretion. We also demonstrate that Arf6 also plays a role in the secretion of ACRP30. Collectively, these data implicate both Arf6 and Rab11 as crucial mediators of constitutive and insulin-stimulated secretion of ACRP30 and further suggest that recycling endosomes may play a central role in this process.

AB - Adipocytes are now known to secrete a range of adipokines that exhibit distinct biological functions. Here, we sought to understand the secretory pathways utilised by ACRP30 to the surface of adipocytes. We find that ACRP30 overlaps with adipsin in intracellular compartments distinct from Glut4, but nonetheless exhibits insulin-stimulated secretion from cells. Both adipsin and ACRP30 overlap with transferrin receptor-positive membranes, implying that the pathway of secretion involves the transferrin receptor-positive endosomal system. Consistent with this, we show that ablation of endosomes significantly inhibited the secretion of ACRP30, as did treatment of cells with Brefeldin A. In order to further probe the role of recycling endosomes on the secretion of ACRP30, we over-expressed a mutant form of Rab11, Rab11-S25N, in 3T3-L1 adipocytes and found that expression of this mutant significantly reduced basal and insulin-stimulated secretion. We also demonstrate that Arf6 also plays a role in the secretion of ACRP30. Collectively, these data implicate both Arf6 and Rab11 as crucial mediators of constitutive and insulin-stimulated secretion of ACRP30 and further suggest that recycling endosomes may play a central role in this process.

UR - http://www.scopus.com/inward/record.url?scp=33644901801&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33644901801&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2006.02.102

DO - 10.1016/j.bbrc.2006.02.102

M3 - Article

C2 - 16516854

AN - SCOPUS:33644901801

VL - 342

SP - 1361

EP - 1367

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -