PMID- 16420524
OWN - NLM
STAT- MEDLINE
DCOM- 20060327
LR  - 20151119
IS  - 1398-9219 (Print)
IS  - 1398-9219 (Linking)
VI  - 7
IP  - 2
DP  - 2006 Feb
TI  - Insulin-regulated aminopeptidase marks an antigen-stimulated recycling 
      compartment in mast cells.
PG  - 155-67
AB  - Insulin-regulated aminopeptidase (IRAP) is a marker for insulin-sensitive 
      recycling compartments of fat and muscle cells that contain the glucose 
      transporter isoform GLUT4. Unlike GLUT4, IRAP is expressed in many other cell 
      types. Thus, it is a potential marker for regulated recycling compartments that 
      are analogous to GLUT4 vesicles. In bone marrow-derived mast cells, IRAP is 
      highly expressed and localizes to an intracellular compartment different from 
      secretory granules. Using cell-surface biotinylation, we determined that IRAP 
      underwent rapid redistribution to the plasma membrane on antigen/immunoglobulin E 
      (IgE) stimulation and was re-internalized within 30 min. When granule exocytosis 
      was inhibited, by removing extracellular calcium, adding the protein kinase C 
      inhibitor bisindolylmaleimide or the phosphatidylinositol 3-kinase inhibitor 
      wortmannin, IRAP redistribution was still detected in stimulated cells. However, 
      the redistribution of IRAP required intracellular calcium. By immunofluorescence, 
      IRAP significantly co-localized with the transferrin receptor (TfR), a marker for 
      constitutively recycling endosomes. However, antigen/IgE stimulation did not 
      increase TfR on the cell surface, indicating that IRAP and TfR may follow 
      different pathways to the plasma membrane. In rat peritoneal mast cells, the 
      distributions of IRAP and TfR overlapped to only a limited extent, indicating 
      that overlap may decrease with cell differentiation. We propose that IRAP 
      vesicles represent a second IgE-sensitive exocytotic compartment in mast cells, 
      which is regulated differently from secretory granules, and that these vesicles 
      may be similar to GLUT4 vesicles.
FAU - Liao, Haini
AU  - Liao H
AD  - Department of Cell Biology, University of Virginia Health System, School of 
      Medicine, Charlottesville, VA 22908, USA. hl7c@virginia.edu
FAU - Keller, Susanna R
AU  - Keller SR
FAU - Castle, J David
AU  - Castle JD
LA  - eng
GR  - AI47150/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - England
TA  - Traffic
JT  - Traffic (Copenhagen, Denmark)
JID - 100939340
RN  - 0 (Antigens)
RN  - 0 (Biomarkers)
RN  - 0 (Glucose Transporter Type 4)
RN  - 0 (Receptors, Transferrin)
RN  - 0 (SNARE Proteins)
RN  - 0 (Slc2a4 protein, rat)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 3.4.11.- (Aminopeptidases)
RN  - EC 3.4.11.3 (Cystinyl Aminopeptidase)
RN  - EC 3.4.11.3 (leucyl-cystinyl aminopeptidase)
SB  - IM
MH  - Aminopeptidases/*metabolism
MH  - Animals
MH  - Antigens/administration & dosage
MH  - Biomarkers/metabolism
MH  - Cell Compartmentation
MH  - Cell Line
MH  - Cell Membrane/enzymology
MH  - Cystinyl Aminopeptidase
MH  - Exocytosis
MH  - Glucose Transporter Type 4/metabolism
MH  - Immunoglobulin E/administration & dosage
MH  - Mast Cells/*enzymology/immunology/physiology
MH  - Mice
MH  - Rats
MH  - Receptors, Transferrin/metabolism
MH  - SNARE Proteins/metabolism
MH  - Secretory Vesicles/enzymology
EDAT- 2006/01/20 09:00
MHDA- 2006/03/28 09:00
CRDT- 2006/01/20 09:00
PHST- 2006/01/20 09:00 [pubmed]
PHST- 2006/03/28 09:00 [medline]
PHST- 2006/01/20 09:00 [entrez]
AID - TRA373 [pii]
AID - 10.1111/j.1600-0854.2006.00373.x [doi]
PST - ppublish
SO  - Traffic. 2006 Feb;7(2):155-67. doi: 10.1111/j.1600-0854.2006.00373.x.