PMID- 10523666
OWN - NLM
STAT- MEDLINE
DCOM- 19991124
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 11
DP  - 1999 Nov
TI  - A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in
      adipocytes.
PG  - 7771-81
AB  - Insulin stimulates glucose uptake into muscle and fat cells by promoting the
      translocation of glucose transporter 4 (GLUT4) to the cell surface.
      Phosphatidylinositide 3-kinase (PI3K) has been implicated in this process.
      However, the involvement of protein kinase B (PKB)/Akt, a downstream target of
      PI3K in regulation of GLUT4 translocation, has been controversial. Here we report
      that microinjection of a PKB substrate peptide or an antibody to PKB inhibited
      insulin-stimulated GLUT4 translocation to the plasma membrane by 66 or 56%,
      respectively. We further examined the activation of PKB isoforms following
      treatment of cells with insulin or platelet-derived growth factor (PDGF) and
      found that PKBbeta is preferentially expressed in both rat and 3T3-L1 adipocytes,
      whereas PKBalpha expression is down-regulated in 3T3-L1 adipocytes. A switch in
      growth factor response was also observed when 3T3-L1 fibroblasts were
      differentiated into adipocytes. While PDGF was more efficacious than insulin in
      stimulating PKB phosphorylation in fibroblasts, PDGF did not stimulate PKBbeta
      phosphorylation to any significant extent in adipocytes, as assessed by several
      methods. Moreover, insulin, but not PDGF, stimulated the translocation of PKBbeta
      to the plasma membrane and high-density microsome fractions of 3T3-L1 adipocytes.
      These results support a role for PKBbeta in insulin-stimulated glucose transport 
      in adipocytes.
FAU - Hill, M M
AU  - Hill MM
AD  - Centre for Molecular Biology, Department of Physiology, University of Queensland,
      Brisbane, Queensland 4072, Australia.
FAU - Clark, S F
AU  - Clark SF
FAU - Tucker, D F
AU  - Tucker DF
FAU - Birnbaum, M J
AU  - Birnbaum MJ
FAU - James, D E
AU  - James DE
FAU - Macaulay, S L
AU  - Macaulay SL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Glucose Transporter Type 4)
RN  - 0 (Insulin)
RN  - 0 (Monosaccharide Transport Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Platelet-Derived Growth Factor)
RN  - 0 (Protein Isoforms)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Slc2a4 protein, mouse)
RN  - 0 (Slc2a4 protein, rat)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (Akt1 protein, rat)
RN  - EC 2.7.11.1 (Akt2 protein, mouse)
RN  - EC 2.7.11.1 (Akt2 protein, rat)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
SB  - IM
MH  - 3T3 Cells
MH  - Adipocytes/cytology/*metabolism
MH  - Animals
MH  - Biological Transport/drug effects
MH  - Cell Compartmentation/drug effects
MH  - Cell Differentiation
MH  - Cell Membrane/enzymology
MH  - Down-Regulation
MH  - Epididymis/cytology
MH  - Glucose Transporter Type 4
MH  - Insulin/*pharmacology
MH  - Male
MH  - Mice
MH  - Microinjections
MH  - Microsomes/enzymology
MH  - Monosaccharide Transport Proteins/*metabolism
MH  - *Muscle Proteins
MH  - Oligopeptides/metabolism
MH  - Phosphorylation
MH  - Platelet-Derived Growth Factor/pharmacology
MH  - Protein Isoforms/metabolism
MH  - Protein Kinases/*metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Proto-Oncogene Proteins/immunology/*metabolism
MH  - Proto-Oncogene Proteins c-akt
MH  - Rats
MH  - Rats, Wistar
MH  - Up-Regulation
PMC - PMC84835
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
AID - 10.1128/mcb.19.11.7771 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Nov;19(11):7771-81. doi: 10.1128/mcb.19.11.7771.