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Differentiated 3T3L1 Adipocytes Are Composed of Heterogenous Cell Populations with Distinct Receptor Tyrosine Kinase Signaling Properties
Journal article   Open access   Peer reviewed

Differentiated 3T3L1 Adipocytes Are Composed of Heterogenous Cell Populations with Distinct Receptor Tyrosine Kinase Signaling Properties

Satoshi Shigematsu, Sarah L. Miller and Jeffrey E. Pessin
The Journal of biological chemistry, Vol.276(18), pp.15292-15297
01/2001
DOI: 10.1074/jbc.M009684200
PMID: 11278545
url
https://doi.org/10.1074/jbc.M009684200View
Published (Version of record) Open Access

Abstract

Various studies have demonstrated that the platelet-derived growth factor (PDGF) receptor in adipocytes can activate PI 3-kinase activity without affecting insulin-responsive glucose transporter (GLUT4) translocation. To investigate this phenomenon of receptor signaling specificity, we utilized single cell analysis to determine the cellular distribution and signaling properties of PDGF and insulin in differentiated 3T3L1 adipocytes. The insulin receptor was highly expressed in a large percentage of the cell population (>95%) that also expressed caveolin 2 and GLUT4 with very low levels of the PDGF receptor. In contrast, the PDGF receptor was only expressed in ∼10% of the differentiated 3T3L1 cell population with relatively low levels of the insulin receptor, caveolin 2, and GLUT4. Consistent with this observation, insulin stimulated the phosphorylation of Akt in the caveolin 2- and GLUT4-positive cells, whereas PDGF primarily stimulated Akt phosphorylation in the caveolin 2- and GLUT4-negative cell population. Furthermore, transfection of the PDGF receptor in the insulin receptor-, GLUT4-, and caveolin 2-positive cells resulted in the ability of PDGF to stimulate GLUT4 translocation. These data demonstrate that differentiated 3T3L1 adipocytes are not a homogeneous population of cells, and the lack of PDGF receptor expression in the GLUT4-positive cell population accounts for the inability of the endogenous PDGF receptor to activate GLUT4 translocation.

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