Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2001-4-30
pubmed:abstractText
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 approximately 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15292-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Differentiated 3T3L1 adipocytes are composed of heterogenous cell populations with distinct receptor tyrosine kinase signaling properties.
pubmed:affiliation
Department of Physiology and Biophysics, The University of Iowa, Iowa City, Iowa 52242, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't