Counter-regulation of insulin-stimulated glucose transport by catecholamines in the isolated rat adipose cell

U. Smith, M. Kuroda, Ian Simpson

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Abstract

The interaction between catecholamines and insulin in regulating glucose transport in isolated rat adipose cells has been evaluated. In the absence of insulin, 1 μM isoproterenol stimulates 3-O-methylglucose transport ~2 fold. However, isoproterenol in combination with adenosine deaminase inhibits glucose transport activity ~60%. N6-Phenylisopropyladenosine, a nonmetabolizable adenosine analogue, substantially reverses this inhibitory effect and actually stimulates glucose transport activity ~2-fold in the absence of isoproterenol. Dibutyryl cAMP inhibits glucose transport activity ~75% regardless of adenosine deaminase. While none of these agents significantly influences the basal concentration of plasma membrane glucose transporters, as assessed by specific D-glucose-inhibitable cytochalasin B binding, isoproterenol or dibutyryl cAMP in combination with adenosine deaminase reduces that in the low density microsomes 19 and 58%, respectively. In the presence of insulin, both isoproterenol and adenosine deaminase alone inhibit glucose transport activity ~25%. However, only the latter is accompanied by a corresponding decrease in the insulin-stimulated concentration of plasma membrane glucose transporters. Together, isoproterenol and adenosine deaminase inhibit insulin-stimulated glucose transport activity ~75%, even in the presence of 5 mM glucose to maintain cellular ATP levels. A similar inhibition is observed with dibutyryl cAMP. However, these agents decrease the insulin-stimulated concentration of plasma membrane glucose transporters only ~45%. Nevertheless, all of these inhibitory effects occur through decreases in the transport V(max). In addition, N6-phenylisopropyladenosine partially reverses the inhibitory effects induced by the presence of adenosine deaminase. These results suggest that catecholamines counter-regulate basal and insulin-stimulated glucose transport in rat adipose cells through a cAMP-mediated mechanism, but only in part by modulating the translocation of glucose transporters.

Original languageEnglish (US)
Pages (from-to)8758-8763
Number of pages6
JournalJournal of Biological Chemistry
Volume259
Issue number14
StatePublished - 1984

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Catecholamines
Rats
Adenosine Deaminase
Insulin
Isoproterenol
Glucose
Facilitative Glucose Transport Proteins
Membrane Transport Proteins
Cell membranes
Phenylisopropyladenosine
Cell Membrane
3-O-Methylglucose
Cytochalasin B
Microsomes
Adenosine
Adenosine Triphosphate

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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title = "Counter-regulation of insulin-stimulated glucose transport by catecholamines in the isolated rat adipose cell",
abstract = "The interaction between catecholamines and insulin in regulating glucose transport in isolated rat adipose cells has been evaluated. In the absence of insulin, 1 μM isoproterenol stimulates 3-O-methylglucose transport ~2 fold. However, isoproterenol in combination with adenosine deaminase inhibits glucose transport activity ~60{\%}. N6-Phenylisopropyladenosine, a nonmetabolizable adenosine analogue, substantially reverses this inhibitory effect and actually stimulates glucose transport activity ~2-fold in the absence of isoproterenol. Dibutyryl cAMP inhibits glucose transport activity ~75{\%} regardless of adenosine deaminase. While none of these agents significantly influences the basal concentration of plasma membrane glucose transporters, as assessed by specific D-glucose-inhibitable cytochalasin B binding, isoproterenol or dibutyryl cAMP in combination with adenosine deaminase reduces that in the low density microsomes 19 and 58{\%}, respectively. In the presence of insulin, both isoproterenol and adenosine deaminase alone inhibit glucose transport activity ~25{\%}. However, only the latter is accompanied by a corresponding decrease in the insulin-stimulated concentration of plasma membrane glucose transporters. Together, isoproterenol and adenosine deaminase inhibit insulin-stimulated glucose transport activity ~75{\%}, even in the presence of 5 mM glucose to maintain cellular ATP levels. A similar inhibition is observed with dibutyryl cAMP. However, these agents decrease the insulin-stimulated concentration of plasma membrane glucose transporters only ~45{\%}. Nevertheless, all of these inhibitory effects occur through decreases in the transport V(max). In addition, N6-phenylisopropyladenosine partially reverses the inhibitory effects induced by the presence of adenosine deaminase. These results suggest that catecholamines counter-regulate basal and insulin-stimulated glucose transport in rat adipose cells through a cAMP-mediated mechanism, but only in part by modulating the translocation of glucose transporters.",
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Counter-regulation of insulin-stimulated glucose transport by catecholamines in the isolated rat adipose cell. / Smith, U.; Kuroda, M.; Simpson, Ian.

In: Journal of Biological Chemistry, Vol. 259, No. 14, 1984, p. 8758-8763.

Research output: Contribution to journalArticle

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AU - Smith, U.

AU - Kuroda, M.

AU - Simpson, Ian

PY - 1984

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