Characterization of the stimulatory action of insulin on insulin-like growth factor II binding to rat adipose cells. Differences in the mechanism of insulin action on insulin-like growth factor II receptors and glucose transporters

K. C. Appell, Ian Simpson, S. W. Cushman

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Insulin is known to increase the number of cell surface insulin-like growth factor II (IGF-II) receptors in isolated rat adipose cells through a subcellular redistribution mechanism similar to that for the glucose transporter. The effects of insulin on these two processes, therefore, have now been directly compared in the same cell preparations. 1) Insulin increases the steady state number of cell surface IGF-II receptors by 7-13-fold without affecting receptor affinity; however, insulin stimulates glucose transport activity by 25-40-fold. 2) The insulin concentration required for half-maximal stimulation of cell surface IGF-II receptor number is ~30% lower than that for the stimulation of glucose transport activity. 3) The half-time for the achievement of insulin's maximal effect at 37°C is much shorter for IGF-II receptor number (~0.8 min) than for glucose transport activity (~2.6 min). 4) Reversal of insulin's action at 37°C occurs more rapidly for cell surface IGF-II receptors (t( 1/2 ) ≃ 2.9 min) than for glucose transport activity (t( 1/2 ) ≃ 4.9 min). 5) When the relative subcellular distribution of IGF-II receptors is examined in basal cells, < 10% of the receptors are localized to the plasma membrane fraction indicating that most of the receptors, like glucose transporters, are localized to an intracellular compartment. However, in response to insulin, the number of plasma membrane IGF-II receptors increases only ~1.4-fold while the number of glucose transporters increases ~4.5-fold. Thus, while the stimulatory actions of insulin on cell surface IGF-II receptors and glucose transport activity are qualitatively similar, marked quantitative differences suggest that the subcellular cycling of these two integral membrane proteins occurs by distinct processes.

Original languageEnglish (US)
Pages (from-to)10824-10829
Number of pages6
JournalJournal of Biological Chemistry
Volume263
Issue number22
StatePublished - Jan 1 1988

Fingerprint

IGF Type 2 Receptor
Insulin-Like Growth Factor II
Facilitative Glucose Transport Proteins
Rats
Insulin
Glucose
Cell membranes
Cell Count
Cell Membrane
Membrane Proteins
Cells

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{697410492cce463888980fe4c4fa22ed,
title = "Characterization of the stimulatory action of insulin on insulin-like growth factor II binding to rat adipose cells. Differences in the mechanism of insulin action on insulin-like growth factor II receptors and glucose transporters",
abstract = "Insulin is known to increase the number of cell surface insulin-like growth factor II (IGF-II) receptors in isolated rat adipose cells through a subcellular redistribution mechanism similar to that for the glucose transporter. The effects of insulin on these two processes, therefore, have now been directly compared in the same cell preparations. 1) Insulin increases the steady state number of cell surface IGF-II receptors by 7-13-fold without affecting receptor affinity; however, insulin stimulates glucose transport activity by 25-40-fold. 2) The insulin concentration required for half-maximal stimulation of cell surface IGF-II receptor number is ~30{\%} lower than that for the stimulation of glucose transport activity. 3) The half-time for the achievement of insulin's maximal effect at 37°C is much shorter for IGF-II receptor number (~0.8 min) than for glucose transport activity (~2.6 min). 4) Reversal of insulin's action at 37°C occurs more rapidly for cell surface IGF-II receptors (t( 1/2 ) ≃ 2.9 min) than for glucose transport activity (t( 1/2 ) ≃ 4.9 min). 5) When the relative subcellular distribution of IGF-II receptors is examined in basal cells, < 10{\%} of the receptors are localized to the plasma membrane fraction indicating that most of the receptors, like glucose transporters, are localized to an intracellular compartment. However, in response to insulin, the number of plasma membrane IGF-II receptors increases only ~1.4-fold while the number of glucose transporters increases ~4.5-fold. Thus, while the stimulatory actions of insulin on cell surface IGF-II receptors and glucose transport activity are qualitatively similar, marked quantitative differences suggest that the subcellular cycling of these two integral membrane proteins occurs by distinct processes.",
author = "Appell, {K. C.} and Ian Simpson and Cushman, {S. W.}",
year = "1988",
month = "1",
day = "1",
language = "English (US)",
volume = "263",
pages = "10824--10829",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "22",

}

TY - JOUR

T1 - Characterization of the stimulatory action of insulin on insulin-like growth factor II binding to rat adipose cells. Differences in the mechanism of insulin action on insulin-like growth factor II receptors and glucose transporters

AU - Appell, K. C.

AU - Simpson, Ian

AU - Cushman, S. W.

PY - 1988/1/1

Y1 - 1988/1/1

N2 - Insulin is known to increase the number of cell surface insulin-like growth factor II (IGF-II) receptors in isolated rat adipose cells through a subcellular redistribution mechanism similar to that for the glucose transporter. The effects of insulin on these two processes, therefore, have now been directly compared in the same cell preparations. 1) Insulin increases the steady state number of cell surface IGF-II receptors by 7-13-fold without affecting receptor affinity; however, insulin stimulates glucose transport activity by 25-40-fold. 2) The insulin concentration required for half-maximal stimulation of cell surface IGF-II receptor number is ~30% lower than that for the stimulation of glucose transport activity. 3) The half-time for the achievement of insulin's maximal effect at 37°C is much shorter for IGF-II receptor number (~0.8 min) than for glucose transport activity (~2.6 min). 4) Reversal of insulin's action at 37°C occurs more rapidly for cell surface IGF-II receptors (t( 1/2 ) ≃ 2.9 min) than for glucose transport activity (t( 1/2 ) ≃ 4.9 min). 5) When the relative subcellular distribution of IGF-II receptors is examined in basal cells, < 10% of the receptors are localized to the plasma membrane fraction indicating that most of the receptors, like glucose transporters, are localized to an intracellular compartment. However, in response to insulin, the number of plasma membrane IGF-II receptors increases only ~1.4-fold while the number of glucose transporters increases ~4.5-fold. Thus, while the stimulatory actions of insulin on cell surface IGF-II receptors and glucose transport activity are qualitatively similar, marked quantitative differences suggest that the subcellular cycling of these two integral membrane proteins occurs by distinct processes.

AB - Insulin is known to increase the number of cell surface insulin-like growth factor II (IGF-II) receptors in isolated rat adipose cells through a subcellular redistribution mechanism similar to that for the glucose transporter. The effects of insulin on these two processes, therefore, have now been directly compared in the same cell preparations. 1) Insulin increases the steady state number of cell surface IGF-II receptors by 7-13-fold without affecting receptor affinity; however, insulin stimulates glucose transport activity by 25-40-fold. 2) The insulin concentration required for half-maximal stimulation of cell surface IGF-II receptor number is ~30% lower than that for the stimulation of glucose transport activity. 3) The half-time for the achievement of insulin's maximal effect at 37°C is much shorter for IGF-II receptor number (~0.8 min) than for glucose transport activity (~2.6 min). 4) Reversal of insulin's action at 37°C occurs more rapidly for cell surface IGF-II receptors (t( 1/2 ) ≃ 2.9 min) than for glucose transport activity (t( 1/2 ) ≃ 4.9 min). 5) When the relative subcellular distribution of IGF-II receptors is examined in basal cells, < 10% of the receptors are localized to the plasma membrane fraction indicating that most of the receptors, like glucose transporters, are localized to an intracellular compartment. However, in response to insulin, the number of plasma membrane IGF-II receptors increases only ~1.4-fold while the number of glucose transporters increases ~4.5-fold. Thus, while the stimulatory actions of insulin on cell surface IGF-II receptors and glucose transport activity are qualitatively similar, marked quantitative differences suggest that the subcellular cycling of these two integral membrane proteins occurs by distinct processes.

UR - http://www.scopus.com/inward/record.url?scp=0023715775&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023715775&partnerID=8YFLogxK

M3 - Article

VL - 263

SP - 10824

EP - 10829

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 22

ER -