Fasting and refeeding alter the insulin receptor tyrosine kinase in chicken liver but fail to affect brain insulin receptors

J. Simon, R. W. Rosebrough, J. P. McMurtry, N. C. Steele, J. Roth, M. Adamo, D. LeRoith

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

Insulin receptors from chicken liver and brain were studied following alterations in the nutritional state. Chickens were either fasted for 48 h, fasted for 48 h and then refed for 24 h, or fed a regular diet ad libitum. 125I-Porcine insulin binding was significantly elevated in liver membranes from the fasted animals and lowered in refed chickens when compared to preparations from ad libitum fed chickens. These changes in 125I-insulin binding were inversely related to the levels of plasma insulin and since receptor affinities for insulin were similar in each group, they probably represent alterations in receptor number. Apparent M(r) of α subunits of the insulin receptor was unaffected by alterations in the nutritional states. The presence of ATPase-like activities that co-eluted with liver insulin receptors from wheat germ agglutinin lectin columns but not from pea lectin columns necessitated the use of both pea and wheat germ agglutinin for liver insulin receptor purification. The insulin receptors purified from both lectin columns were recognized by anti-insulin receptor antiserum and had similar affinities for insulin which were unaltered by the nutritional state. Insulin-stimulatable autophosphorylation of the β subunit of the insulin receptor was lower in livers from fasted chickens and intermediate in refed chickens. Furthermore, basal and insulin-induced phosphorylation of the artificial substrate poly(Glu,Tyr)4:1 was significantly less in the fasting state and intermediate in the refed state compared to the ad libitum fed state. Insulin sensitivity (measured as the dose of insulin required for 50% maximal stimulation of kinase activity) was similar in all three states suggesting that the differences in insulin-induced phosphorylation are due to a change in maximal stimulation and not a change in insulin sensitivity. In contrast to the alterations seen with liver receptors, brain insulin receptors were unaffected by these alterations in nutritional state. These findings suggest that: 1) liver insulin receptors are affected by altering the nutritional state; 2) insulin binding to liver membranes is inversely related to plasma insulin levels; and 3) tyrosine kinase is decreased both in fasted and refed animals suggesting an uncoupling of the normal interaction between α subunit and β subunit in liver insulin receptors.

Original languageEnglish (US)
Pages (from-to)17081-17088
Number of pages8
JournalJournal of Biological Chemistry
Volume261
Issue number36
StatePublished - Dec 1 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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