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  • Radioimmunoassay of a 26,000-dalton plasma insulin-like growth factor-binding protein: control by nutritional variables. 2461386

    Insulin-like growth factor I (IGF-I) is a peptide growth factor that circulates bound to carrier proteins. One form of carrier protein (mol wt, approximately 26K) is not believed to be GH dependent, is relatively unsaturated, and modulates the cellular response to IGF-I. This study was undertaken to determine the variables that control the plasma concentration of this protein, which was measured using a specific RIA. The mean plasma 26K IGF-binding protein (IGF-BP) concentration in 15 normal fasting subjects at 0800 h was 9.4 +/- 4.4 (+/- SD) micrograms/L. The mean value in GH-deficient patients was increased to 19.5 +/- 10.1 micrograms/L (n = 60; P less than 0.05), and it was 7.3 +/- 4.3 micrograms/L in patients with acromegaly (n = 31). The GH dependency of these changes is further supported by the observation that subjects who received GH injections had a 51% reduction in their fasting values. Nutritional intake appeared to be a more important controlling variable than GH. During an overnight fast plasma 26K IGF-BP values increased approximately 4-fold in 6 normal subjects. After 2 days of fasting, the mean value in 7 obese subjects rose progressively from 6.5 +/- 2.3 to 11.7 +/- 5.4 micrograms/L (P less than 0.001), and it increased further to 19.2 +/- 5.9 micrograms/L by day 4 of fasting; after 2 days of refeeding it returned to the prefasting level of 6.8 +/- 1.9 micrograms/L. Likewise, ingestion of a standard test meal resulted in a significant decrease in mean plasma 26K IGF-BP from a fasting value of 8.4 +/- 2.9 to 5.6 +/- 2.8 micrograms/L 4 h postprandially (P less than 0.05). In summary, the plasma concentrations of the 26K IGF-I-BP fluctuate widely in response to dietary manipulation, whereas GH status appears to be a secondary controlling variable.
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  • Calorie restriction increases the ratio of phosphatidylinositol 3-kinase catalytic to regulatory subunits in rat skeletal muscle. 15613677

    Calorie restriction [CR; 60% of ad libitum (AL) intake] improves insulin-stimulated glucose transport, concomitant with enhanced phosphorylation of Akt. The mechanism(s) for the CR-induced increase in Akt phosphorylation of insulin-stimulated muscle is unknown. The purpose of this study was to determine whether CR increased the ratio of catalytic to regulatory subunits favoring enhanced phosphatidylinositol (PI) 3-kinase signaling, which may contribute to increases in Akt phosphorylation and glucose transport in insulin-stimulated muscles. We measured the PI 3-kinase regulatory (p85alpha/beta, p50alpha, and p55alpha) and catalytic (p110) subunits abundance in skeletal muscle from male F344B/N rats after 8 wk of AL or CR treatment. In CR compared with AL muscles, regulatory isoforms, p50alpha and p55alpha abundance were approximately 40% lower (P less than 0.01) with unchanged p85alpha/beta levels. There was no diet-related change in catalytic subunit abundance. Despite lower IRS-1 levels ( approximately 35%) for CR vs. AL, IRS-1-p110 association in insulin-stimulated muscles was significantly (P less than 0.05) enhanced by approximately 50%. Downstream of PI 3-kinase, CR compared with AL significantly enhanced Akt serine phosphorylation by 1.5-fold higher (P = 0.01) and 3-O-methylglucose transport by approximately 20% in muscles incubated with insulin. The increased ratio of PI 3-kinase catalytic to regulatory subunits favors enhanced insulin signaling, which likely contributes to greater Akt phosphorylation and improved insulin sensitivity associated with CR in skeletal muscle.
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