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Investigations into the Actions of Glucose-Dependent Insulinotropic Polypeptide and Glucagon-Like Peptide-1(7–36)amide on Lipoprotein Lipase Activity in Explants of Rat Adipose Tissue1,2,

Jacqueline M. E. Knapper3,4,, Sarah M. Puddicombe, Linda M. Morgan and John M. Fletcher*

School of Biological Sciences, University of Surrey, Guildford, Surrey GU2 5XH, United Kingdom * Biosciences, Nutrition and Safety, URL Vlaardingen, 3130AC Vlaardingen, The Netherlands

The direct actions of glucose-dependent insulinotropic polypeptide, glucagon-like peptide-1(7–36)amide and insulin on lipoprotein lipase activity in explants of rat epididymal adipose tissues were investigated. Lipoprotein lipase was extracted into the incubation medium by heparin release of lipoprotein lipase and measured by fatty acid release from a glyceroltriolein emulsion. Insulin and glucose-dependent insulinotropic polypeptide caused a significant stimulation of lipoprotein lipase activity over a dose range of 0.25–4 nmol/L and 4–8 nmol/L, respectively. Explants incubated in the presence of both insulin and glucose-dependent insulinotropic polypeptide (at 0.5 and 4 nmol/L, respectively) showed levels of lipoprotein lipase activity significantly greater than that seen with either hormone alone. Neither insulin- nor glucose-dependent insulinotropic polypeptide-stimulated lipoprotein lipase was modified by the presence of the antibiotic actinomycin-D in the incubation medium, indicating that these two hormones exert their actions on the pre-existing cellular pool of lipoprotein lipase. Glucagon-like polypeptide-1(7–36)amide, over a dose range of 1–8 nmol/L, did not stimulate lipoprotein lipase activity. This study indicates that glucose-dependent insulinotropic polypeptide, in addition to stimulating insulin secretion, has a direct biological action on adipose tissue and in vivo, together with insulin, may promote lipoprotein lipase activity postprandially.


KEY WORDS: • glucose-dependent insulinotropic polypeptide • glucagon-like peptide-1 • rats • lipoprotein lipase

1 Supported by Unilever.

2 The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC section 1734 solely to indicate this fact.

3 JMEK holds a Unilever research fellowship.

4 To whom correspondence should be addressed.

Manuscript received 2 March 1994. Revision accepted 1 August 1994.




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