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Submitted on December 9, 2003
Accepted on May 5, 2004
Department of Cell and Molecular Biologyand Departments of Medicineand Physiological Sciencesat Lund University, Biomedical Center, SE-221 84, Sweden. The Oxford Center for Diabetes, Endocrinology and Metabolism , Churchill Hospital, Oxford Ox 37LJ, United Kingdom
* To whom correspondence should be addressed. E-mail: hindrik.mulder{at}medkem.lu.se.
Lipids are thought to serve as coupling factors in insulin secretion. Hormone-sensitive Lipase (HSL) is expressed in pancreatic 
-cells, and could potentially regulate insulin secretion via mobilization of stored triglycerides. Here, we examined the impact of HSL-deficiency on fuel metabolism and insulin secretion in mouse islets. Lack of HSL resulted in abrogation of neutral cholesterol ester hydrolase activity, whereas diglyceride lipase activity remained intact. While glucose stimulates lipolysis in rat islets, elevation of glucose with or without addition of cAMP failed to increase lipolysis in mouse islets regardless of genotype, as indicated by release of glycerol from islets. Storage of lipids, assayed as total acylglycerides, was unaltered in HSL null islets, and oxidation of fatty acids or glucose was not different. The intracellular rise in Ca2+ triggered by glucose and its subsequent oscillations were unaffected in HSL null islets. Accordingly, insulin secretion in static incubations of islets, in response to fuel- and non-fuel secretagogues, was in no instance significantly different between wild-type and HSL null mice. The lacking impact of HSL deficiency on insulin secretion may be attributed to the failure of insulin secretagogues to stimulate lipolysis. Consequently, a regulatory function of lipid mobilization in insulin secretion in the mouse appears unlikely.
-cells •
gene knock out •
stimulus-secretion coupling •
KATP •
metabolism
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