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Pancreatic islet insulin secretion and metabolism in adult rats malnourished during neonatal life

Published online by Cambridge University Press:  09 March 2007

Francisco B. Barbosa ,
Kirsten Capito ,
Hans Kofod  and
Peter Thams
Francisco B. Barbosa
Affiliation:
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen, Denmark
Kirsten Capito*
Affiliation:
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen, Denmark
Hans Kofod
Affiliation:
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen, Denmark
Peter Thams
Affiliation:
Department of Medical Biochemistry and Genetics, The Panum Institute, University of Copenhagen, Copenhagen, Denmark
*
*Corresponding author: Kristen Capito, fax +45 35 32 77 01, email capito@imbg.ku.dk
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Abstract

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Pancreatic islets were isolated from rats that had been nursed by dams fed with a control or an 8·7 % protein diet during the first 12 d of the lactation period. Glucose-induced insulin secretion from islets in the 8·7 % protein group was reduced 50 %. The islet insulin and DNA content were similar, whereas the pancreatic insulin content was reduced by 30 % in the rats fed 8·7 % protein. In order to elucidate the mechanism responsible for the attenuation of insulin secretion, measurements were performed of the activity of several islet enzymes that had previously been supposed to be involved in the coupling of glucose stimulation to insulin secretion. Islet glucose oxidation was unaffected, but glucose-stimulated hydrolysis of phosphatidylinositol was reduced by one-third in the islets of rats fed 8·7 % protein. The activity of mitochondrial glycerophosphate dehydrogenase was similar in islets of rats fed the 8·7 % protein diet and those fed the control diet. The activity of Ca-independent phospholipase A2 was increased fourfold in the islets of rats fed 8·7 % protein. It is concluded that impairment of glucose-induced insulin secretion in rats fed a low-protein diet may be caused by attenuation of islet phosphatidylinositol hydrolysis, and it is tentatively suggested that the increased activity of Ca-independent phospholipase A2 in islets of rats fed a low-protein diet may participate in the stimulation of apoptosis.

Keywords

Protein malnutritionPancreatic islet metabolismInsulin secretionPhosphoinositidesPhospholipase A2Glycerophosphate dehydrogenase
Type
Research Article
Information
British Journal of Nutrition , Volume 87 , Issue 2 , February 2002 , pp. 147 - 155
Copyright
Copyright © The Nutrition Society 2006

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