Altered muscle insulin sensitivity in the male offspring of protein
malnourished rats.
E., Ozanne S., C. L. Wang, N. Coleman, and G. D. Smith.
Dept. of Clinical Biochemistry, Addenbrookeaes Hospital, Hills
Road, Cambridge, CB2 2QR, U.K., Dept.of Histopathology,
Addenbrookeaes Hospital, Hills Road, Cambridge, CB2 2QR, U.K.
APStracts 3:0189E, 1996.
Insulin sensitivity of skeletal muscle was studied in male offspring
of dams fed either a 20 % (control) or 8 % (low protein) diet during
pregnancy and lactation. Freshly isolated muscle strips from low
protein animals took up more 3H-methyl glucose than controls (19.2
2.5 and 4.26 0.45 nmol/min/mg muscle respectively, (p < 0.001).
However after a 60 minute preincubation there was no significant
difference in basal glucose transport (4.02 0.42 and 4.23 0.35
nmol/min/mg for control and low protein, respectively). Insulin (300
pM) had a significantly greater (p < 0.001) effect on
stimulation of glucose transport into preincubated low protein muscle
strips than controls (to 14.14 1.25 and 9.61 0.71 nmol/min/mg,
respectively). There were no differences in total Glut 4 protein
content. However, subcellular fractionation revealed significantly (p
< 0.001) more Glut 4 in muscle plasma membranes of low protein
animals compared to controls. Insulin increased (p < 0.001) the
Glut 4 content of control plasma membranes but had no effect in low
protein animals. There were two-fold more insulin receptors in low
protein muscle membranes compared to controls (1.28 0.10 x 1011 and
2.35 0.17 x 1011 insulin receptors/mg muscle membrane protein,
respectively, p < 0.01). These results suggest that programming
of muscle insulin sensitivity can occur during fetal life.
Received 17 June 1996; accepted in final form 30 August 1996.
APS Manuscript Number E292-6.
Article publication pending Am. J. Physiol. (Endocrinol. Metab.).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 19 September 1996