Insulin receptor binding and kinase activity in liver and skeletal muscles of lactating goats.
Lactation in goats has been shown to modify in vivo insulin action. [Debras, E., J. Grizard, E. Aina, S. Tesseraud, C. Champredon, and M. Arnal. Am. J. Physiol. 256 (Endocrinol. Metab. 19): E295-E302, 1989]. To further elucidate the mechanism of insulin action, we studied insulin binding and insulin receptor tyrosine kinase activity in solubilized and partially purified receptor preparations from liver and skeletal muscles (longissimus dorsi, tensor fascia lata, diaphragm, and masseter) from lactating and nonlactating goats. Lactation did not alter insulin receptors in the various skeletal muscles and had a minor influence on liver receptors (where only a 20% increase in receptor number was visible, P less than 0.05). Insulin-stimulated autophosphorylation and the kinase activity against polyglutamyltyrosine (4:1) were not significantly modified in skeletal muscle receptor preparations from lactating goats when compared with nonlactating animals. They tended to decrease in liver preparations, but not significantly. Thus the changes in insulin action in vivo during lactation in goats were not related to modifications in insulin kinase activity but were probably localized at a postreceptor level.
Balage
M
M
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Theix, Ceyrat, France.
Sornet
C
C
Grizard
J
J
D000818:Animals; D005260:Female; D006041:Goats / Q000378:metabolism / Q000502:physiology*; D007774:Lactation / Q000502:physiology*; D008099:Liver / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011972:Receptor, Insulin / Q000378:metabolism*
D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin