AJP - Endocrinology and Metabolism, Vol 262, Issue 5 E561-E568, Copyright © 1992 by American Physiological Society

ARTICLES

Insulin receptor binding and kinase activity in liver and skeletal muscles of lactating goats

M. Balage, C. Sornet and J. Grizard
Laboratoire d'Etude du Metabolisme Azote, Institut National de la Recherche Agronomique, Centre de Clermont-Theix, Ceyrat, France.

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.

This article has been cited by other articles:

				S. Lemosquet, E. Debras, M. Balage, J. F. Hocquette, H. Rulquin, and J. Grizard Short-term mild hyperglycemia enhances insulin-stimulated glucose disposal in lactating goats Am J Physiol Regulatory Integrative Comp Physiol, February 1, 2002; 282(2): R464 - R474. [Abstract] [Full Text] [PDF]