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Journal of Clinical Endocrinology & Metabolism, Vol 79, 485-488, Copyright © 1994 by Endocrine Society

ARTICLES

Immunoreactive glycogen-binding subunit of protein phosphatase-1 in human skeletal muscle

BL Nyomba and DM Mott
Clinical Diabetes and Nutrition Section, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Phoenix, Arizona 85016.

In rabbit muscle, analyzed by Western blot, the glycogen-bound protein phosphatase-1 (PP-1G) is composed of a 37-kilodalton (kDa) catalytic subunit complexed to a 160-kDa glycogen-binding subunit (G-subunit) responsible for the interaction of PP-1G with glycogen. PP-1G has not been characterized in humans. In the present study, G-subunit was identified in human muscle extracts by Western blot using an antibody raised against a sequence (the phosphoregulatory domain) of the rabbit muscle G-subunit. The human G-subunit was also a 160-kDa protein by Western blot. When the G-subunit content of skeletal muscle was quantitated in 17 Pima Indians with a wide range of insulin sensitivities determined during euglycemic clamps, there was a significant negative correlation (r = -0.55; P = 0.02) between the G- subunit content and in vivo insulin-mediated glucose disposal rates. The results suggest that insulin resistance is associated with an increased content and/or immunoreactivity of G-subunit in human muscle.




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Copyright © 1994 by The Endocrine Society