Hormone and Metabolic Research, Table of Contents Horm Metab Res 1999; 31(1): 5-7DOI: 10.1055/s-2007-978687 Originals Basic © Georg Thieme Verlag Stuttgart · New YorkDecreased Na,K-ATPase Activity by Glycation at the Catalytic CenterT. Katori1 , C. Bannai1 , Y. Hayashi2 , K. Yamashita1 1Division of Endocrinology and Metabolism, Institute of Clinical Medicine, University of Tsukuba, Tsukuba, Ibaraki, Japan 21st Department of Biochemistry, Kyorin University School of Medicine, Mitaka, Tokyo, Japan Recommend Article Abstract PDF Download(opens in new window) Buy Article(opens in new window) The in vitro activity of Na,K-ATPase isolated from outer medulla of dog kidney was decreased in a dose- and time-dependent manner by interaction with 100 mM glucose 6-phosphate (G6P) during the first 8 h. In the subsequent 16 h no change in activity was observed. On the other hand, Amadori-products of the enzyme increased in a dose- and time-dependent manner by glycation up to 100 mM G6P during 24 h. The presence of 5 mM ATP in glycation experiments protected the enzyme activity but did not inhibit the formation of Amadori-products. These results were consistent with inhibition of the Na,K-ATPase activity by glycation of the amino groups located in the catalytic center of the molecule. Key words Glycation - Na,K-ATPase - Amadori-Products - Catalytic Center PDF (214 kb)
