The inhibition of glucokinase by rat and Xenopus GKRPs (glucokinase regulatory protein) is well documented. We report a comparison of the effects of human and rat GKRPs on glucokinase activity. Human GKRP is a more potent inhibitor of glucokinase than rat GKRP in the absence of fructose 6-phosphate or sorbitol 6-phosphate, and has a higher affinity for these ligands. However, human and rat GKRPs have similar affinities for fructose 1-phosphate and chloride. Residues that are not conserved between the rodent and human proteins affect both the affinity for fructose 6-phosphate and sorbitol 6-phosphate and the inhibitory potency of GKRP on glucokinase in the absence of these ligands.
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http://dx.doi.org/10.1042/BJ20031414 | DOI Listing |
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Bundeswehr Institute of Pharmacology and Toxicology, Neuherbergstrasse 11, 80937 Munich, Germany; Walther-Straub-Institute of Pharmacology and Toxicology, Faculty of Medicine, Ludwig-Maximilians-Universität München, Goethestrasse 33, 80336 Munich, Germany. Electronic address:
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State Key Laboratory of Oral & Maxillofacial Reconstruction and Regeneration & National Clinical Research Center for Oral Diseases & Shaanxi International Joint Research Center for Oral Diseases, Center for Tissue Engineering, School of Stomatology, The Fourth Military Medical University, Xi'an, Shaanxi, 710032, China; Department of Orthodontics, School of Stomatology, The Fourth Military Medical University, Xi'an, Shaanxi, 710032, China. Electronic address:
Periodontal disease is a major contributor to tooth loss worldwide in adults. Particularly, periodontal bone defect is a common clinical condition, yet current therapeutic strategies exhibit limited effectiveness. Recently, natural bone graft materials have attracted considerable interest for enhancing bone defect repair due to their superior biocompatibility and osteogenic capabilities.
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Human Anatomy & Embryology Department, Faculty of Medicine, Zagazig University, Egypt.
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Department of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada.
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