title: Characterization of glycyrrhizin-binding protein kinase from the crude membrane fraction of rat liver.
abstract: Using GL-affinity column chromatography, a casein phosphorylating protein kinase was purified selectively from the crude membrane fraction of rat liver. The biochemical characteristics of the purified kinase (approximately Mr 210 kDa) are very similar to those reported for polypeptide-dependent protein kinase (kinase P). Moreover, low doses of GL selectively inhibit phosphorylation of Mr 35-36 kDa polypeptides (which are cross-reacted with anti-lipocortins I and II) by the kinase in vitro. These results suggest that the anti-inflammatory activity of GL may involve the impairment of the physiological functions of lipocortins through their specific modification by the kinase at the cell membrane level.
authors: Department of Clinical Cancer Chemotherapy, Tohoku University, Sendai, Japan.
authors: A
authors: A
authors: Ishikawa
authors: R
authors: R
authors: Kanamaru
authors: A
authors: A
authors: Wakui
authors: S
authors: S
authors: Kanno
authors: K
authors: K
authors: Ohtsuki
mesh_terms: D000818:Animals; D017302:Annexins; D000998:Antiviral Agents / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D002846:Chromatography, Affinity / Q000379:methods; D002848:Chromatography, DEAE-Cellulose; D006034:Glycyrrhetinic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D019695:Glycyrrhizic Acid; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
chemical_list: D017302:Annexins; D000998:Antiviral Agents; D002135:Calcium-Binding Proteins; D010455:Peptides; D019695:Glycyrrhizic Acid; D011494:Protein Kinases; D006034:Glycyrrhetinic Acid