Characterization of complement C3 as a glycyrrhizin (GL)-binding protein and the phosphorylation of C3alpha by CK-2, which is potently inhibited by GL and glycyrrhetinic acid in vitro.

Kawakami, Fumitaka; Shimoyama, Yoshihito; Ohtsuki, Kenzo

Kawakami, Fumitaka; Shimoyama, Yoshihito; Ohtsuki, Kenzo.

Affiliation

Kawakami F; Genetical Biochemistry and Signal Biology, Graduate School of Medical Sciences, Kitasato University, 1-15-1 Kitasato, Sagamihara 228-8555, Japan.

J Biochem ; 133(2): 231-7, 2003 Feb.

Article in En | MEDLINE | ID: mdl-12761187

Subject(s)

Complement C3/metabolism; Complement C3a/metabolism; Glycyrrhetinic Acid/pharmacology; Glycyrrhizic Acid/metabolism; Protein Serine-Threonine Kinases/metabolism; Arthritis; Binding Sites; Casein Kinase II; Complement C3/analysis; Complement C3/antagonists & inhibitors; Complement C3a/antagonists & inhibitors; Glycyrrhiza/chemistry; Glycyrrhizic Acid/pharmacology; Humans; Phosphorylation/drug effects; Protein Binding; Protein Conformation/drug effects; Synovial Fluid/chemistry

Search on Google

Add to My VHL

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Complement C3 / Complement C3a / Protein Serine-Threonine Kinases / Glycyrrhizic Acid / Glycyrrhetinic Acid Limits: Humans Language: En Journal: J Biochem Year: 2003 Document type: Article Affiliation country: Japan Country of publication: United kingdom

Search on Google

Add to My VHL

XML

PubMed Links