Purification and characterization of a 200 kDa fructosyllysine-specific binding protein from cell membranes of U937 cells.
Amadori-modified proteins are bound by macrophages and monocytes via fructosyllysine-specific receptors. Detergent extracts from U937 cell membranes were used to purify the binding proteins by affinity purification on glycated polylysine coated magnetic beads followed by SDS-PAGE. Two proteins of 200 and 100kDa were isolated. MS-analysis of the 200 kDa protein showed high homologies with cellular myosin heavy chain, type A. Both fructosyllysine specific binding proteins, cellular myosin heavy chain and nucleolin, are glycosylated.
Salazar
R
R
Institut für Medizinische Biochemie und Molekularbiologie, Ernst-Moritz-Arndt-Universität, Greifswald, Germany.
Brandt
R
R
Kellermann
J
J
Krantz
S
S
D000595:Amino Acid Sequence; D006031:Glycosylation; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D020409:Molecular Motor Proteins; D008969:Molecular Sequence Data; D018995:Myosin Heavy Chains / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D009687:Nuclear Proteins; D010750:Phosphoproteins / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D020298:U937 Cells; D000097796:Nucleolin
D008565:Membrane Proteins; D020409:Molecular Motor Proteins; D018995:Myosin Heavy Chains; D009687:Nuclear Proteins; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D000097796:Nucleolin; C103814:MYH9 protein, human; C093206:fructosyllysine-binding protein, human