Phosphorylation of human serum amyloid A protein by protein kinase C
| Autor: | M L Vandenplas, Andre E. Nel, A F Strachan, M.C. De Beer, E G Shephard, F C de Beer |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1988 |
| Předmět: |
animal diseases
Biochemistry Peptide Mapping MAP2K7 Cell Line hemic and lymphatic diseases Humans Protein phosphorylation Serum amyloid A Amino Acids Phosphorylation Protein kinase A Molecular Biology Serum Amyloid A Protein Protein kinase C Protein Kinase C Chemistry Cell Biology stomatognathic diseases Apolipoproteins lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Isoelectric Focusing Lipoprotein Research Article |
| Popis: | Monokine-induced hepatic secretion of serum amyloid A protein (apo-SAA), an acute-phase reactant, is followed by rapid association with high-density lipoprotein (HDL) in plasma. Plasma clearance of apo-SAA is more rapid than any of the other HDL apolipoproteins. It has been shown that, of the acute-phase HDL3 apolipoproteins, apo-SAA preferentially associates with neutrophil membranes. HDL apolipoproteins have been shown to activate protein kinase C in endothelial cells. We therefore investigated potential phosphorylation of HDL3 apolipoproteins by protein kinase C. Apo-SAA was the only apolipoprotein phosphorylated (Km = 12 mM). Phosphorylation of the apo-SAA-containing HDL3 particle was selective for the more basic isoforms of apo-SAA (pI 7.0, 7.4, 7.5 and 8.0), with more acidic isoforms being phosphorylated when delipidated acute-phase apolipoproteins were used as substrate. However, phosphorylation was not in itself responsible for the establishment of the apo-SAA isoforms. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|