Serum amyloid A‐derived peptides, present in human rheumatic synovial fluids, induce the secretion of interferon‐γ by human CD4+ T‐lymphocytes
- 27 April 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 472 (2-3) , 259-262
- https://doi.org/10.1016/s0014-5793(00)01470-8
Abstract
Serum amyloid A (SAA) is a major acute-phase protein whose biochemical functions remain largely obscure. Human rheumatic synovial fluids were screened by high performance liquid chromatography mass spectrometry for SAA-derived peptides, specifically the sequence AGLPEKY (SAA(98-104)) which was previously shown to modulate various leukocyte functions. Two such fluids were found to contain a truncated version of SAA(98-104). Synthetic SAA(98-104) and several of its analogs were shown capable of binding isolated human CD(4)(+) T-lymphocytes and stimulating them to produce interferon-gamma. Given the high acute-phase serum level of SAA and its massive proteolysis by inflammatory related enzymes, SAA-derived peptides may be involved in host defense mechanisms.Keywords
This publication has 12 references indexed in Scilit:
- Apolipoprotein A-I and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesisPublished by Elsevier ,2002
- Peptides derived from human C‐reaetive protein inhibit the enzymatic activities of human leukocyte elastase and cathepsin G: use of overlapping peptide sequences to identify a unique inhibitorChemical Biology & Drug Design, 1998
- Cathepsin B Generates the Most Common Form of Amyloid A (76 Residues) as a Degradation Product from Serum Amyloid AScandinavian Journal of Immunology, 1995
- Inhibition of cell adhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid AEuropean Journal of Biochemistry, 1994
- Neutrophil association and degradation of normal and acute-phase high-density lipoprotein 3Biochemical Journal, 1987
- Degradation of serum amyloid A and apolipoproteins by serum proteasesBiochemistry, 1984
- Plasma clearance kinetics of the amyloid-related high density lipoprotein apoprotein, serum amyloid protein (apoSAA), in the mouse. Evidence for rapid apoSAA clearance.Journal of Clinical Investigation, 1983
- Degradation of Amyloid Proteins by Different Serine ProteasesScandinavian Journal of Immunology, 1981
- Elastase-type proteases on the surface of human blood monocytes: possible role in amyloid formation.The Journal of Immunology, 1980
- Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes.The Journal of Experimental Medicine, 1978