Abstract
A mixture of low-molecular weight peptides was isolated from an inflammatory synovial fluid and fractionated by high performance liquid chromatography (HPLC). One fraction, capable of inhibiting lucigenin-enhanced chemiluminescence of activated neutrophils, was found to be the peptide H-Ala-Gly-Leu-Pro-Glu-Lys-Tyr-OH corresponding to amino acid residues 98-104 of SAA. Respective synthetic peptide, coeluted on HPLC with the natural fraction, was found to modulate superoxide anion production by activated human neutrophils. Related synthetic peptides were found to have modulatory effects. Taking together the fact that toxic free-radicals have been implicated as important pathological mediators of organ injury in a wide range of human diseases, and the fact that these diseases are usually associated with induction of acute phase response, modulatory effect of SAA-related peptides on superoxide release from PMNs, shed new light on the potential functional importance of SAA in a broad spectrum of clinical situations.
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© 1991 Springer Science+Business Media Dordrecht
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Levartowsky, D., Pras, M., Shephard, E., Rosen, O., Matifridkin (1991). Serum Amyloid A (SAA)-Related Peptide Isolated from Synovial Fluid Modulates Superoxide Production by Human Neutrophils.. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_34
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DOI: https://doi.org/10.1007/978-94-011-3284-8_34
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