Editorial: Serum amyloid A; in search of function

Amyloid

Volumn 9, Issue 4, 2002, Pages 276-278

  Schreiber, Barbara M ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; ANTIINFLAMMATORY AGENT; CYTOKINE; RECEPTOR; APOLIPOPROTEIN; SERUM AMYLOID A;

ACUTE PHASE RESPONSE; AMYLOIDOSIS; ATHEROSCLEROSIS; EDITORIAL; INFLAMMATION; LIPID METABOLISM; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; TRANSCRIPTION REGULATION; GENE EXPRESSION REGULATION; GENETICS; PHYSIOLOGY;

APOLIPOPROTEINS; GENE EXPRESSION REGULATION; SERUM AMYLOID A PROTEIN;

EID: 0036965638     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506120209114107     Document Type: Editorial

References (23)

1. Uhlar CM and Whitehead AS (1999). Serum amyloid A, the major vertebrate acute-phase reactant. Eur J Biochem 265, 501-523
2. Thorn CF and Whitehead AS (2002). Differential transcription of the mouse acute phase serum amyloid A genes in response to pro-inflammatory cytokines. Amyloid J Protein Folding Disord 9:229-236
3. Thorn CF and Whitehead AS (2002). Differential glucocorticoid enhancement of the cytokine-driven transcriptional activation of the human acute phase serum amyloid A genes, SAA1 and SAA2. J Immunol 169, 399-406
4. Ely S, Bonatesta R, Ancsin JB, Kindy M and Kisilevsky R (2001). The in-vitro influence of serum amyloid A isoforms on enzymes that regulate the balance between esterified and un-esterified cholesterol. Amyloid J Prot Fold Dis 8, 169-181
5. Schreiber BM, Veverbrants M, Fine RE, Blusztajn JK, Salmona M, Patel A and Sipe JD (1999). Apolipoprotein serum amyloid A (SAA) down-regulates smooth-muscle cell lipid biosynthesis. Biochem J 344, 7-13
6. Artl A, Marsche G, Lestavel S, Sattler W and Malle E (2000). Role of serum amyloid A during metabolism of acute-phase HDL by macrophages. Arterioscler Thromb Vasc Biol 20, 763-772
7. Urieli-Shoval S, Cohen P, Eisenberg S and Matzner Y (1998). Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium. J Histochem Cytochem 46, 1377-1384
8. Yavin EJ, Preciado-Patt L, Rosen O, Yaron M, Suessmuth RD, Levartowsky D, Jung G, Lider O and Fridkin M (2000). Serum amyloid A-derived peptides, present in human rheumatic synovial fluids, induce the secretion of interferon-γ human CD(4)(+) T-lymphocytes. FEBS Lett 472, 259-262
9. Badolato R, Wang JM, Stornello SL, Ponzi AN, Duse M and Musso T (2000). Serum amyloid A is an activator of PMN antimicrobial functions: induction of degranulation, phagocytosis, and enhancement of anti-Candida activity. J Leukoc Biol 67, 381-386
10. Olsson N, Siegbahn A and Nilsson G (1999). Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway. Biochem Biophys Res Commun 254, 143-146
11. Su SB, Gong W, Gao JL, Shen W, Murphy PM, Oppenheim JJ and Wang JM (1999). A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells. J Exp Med 189, 395-402
12. Liang TS, Wang JM, Murphy PM and Gao JL (2000). Serum amyloid A is a chemotactic agonist at FPR2, a low-affinity N-formylpeptide receptor on mouse neutrophils. Biochem Biophys Res Commun 270, 331-335
13. Le Y, Oppenheim JJ and Wang JM (2001). Pleiotropic roles of formyl peptide receptors. Cytokine Growth Factor Rev 12, 91-105
14. Urieli-Shoval S, Shubinsky G, Linke RP, Fridkin M, Tabi I and Matzner Y (2002). Adhesion of human platelets to serum amyloid A. Blood 99, 1224-1229
15. Walder K, Kantham L, McMillan JS, Trevaskis J, Kerr L, De Silva A, Sunderland T, Godde N, Gao Y, Bishara N, Windmill K, Tenne-Brown J, Augert G, Zimmet PZ and Collier GR (2002). Tanis: a link between type 2 diabetes and inflammation? Diabetes 51, 1859-1866
16. Mendoza LM, Villaflor G, Eden P, Roopenian D and Shastri N (2001). Distinguishing self from nonself: immunogenicity of the murine H47 locus is determined by a single amino acid substitution in an unusual peptide. J Immunol 166, 4438-4445
17. Shainkin-Kestenbaum R, Zimlichman S, Lis M, Preciado-Patt L, Fridkin M and Berenheim J (1996-97). Modulation of prostaglandin I2 production from bovine aortic endothelial cells by serum amyloid A and its N-terminal tetradecapeptide. Biomed Pept Proteins Nucleic Acids 2, 101-106
18. Hosoai H, Webb NR, Glick JM, Tietge UJ, Purdom MS, deBeer FC and Rader DJ (1999). Expression of serum amyloid A protein in the absence of the acute phase response does not reduce HDL cholesterol or apoA-I levels in human apoA-I transgenic mice. J Lipid Res 40, 648-653
19. Ridker PM, Rifai N, Pfeffer MA, Sacks FM, Moye LA, Goldman S, Flaker GC and Braunwald E (1998). Inflammation, pravastatin, and the risk of coronary events after myocardial infarction in patients with average cholesterol levels. Cholesterol and Recurrent Events (CARE) Investigators. Circulation 98, 839-844
20. Hirakura Y, Carreras I, Sipe JD and Kagan BL (2002). Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense. Amyloid J Prot Fold Dis 9, 13-23
21. Liang JS and Sipe JD (1995). Recombinant human serum amyloid A (apoSAAp) binds cholesterol and modulates cholesterol flux. J Lipid Res 36, 37-46
22. Ancsin JB and Kisilevsky R (1997). Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A. J Biol Chem 272, 406-413
23. Ancsin JB and Kisilevsky R. The heparin/heparan sulfate-binding site on apo-serum amyloid A (1999). Implications for the therapeutic intervention of amyloidosis. J Biol Chem 274, 7172-7181