Acute phase serum amyloid A (SAA) and cholesterol transport during acute inflammation: A hypothesis

Amyloid

Volumn 3, Issue 4, 1996, Pages 252-260

  Kisilevsky, Robert ^a   Lindhorst, Elaine ^a   Ancsin, John B ^a   Young, Dorothy ^a   Bagshaw, William ^a  

^a QUEEN S UNIVERSITY   (Canada)

Author keywords

Acute inflammation; Cholesterol transport; SAA

Indexed keywords

EID: 1842530792     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.3109/13506129609014373     Document Type: Article

References (59)

1. Lowell CA, Potter DA, Stearman RS and Morrow JF (1986). Structure of the murine serum amyloid A gene family. Gene conversion. J Biol Chem 261, 8442-8452
2. Benditt EP and Meek RL (1989). Expression of the third member of the serum amyloid A gene family in mouse adipocytes. J Exp Med 169, 1841-1846
3. Rokita H, Shirahama T, Cohen AS, Meek RL, Benditt EP and Sipe JD (1987). Differential expression of the amyloid SAA gene in liver and peritoneal macrophages of mice undergoing dissimilar inflammatory episodes. J Immunol 139, 3849-3853
4. Sipe JD (1995). Serum amyloid A protein classification: A preliminary report of a subcommittee of the International Society of Amyloidosis. Amyloid 2, 69-70
5. Whitehead AS, de Beer MC, Steel DM, Rits M, Lelias JM, Lane WS and de Beer FC (1992). Identification of novel members of the serum amyloid-A protein superfamily as constitutive apolipoproteins of high density lipoprotein. J Biol Chem 267, 3862-3867
6. Meek RL, Eriksen N and Benditt EP (1992). Murine serum amyloid-A(3) is a high density apolipoprotein and is secreted by macrophages. Proc Natl Acad Sci USA 89, 7949-7952
7. Urieli-Shoval S, Meek RL, Hanson RH, Eriksen N and Benditt EP (1994). Human serum amyloid a genes are expressed in monocyte/macrophage cell lines. Amer J Pathol 145, 650-660
8. Kushner I and Rzewnicki DL (1994). The acute phase response: general aspects. In Husby G (ed.) Clinical Rheumatology: Vol.8 No.3, Reactive Amyloidosis and the Acute Phase Response pp. 513-530. (London: Bailliere Tindall)
9. Edbrooke MR, Burt DW, Cheshire JK and Woo P (1989). Identification of cis-acting sequences responsible for phorbol ester induction of human serum amyloid A gene expression via a nuclear factor kB-like transcription factor. Mol Cell Biol 9, 1908-1916
10. Edbrooke MR, Foldi J, Cheshire JK, Li F, Faulkes DJ and Woo P (1991). Constitutive and NF-kappaB Like Proteins in the Regulation of the Serum Amyloid-A Gene by Interleukin-1. Cytokine 3, 380-388
11. Betts JC, Cheshire JK, Akira S, Kishimoto T and Woo P (1993). The Role of NF-kappa B and NF-IL6 Transactivating factors in the synergistic activation of human serum amyloid-A gene expression by interleukin-1 and interleukin-6. J Biol Chem 268, 25624-25631
12. Ray A and Ray BK (1994). Serum amyloid A gene expression under acute-phase conditions involves participation of inducible C/EBP-beta and C/EBP-delta and their activation by phosphorylation. Mol Cell Biol 14, 4324-4332
13. Brissette L, Young I, Narindrasorasak S, Kisilevsky R and Deeley R (1989). Differential induction of the serum amyloid-A gene family in response to an inflammatory agent and to amyloid-enhancing factor. J Biol Chem 264, 19327-19332
14. Morrow JF, Stearman RS, Peltzman CG and Potter DA (1981). Induction of hepatic synthesis of serum amyloid A protein and actin. Proc Natl Acad Sci USA 78, 4718-4722
15. McAdam KPWJ and Sipe JD (1976). Murine model for human secondary amyloidosis: genetic variability of the acute-phase serum protein SAA response to endotoxins and casein. J Exp Med 144, 1121-1127
16. McAdam KPWJ, Elin RJ, Sipe JD and Wolff SM (1978). Changes in human serum amyloid-A and C-reactive protein after etiocholanolone-induced inflammation. J Clin Invest 61, 390-394
17. Kisilevsky R, Boudreau L and Foster D (1983). Kinetics of amyloid deposition. II. The effects of dimethylsulfoxide and colchicine therapy. Lab Invest 48, 60-67
18. van der Westhuyzen DR, Coetzee GA and de Beer FC (1986). Serum amyloid A protein in plasma: characteristics of acute phase HDL. In Marrink J and Van Rijswijk MH (eds.) Amyloidosis pp. 115-125. (Martinus Nijhoff, Dordrecht)
19. Benson MD and Aldo-Benson MA (1982). SAA suppression of immune response in vitro: evidence for an effect on T cell-macrophage interaction. J Immunol 128, 2390-2392
20. Benson MD, Aldo-Benson MA, Shirahama T, Borel Y and Cohen AS (1975). Suppression of in vitro antibody response by a serum factor (SAA) in experimentally induced amyloidosis. J Exp Med 142, 236-241
21. Benson MD and Aldo-Benson M (1979). Effect of purified protein SAA on immune response in vitro: mechanisms of suppression. J Immunol 122, 2077-2082
22. 2-microglobulin-like proteins. Science 243, 655-656
23. Sack GH and Talbot CC (1989). The Human Serum Amyloid-A (SAA)-Encoding Gene Gsaal-nucleotide sequence and possible autocrine-collagenase-inducer function. Gene 84, 509-515
24. Mitchell TI, Coon CI and Brinckerhoff CE (1991). Serum amyloid-A (SAA3) produced by rabbit synovial fibroblasts treated with phorbol esters or interleukin-1 induces synthesis of collagenase and is neutralized with specific antiserum. J Clin Invest 87, 1177-1185
25. Mitchell TI, Jeffrey JJ, Palmiter RD and Brinckerhoff CE (1993). The acute phase reactant serum amyloid-A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin. Biochim Biophys Acta 1156, 245-254
26. Linke RP, Bock V, Valet G and Rothe G (1991). Inhibition of the oxidative burst response of N-formyl peptide-stimulated neutrophils by serum amyloid-A protein. Biochem Biophys Res Commun 176, 1100-1105
27. Badolato R, Wang JM, Murphy WJ, Lloyd AR, Michiel DF, Bausserman LL, Kelvin DJ and Oppenheim JJ (1994). Serum amyloid A is a chemoattractant: Induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 180, 203-209
28. Preciado-Patt L, Hershkoviz R, Fridkin M and Lider O (1996). Serum amyloid A binds specific extracellular matrix glycoproteins and induces the adhesion of resting CD4(+) T cells. J Immunol 156, 1189-1195
29. Goldfarb D, Nathan I, Dvilansky A, Khoda G and Shainkin-Kestenbaum R (1991). Modulation of transformed cells by serum amyloid-A interaction with TPA. Cancer J 4, 35-38
30. Preciado-Patt L, Levartowsky D, Pras M, Hershkoviz R, Lider O and Fridkin M (1994). Inhibition of cell adhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid A - Toward understanding the physiological role of an enigmatic protein. Eur J Biochem 223, 35-42
31. Assmann G and Funke H (1990). HDL Metabolism and Atherosclerosis. J Cardiovasc Pharmacol 16, S15-S20
32. Vanlenten BJ, Hama SY, de Beer FC, Stafforini DM, Mcintyre TM, Prescott SM, Ladu BN, Fogelman AM and Navab M (1995). Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response - Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures. J Clin Invest 96, 2758-2767
33. Steinmetz A, Hocke G, Saile R, Puchois P and Fruchart JC. (1989). Influence of serum amyloid-A on cholesterol esterification in human plasma. Biochim Biophys Acta 1006, 173-178
34. Fielding CJ and Fielding PE (1995). Molecular physiology of reverse cholesterol transport - Review. J Lipid Res 36, 211-228
35. Parks JS, Li H, Gebre AK, Smith TL and Maeda N (1995). Effect of apolipoprotein A-I deficiency on lecithin: cholesterol acyltransferase activation in mouse plasma. J Lipid Res 36, 349-355
36. Husby G, Marhaug G, Dowton B, Sletten K and Sipe JD (1994). Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid Int J Exp Clin Invest 1, 118-137
37. Marhaug G and Dowton SB (1994). Serum amyloid A: An acute phase apolipoprotein and the precursor of AA amyloid. In Husby G (ed.) Clinical Rheumatology: Vol.8 No.3, Reactive Amyloidosis and the Acute Phase Response pp. 553-573. (London: Bailliere Tindall)
38. Ericsson LH, Eriksen N, Walsh KA and Benditt EP (1987). Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor. FEBS Lett 218, 11-16
39. Syversen PV, Juul J, Marhaug G, Husby G and Sletten K (1994). The primary structure of serum amyloid-A protein in the sheep -comparison with serum amyloid-A in other species. Scand J Immunol 39, 88-94
40. Fantone JC and Ward PA (1994). Inflammation. In Rubin E and Farber J (eds.) Pathology pp. 32-67. (Philadelphia: Lippincott)
41. Macchia T, Mancinelli R, Barbini DA, Taggi F, Avico U and Cantafora A (1991). Determination of membrane cholesterol in normal and pathological red blood cells. Clin Chim Acta 199, 59-67
42. Cooper RA (1978). Influence of increased membrane cholesterol on membrane fluidity and cell function in human red blood cells. J Supramol Struct 8, 413-430
43. Mindham MA and Mayes PA (1991). Reverse cholesterol transport in the rat - studies using the isolated perfused spleen in conjunction with the perfused liver. Biochem J 279, 503-508
44. Glomset JA (1968). The plasma lecithin:cholesterol acyltransferase reaction. J Lipid Res 9, 155-167
45. Mindham MA and Mayes PA (1994). Application of simultaneous spleen and liver perfusion to the study of reverse cholesterol transport. Biochem J 302, 207-213
46. Mindham MA, Mayes PA and Miller NE (1990). Reverse cholesterol transport in the isolated perfused rat spleen. Biochem J 268, 499-505
47. Jiao S, Cole TG, Kitchens RT, Pfleger B and Shonfeld G (1990). Genetic heterogeneity of lipoproteins in inbred strains of mice: analysis by gel permeation chromatography. Metabolism 39, 155-160
48. Kisilevsky R and Subrahmanyan L (1992). Serum amyloid A changes high density lipoprotein's cellular affinity: a clue to serum amyloid A's principal function. Lab Invest 66, 778-785
49. Banka CL, Yuan T, de Beer MC, Kindy M, Curtiss LK and de Beer FC (1995). Serum amyloid A (SAA): Influence on HDL-mediated cellular cholesterol efflux. J Lipid Res 36, 1058-1065
50. Elliott-Bryant R, Sipe JD, Gonnerman WA, Newcombe D and Cathcart ES (1994). In-vitro clearance of HDL associated SAA by resident peritoneal cells from CBA/J mice. In Kisilevsky R, Benson MD, Frangione B, Gauldie J, Muckle TJ and Young ID (eds.) Amyloid and Amyloidosis 1993 pp. 119-121. (Pearl River, NY: Parthenon Publishing Group Inc.)
51. Lavie G, Zucker-Franklin D and Franklin EC (1978). Degradation of serum amyloid A protein by surface associated enzymes of human blood monocytes. J Exp Med 148, 1020-1031
52. Lavie G, Zucker-Franklin D and Franklin EC (1980). Elastase-type proteases on the surface of human blood monocytes possible role in amyloid formation. J Immunol 125, 175-180
53. Yamada T, Liepnieks JJ, Kluve-Beckerman B and Benson MD (1995). Cathepsin B generates the most common form of amyloid A (76 residues) as a degradation product from serum amyloid A. Scand J Immunol 41, 94-97
54. Yamada T, Kluve-Beckerman B, Liepnieks JJ and Benson MD (1995). In vitro degradation of serum amyloid A by Cathepsin D and other acid proteases: Possible protection against amyloid fibril formation. Scand J Immunol 41, 570-574
55. Mayes PA (1993). Cholesterol synthesis, transport, and excretion. In Murray RK, Granner DK, Mayes PA and Rodwell VW (eds.) Harper's Biochemistry pp. 266-278. (Norwalk, Conn: Appleton & Lange)
56. Liang JS, and Sipe JD (1995). Recombinant human serum amyloid A [apoSAA(p)] binds cholesterol and modulates cholesterol flux. J Lipid Res 36, 526-533
57. Liang HQ, Rye KA and Barter PJ (1995). Cycling of apolipoprotein A-I between lipid-associated and lipid-free pools. Biochim Biophys Acta 1257, 31-37
58. Meek RL and Benditt EP (1989). Rat tissues express serum amyloid A protein-related mRNAs. Proc Nat Acad Sci USA 86, 1890-1894
59. Kisilevsky R and Subrahmanyan L (1994). Serum amyloid A influences the efflux of cholesterol from macrophages. In Kisilevsky R, Benson MD, Frangione B, Gauldie J, Muckle TJ and Young ID (eds.) Amyloid and Amyloidosis 1993 pp. 115-118. (Park Ridge, New Jersey: The Parthenon Publishing Group)