nach oben

Current Atherosclerosis Reports

Erschienen in:

01.11.2020 | Vascular Biology (J. Hamilton, Section Editor)

Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve

verfasst von: Olga Gursky

Erschienen in: Current Atherosclerosis Reports | Ausgabe 11/2020

Einloggen, um Zugang zu erhalten

Abstract

Purpose of Review

This review addresses normal and pathologic functions of serum amyloid A (SAA), an enigmatic biomarker of inflammation and protein precursor of AA amyloidosis, a life-threatening complication of chronic inflammation. SAA is a small, highly evolutionarily conserved acute-phase protein whose plasma levels increase up to one thousand-fold in inflammation, infection, or after trauma. The advantage of this dramatic but transient increase is unclear, and the complex role of SAA in immune response is intensely investigated. This review summarizes recent advances in our understanding of the structure-function relationship of this intrinsically disordered protein, outlines its newly emerging beneficial roles in lipid transport and inflammation control, and discusses factors that critically influence its misfolding in AA amyloidosis.

Recent Findings

High-resolution structures of lipid-free SAA in crystals and fibrils have been determined by x-ray crystallography and electron cryo-microscopy. Low-resolution structural studies of SAA-lipid complexes, together with biochemical, cell-based, animal model, genetic, and clinical studies, have provided surprising new insights into a wide range of SAA functions. An emerging vital role of SAA is lipid encapsulation to remove cell membrane debris from sites of injury. The structural basis for this role has been proposed. The lysosomal origin of AA amyloidosis has solidified, and its molecular and cellular mechanisms have emerged.

Summary

Recent studies have revealed molecular underpinnings for understanding complex functions of this Cambrian protein in lipid transport, immune response, and amyloid formation. These findings help guide the search for much-needed targeted therapies to block the protein deposition in AA amyloidosis.

• Ye RD, Sun L. Emerging functions of serum amyloid A in inflammation. J Leukoc Biol. 2015;98(6):923–9 A superb review of diverse functions of SAA in inflammatory diseases.PubMedPubMedCentral

Zhang Y, Zhang J, Sheng H, Li H, Wang R. Acute phase reactant serum amyloid A in inflammation and other diseases. Adv Clin Chem. 2019;90:25–80.PubMed

• Westermark GT, Fändrich M, Westermark P. AA amyloidosis: pathogenesis and targeted therapy. Annu Rev Pathol. 2015;10:321–44 An excellent comprehensive review of clinical, cellular and molecular aspects of AA amyloidosis.PubMed

Papa R, Lachmann HJ. Secondary, AA, amyloidosis. Rheum Dis Clin N Am. 2018;44(4):585–603.

Perez L. Acute phase protein response to viral infection and vaccination. Arch Biochem Biophys. 2019;671:196–202.PubMedPubMedCentral

Abouelasrar Salama S, Lavie M, De Buck M, Van Damme J, Struyf S. Cytokines and serum amyloid A in the pathogenesis of hepatitis C virus infection. Cytokine Growth Factor Rev. 2019;50:29–42.PubMed

• Lee JW, Stone ML, Porrett PM, Thomas SK, Komar CA, Li JH, et al. Hepatocytes direct the formation of a pro-metastatic niche in the liver. Nature. 2019;567(7747):249–52 This study combines cell-based, genetic and mouse model studies to show that signaling via the interleukin-6 – STAT3 – SAA complex is central to the spread of tumor cells in the liver. Blocking this signaling inhibits metastatic disease and provides a potential therapeutic target.PubMedPubMedCentral

Xie N, Li Z, Zuo R, Qi S, Zhu T, Liu L, et al. Serum SAA1 and APOE are novel indicators for human cytomegalovirus infection. Sci Rep. 2017;7(1):13407.PubMedPubMedCentral

Todorov I, Gospodinova M, Bocheva Y, Popcheva G. Serum amyloid A protein in the course of infectious mononucleosis. Ther Adv Infect Dis. 2019;6:2049936118811208.PubMedPubMedCentral

10.

Li H, Xiang X, Ren H, Xu L, Zhao L, Chen X, et al. Serum Amyloid A is a biomarker of severe coronavirus disease and poor prognosis. J Inf Secur. 2020:S0163–4453(20)30162–30166.

11.

McKay PF, Cizmeci D, Aldon Y, Maertzdorf J, Weiner J, Kaufmann SH, et al. Identification of potential biomarkers of vaccine inflammation in mice. Elife. 2019;8:e46149.PubMedPubMedCentral

12.

Sanada Y, Yamamoto T, Satake R, Yamashita A, Kanai S, Kato N, et al. Serum amyloid A3 gene expression in adipocytes is an indicator of the interaction with macrophages. Sci Rep. 2016;6:38697.PubMedPubMedCentral

13.

Ather JL, Dienz O, Boyson JE, Anathy V, Amiel E, Poynter ME. Serum Amyloid A3 is required for normal lung development and survival following influenza infection. Sci Rep. 2018;8(1):16571.PubMedPubMedCentral

14.

Kisilevsky R, Manley PN. Acute-phase serum amyloid A: perspectives on its physiological and pathological roles. Amyloid. 2012;19(1):5–14.PubMed

15.

Vaisar T, Tang C, Babenko I, Hutchins P, Wimberger J, Suffredini AF, et al. Inflammatory remodeling of the HDL proteome impairs cholesterol efflux capacity. J Lipid Res. 2015;56(8):1519–30.PubMedPubMedCentral

16.

Han CY, Tang C, Guevara ME, Wei H, Wietecha T, Shao B, et al. Serum amyloid A impairs the antiinflammatory properties of HDL. J Clin Invest. 2016;126(1):266–81.PubMed

17.

Zewinger S, Drechsler C, Kleber ME, Dressel A, Riffel J, Triem S, et al. Serum amyloid A: high-density lipoproteins interaction and cardiovascular risk. Eur Heart J. 2015;36(43):3007–16.PubMed

18.

Thompson JC, Jayne C, Thompson J, Wilson PG, Yoder MH, Webb N, et al. A brief elevation of serum amyloid A is sufficient to increase atherosclerosis. J Lipid Res. 2015;56(2):286–93.PubMedPubMedCentral

19.

McEneny J, McKavanagh P, York E, Nadeem N, Harbinson M, Stevenson M, et al. Serum- and HDL3-serum amyloid A and HDL3-LCAT activity are influenced by increased CVD-burden. Atherosclerosis. 2016;244:172–8.PubMed

20.

Getz GS, Krishack PA, Reardon CA. Serum amyloid A and atherosclerosis. Curr Opin Lipidol. 2016;27(5):531–5.PubMed

21.

Getz GS, Reardon CA, Apoproteins E. A-I, and SAA in macrophage pathobiology related to atherogenesis. Front Pharmacol. 2019;10:536.PubMedPubMedCentral

22.

Thompson JC, Wilson PG, Shridas P, Ji A, de Beer M, de Beer FC, et al. Serum amyloid A3 is pro-atherogenic. Atherosclerosis. 2018;268:32–5.PubMed

23.

• Shridas P, Tannock LR. Role of serum amyloid A in atherosclerosis. Curr Opin Lipidol. 2019;30(4):320–5 A comprehensive review summarizing mounting evidence that SAA is a causative risk factor for atherosclerosis.PubMedPubMedCentral

24.

De Buck M, Gouwy M, Wang JM, Van Snick J, Opdenakker G, Struyf S, et al. Structure and expression of different serum amyloid A (SAA) variants and their concentration-dependent functions during host insults. Curr Med Chem. 2016a;23(17):1725–55.PubMedPubMedCentral

25.

Sun L, Ye RD. Serum amyloid A1: structure, function and gene polymorphism. Gene. 2016;583(1):48–57.PubMedPubMedCentral

26.

• Sack GH Jr. Serum amyloid A - a review. Mol Med. 2018;24(1):46 An interesting and timely review of SAA functions.PubMedPubMedCentral

27.

Sack GH Jr. Serum amyloid a (SAA) proteins. Subcell Biochem. 2020;94:421–36.PubMed

28.

Kim MH, de Beer MC, Wroblewski JM, Charnigo RJ, Ji A, Webb NR, et al. Impact of individual acute phase serum amyloid A isoforms on HDL metabolism in mice. J Lipid Res. 2016;57(6):969–79.PubMedPubMedCentral

29.

• Tannock LR, De Beer MC, Ji A, Shridas P, Noffsinger VP, den Hartigh L, et al. Serum amyloid A3 is a high density lipoprotein-associated acute-phase protein. J Lipid Res. 2018;59(2):339–47 This study reveals functional importance of murine SAA3.PubMed

30.

Jumeau C, Awad F, Assrawi E, Cobret L, Duquesnoy P, Giurgea I, et al. Expression of SAA1, SAA2 and SAA4 genes in human primary monocytes and monocyte-derived macrophages. PLoS One. 2019;14(5):e0217005.PubMedPubMedCentral

31.

Wilson PG, Thompson JC, Shridas P, McNamara PJ, de Beer MC, de Beer FC, et al. Serum amyloid A is an exchangeable apolipoprotein. Arterioscler Thromb Vasc Biol. 2018;38(8):1890–900.PubMedPubMedCentral

32.

• Ji A, Wang X, Noffsinger VP, Jennings D, de Beer MC, de Beer FC, et al. Serum amyloid A is not incorporated into HDL during HDL biogenesis. J Lipid Res. 2020;61(3):328–37 Analysis of protein lipidation by hepatocytes shows that SAA transiently forms nascent lipoproteins that are distinct from the apoA-I-containing plasma HDL.PubMed

33.

De Buck M, Gouwy M, Wang JM, Van Snick J, Proost P, Struyf S, et al. The cytokine-serum amyloid A-chemokine network. Cytokine Growth Factor Rev. 2016b;30:55–69.PubMed

34.

Thaler R, Sturmlechner I, Spitzer S, Riester SM, Rumpler M, Zwerina J, et al. Acute-phase protein serum amyloid A3 is a novel paracrine coupling factor that controls bone homeostasis. FASEB J. 2015;29(4):1344–59.PubMed

35.

Kim J, Yang J, Park OJ, Kang SS, Yun CH, Han SH. Serum amyloid A inhibits osteoclast differentiation to maintain macrophage function. J Leukoc Biol. 2016;99(4):595–603.PubMed

36.

Choudhary S, Goetjen A, Estus T, Jacome-Galarza CE, Aguila HL, Lorenzo J, et al. Serum amyloid A3 secreted by preosteoclasts inhibits parathyroid hormone-stimulated cAMP signaling in murine osteoblasts. J Biol Chem. 2016;291(8):3882–94.PubMed

37.

Choudhary S, Santone E, Yee SP, Lorenzo J, Adams DJ, Goetjen A, et al. Continuous PTH in male mice causes bone loss because it induces serum amyloid. Endocrinology. 2018;159(7):2759–76.PubMedPubMedCentral

38.

Jayaraman S, Haupt C, Gursky O. Paradoxical effects of SAA on lipoprotein oxidation suggest a new antioxidant function for SAA. J Lipid Res. 2016;57(12):2138–49.PubMedPubMedCentral

39.

Sato M, Ohkawa R, Yoshimoto A, Yano K, Ichimura N, Nishimori M, et al. Effects of serum amyloid A on the structure and antioxidant ability of high-density lipoprotein. Biosci Rep. 2016;36(4):e00369.PubMedPubMedCentral

40.

Zhu S, Wang Y, Chen W, Li W, Wang A, Wong S, et al. High-density lipoprotein (HDL) counter-regulates serum amyloid A (SAA)-induced sPLA2-IIE and sPLA2-V expression in macrophages. PLoS One. 2016;11(11):e0167468.PubMedPubMedCentral

41.

Shridas P, De Beer MC, Webb NR. High-density lipoprotein inhibits serum amyloid A-mediated reactive oxygen species generation and NLRP3 inflammasome activation. J Biol Chem. 2018;293(34):13257–69.PubMedPubMedCentral

42.

Dieter BP, Meek RL, Anderberg RJ, Cooney SK, Bergin JL, Zhang H, et al. Serum amyloid A and Janus kinase 2 in a mouse model of diabetic kidney disease. PLoS One. 2019;14(2):e0211555.PubMedPubMedCentral

43.

Yu J, Zhu H, Taheri S, Mondy W, Bonilha L, Magwood GS, et al. Serum amyloid A-mediated inflammasome activation of microglial cells in cerebral ischemia. J Neurosci. 2019;39(47):9465–76.PubMedPubMedCentral

44.

• Lee JY, Hall JA, Kroehling L, Wu L, Najar T, Nguyen HH, et al. Serum amyloid A proteins induce pathogenic Th17 cells and promote inflammatory disease. Cell. 2020;180(1):79–91 This mouse model study shows that SAA1, SAA2 and SAA3 have distinct functions in promoting T-helper cell-mediated inflammation in synergy with STAT3-activating cytokines. It suggests that SAA-modulated T-cell signaling pathways provide targets for anti-inflammatory therapies.PubMed

45.

Linke RP, Meinel A, Chalcroft JP, Urieli-Shoval S. Serum amyloid A (SAA) treatment enhances the recovery of aggravated polymicrobial sepsis in mice, whereas blocking SAA’s invariant peptide results in early death. Amyloid. 2017;24(S1):149–50.PubMed

46.

Cheng N, Liang Y, Du X, Ye RD. Serum amyloid A promotes LPS clearance and suppresses LPS-induced inflammation and tissue injury. EMBO Rep. 2018;19(10):e45517.PubMedPubMedCentral

47.

Murdoch CC, Espenschied ST, Matty MA, Mueller O, Tobin DM, Rawls JF. Intestinal serum amyloid A suppresses systemic neutrophil activation and bactericidal activity in response to microbiota colonization. PLoS Pathog. 2019;15(3):e1007381.PubMedPubMedCentral

48.

• Zheng H, Li H, Zhang J, Fan H, Jia L, Ma W, et al. Serum amyloid A exhibits pH dependent antibacterial action and contributes to host defense against Staphylococcus aureus cutaneous infection. J Biol Chem. 2020;295(9):2570–81.PubMed

49.

Sun L, Zhou H, Zhu Z, Yan Q, Wang L, Liang Q, et al. Ex vivo and in vitro effect of serum amyloid a in the induction of macrophage M2 markers and efferocytosis of apoptotic neutrophils. J Immunol. 2015;194(10):4891–900.PubMedPubMedCentral

50.

• Burgess EJ, Hoyt LR, Randall MJ, Mank MM, Bivona JJ 3rd, Eisenhauer PL, et al. Bacterial lipoproteins constitute the TLR2-stimulating activity of serum amyloid A. J Immunol. 2018;201(8):2377–84 This study helps resolve some discrepancies related to pro-inflammatory effect of SAA on TLR2, which the authors attribute to bacterial contamination of commercial protein preparations.PubMedPubMedCentral

51.

Smole U, Kratzer B, Pickl WF. Soluble pattern recognition molecules: guardians and regulators of homeostasis at airway mucosal surfaces. Eur J Immunol. 2020;50(5):624–42.PubMedPubMedCentral

52.

• Derebe MG, Zlatkov CM, Gattu S, Ruhn KA, Vaishnava S, Diehl GE, et al. Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection. Elife. 2014;3:e03206 High-resolution x-ray crystal structure of murine SAA3 reveals a molecular fold similar to that in human SAA1, suggesting that this unusual fold with a water-filled interior has been evolutionarily conserved. The results show that SAA binds retinol and suggest that helix h3 mediates the binding.PubMedPubMedCentral

53.

• Hu Z, Bang YJ, Ruhn KA, Hooper LV. Molecular basis for retinol binding by serum amyloid A during infection. Proc Natl Acad Sci U S A. 2019;116(38):19077–82 A high-resolution x-ray crystal structure shows a retinol molecule bond in a hydrophobic cavity formed by helices h1 and h3 from three molecules of murine SAA3. This is the first atomic structure of SAA in complex with a lipophilic molecule.PubMedPubMedCentral

54.

Gattu S, Bang YJ, Pendse M, Dende C, Chara AL, Harris TA, et al. Epithelial retinoic acid receptor β regulates serum amyloid A expression and vitamin A-dependent intestinal immunity. Proc Natl Acad Sci U S A. 2019;116(22):10911–6.PubMedPubMedCentral

55.

Murakami T, Inoshima Y, Ishiguro N. Systemic AA amyloidosis as a prion-like disorder. Virus Res. 2015;207:76–81.PubMed

56.

Gaffney PM. Amyloid A amyloidosis. Vet Pathol. 2017;54(1):5–8.PubMed

57.

Nuvolone M, Merlini G. Systemic amyloidosis: novel therapies and role of biomarkers. Nephrol Dial Transplant. 2017;32(5):770–80.PubMed

58.

• Frame NM, Gursky O. Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks. FEBS Lett. 2016;590(6):866–79 Amino-acid sequence analysis of the SAA protein family is combined with the crystal structures of hSAA1 and mSAA3 to propose that SAA binds HDL via a concave hydrophobic surface formed by evolutionarily conserved helices h1 and h3. SAA is proposed to act as an intrinsically disordered protein hub in inflammation signaling.PubMedPubMedCentral

59.

Colón W, Aguilera JJ, Srinivasan S. Intrinsic stability, oligomerization, and amyloidogenicity of HDL-free serum amyloid A. Adv Exp Med Biol. 2015;855:117–34.PubMed

60.

Uversky VN. Dancing protein clouds: the strange biology and chaotic physics of intrinsically disordered proteins. J Biol Chem. 2016;291(13):6681–8.PubMedPubMedCentral

61.

Weng J, Wang W. Dynamic multivalent interactions of intrinsically disordered proteins. Curr Opin Struct Biol. 2019;62:9–13.PubMed

62.

Macossay-Castillo M, Marvelli G, Guharoy M, Jain A, Kihara D, Tompa P, et al. The balancing act of intrinsically disordered proteins: enabling functional diversity while minimizing promiscuity. J Mol Biol. 2019;431(8):1650–70.PubMedPubMedCentral

63.

Takase H, Furuchi H, Tanaka M, Yamada T, Matoba K, Iwasaki K, et al. Characterization of reconstituted high-density lipoprotein particles formed by lipid interactions with human serum amyloid A. Biochim Biophys Acta. 2014;1842(10):1467–74.PubMed

64.

Jayaraman S, Haupt C, Gursky O. Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL. J Lipid Res. 2015;56(8):1531–42.PubMedPubMedCentral

65.

Frame NM, Jayaraman S, Gantz DL, Gursky O. Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: a hypothetical function of SAA as a "molecular mop" in immune response. J Struct Biol. 2017;200(3):293–302.PubMedPubMedCentral

66.

Jayaraman S, Gantz DL, Haupt C, Fändrich M, Gursky O. Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner. Chem Commun. 2018;54(28):3532–5.

67.

Takase H, Tanaka M, Nakamura Y, Morita SY, Yamada T, Mukai T. Effects of lipid composition on the structural properties of human serum amyloid A in reconstituted high-density lipoprotein particles. Chem Phys Lipids. 2019;221:8–14.PubMed

68.

•• Lu J, Yu Y, Zhu I, Cheng Y, Sun PD. Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis. Proc Natl Acad Sci U S A. 2014;111(14):5189–94 This study reports the first high-resolution structure of human SAA1 in two different crystal forms solved by x-ray crystallography. This structure sets the basis for later studies determining the lipid-binding site and other aspects of the structure-function relationship in SAA protein family.PubMedPubMedCentral

69.

Das M, Gursky O. Amyloid-forming properties of human apolipoproteins: sequence analyses and structural insights. Adv Exp Med Biol. 2015;855:175–211.PubMedPubMedCentral

70.

• Frame NM, Kumanan M, Wales TE, Bandara A, Fändrich M, Straub JE, et al. Structural basis for lipid binding and function by an evolutionarily conserved protein, serum amyloid A. J Mol Biol. 2020;432(7):1978–95 Hydrogen-deuterium exchange mass spectrometry is combined with molecular dynamics simulations and other biophysical techniques to compare conformation and dynamics in lipid-free and POPC-bound SAA. The results reveal the evolutionarily conserved lipid binding mechanism via helices h1 and h3.PubMed

71.

• Claus S, Meinhardt K, Aumüller T, Puscalau-Girtu I, Linder J, Haupt C, et al. Cellular mechanism of fibril formation from serum amyloid A1 protein. EMBO Rep. 2017;18(8):1352–66 The cell culture model is used to show that mSAA1 accumulation in lysosomes of monocytes and macrophages causes cellular membrane disruption, lysosomal leakage, and cell death, while the pre-formed amyloid seeds the extracellular fibrils, recapitulating key steps in AA deposition.PubMedPubMedCentral

72.

•• Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, et al. Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. Nat Commun. 2019;10(1):1104 Amyloid fibril structures of SAA fragments, which were derived from human and murine AA deposits, were determined by electron cryo-microscopy to 2.7–3.0 Å resolution. The results reveal parallel in-register twisted β-sheets running through the molecules, show that deletion of Arg1 is critical for fibrillogenesis, and reveal similarities and differences between the fibril structures of human and murine protein which help explain limited cross-seeding in a mouse model.PubMedPubMedCentral

73.

Röcken C, Menard R, Bühling F, Vöckler S, Raynes J, Stix B, et al. Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation. Ann Rheum Dis. 2005;64(6):808–15.PubMedPubMedCentral

74.

• Jayaraman S, Gantz DL, Haupt C, Gursky O. Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis. Proc Natl Acad Sci U S A. 2017;114(32):E6507–15 This physicochemical study shows that at pH4.3, murine and human SAA1 form proteolysis-resistant oligomers that disrupt lipid bilayers, undergo a lipid-induced β-sheet folding, and form amyloid fibrils, pointing to the lysosomal origin of AA amyloidosis.PubMedPubMedCentral

75.

Liang JS, Schreiber BM, Salmona M, Phillip G, Gonnerman WA, de Beer FC, et al. Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells. J Lipid Res. 1996;37(10):2109–16.PubMed

76.

Rennegarbe M, Lenter I, Schierhorn A, Sawilla R, Haupt C. Influence of C-terminal truncation of murine serum amyloid A on fibril structure. Sci Rep. 2017;7(1):6170.PubMedPubMedCentral

77.

Tanaka M, Nishimura A, Takeshita H, Takase H, Yamada T, Mukai T. Effect of lipid environment on amyloid fibril formation of human serum amyloid A. Chem Phys Lipids. 2017;202:6–12.PubMed

78.

• Jayaraman S, Fändrich M, Gursky O. Synergy between serum amyloid A and secretory phospholipase A2. Elife. 2019;8:e46630 This biochemical study shows that, by encapsulating lipids and their degradation products, SAA augments the activity of another acute-phase protein, secretory phospholipase A2. SAA and sPLA2 are proposed to act in synergy to clear cell membrane debris from the sites of injury.PubMedPubMedCentral

79.

Massey JB, Pao Q, Van Winkle WB, Pownall HJ. Interaction of human plasma lecithin: cholesterol acyltransferase and venom phospholipase A2 with apolipoprotein A-I recombinants containing nonhydrolyzable diether phosphatidylcholines. J Biol Chem. 1985;260(21):11719–23.PubMed

80.

Cabana VG, Reardon CA, Wei B, Lukens JR, Getz GS. mSAA-only HDL formed during the acute phase response in apoA-I+/+ and apoA-I-/- mice. J Lipid Res. 1999;40(6):1090–103.PubMed

81.

Stonik JA, Remaley AT, Demosky SJ, Neufeld EB, Bocharov A, Brewer HB. Serum amyloid A promotes ABCA1-dependent and ABCA1-independent lipid efflux from cells. Biochem Biophys Res Commun. 2004;321(4):936–41.PubMed

82.

Abe-Dohmae S, Kato KH, Kumon Y, Hu W, Ishigami H, Iwamoto N, et al. Serum amyloid A generates high density lipoprotein with cellular lipid in an ABCA1- or ABCA7-dependent manner. J Lipid Res. 2006;47(7):1542–50.PubMed

83.

Ancsin JB, Kisilevsky R. The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis. J Biol Chem. 1999;274(11):7172–81.PubMed

84.

Shao B, Heinecke JW. Quantifying HDL proteins by mass spectrometry: how many proteins are there and what are their functions? Expert Rev Proteomics. 2018;15(1):31–40.PubMed

85.

Liberta F, Rennegarbe M, Rösler R, Bijzet J, Wiese S, Hazenberg BPC, et al. Morphological and primary structural consistency of fibrils from different AA patients (common variant). Amyloid. 2019;26(3):164–70.PubMed

86.

Kisilevsky R, Raimondi S, Bellotti V. Historical and current concepts of fibrillogenesis and in vivo amyloidogenesis: implications of amyloid tissue targeting. Front Mol Biosci. 2016;3:17.PubMedPubMedCentral

87.

Annamalai K, Liberta F, Vielberg MT, Close W, Lilie H, Gührs KH, et al. Common fibril structures imply systemically conserved protein misfolding pathways in vivo. Angew Chem Int Ed Eng. 2017;56(26):7510–4.

88.

Tanaka M, Kawakami T, Okino N, Sasaki K, Nakanishi K, Takase H, et al. Acceleration of amyloid fibril formation by carboxyl-terminal truncation of human serum amyloid. Arch Biochem Biophys. 2018;639:9–15.PubMed

89.

• Claus S, Puscalau-Girtu I, Walther P, Syrovets T, Simmet T, Haupt C, et al. Cell-to-cell transfer of SAA1 protein in a cell culture model of systemic AA amyloidosis. Sci Rep. 2017;7:45683 An interesting cell-based study addressing the mechanism of AA transmission.PubMedPubMedCentral

90.

• Kollmer M, Meinhardt K, Haupt C, Liberta F, Wulff M, Linder J, et al. Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits. Proc Natl Acad Sci U S A. 2016;113(20):5604–9 Imaging of cell-derived amyloid reveals fibrillar networks infiltrated by lipid vesicles that may originate from the dead amyloid-forming cells. The results support the direct role of lipids in amyloid deposition.PubMedPubMedCentral

91.

Yamagata A, Uchida T, Yamada Y, Nakanishi T, Nagai K, Imakiire T, et al. Rapid clinical improvement of amyloid A amyloidosis following treatment with tocilizumab despite persisting amyloid deposition: a case report. BMC Nephrol. 2017;18(1):377.PubMedPubMedCentral

92.

Sayed RH, Hawkins PN, Lachmann HJ. Emerging treatments for amyloidosis. Kidney Int. 2015;87(3):516–26.PubMed

93.

Blank N, Hegenbart U, Dietrich S, Brune M, Beimler J, Röcken C, et al. Obesity is a significant susceptibility factor for idiopathic AA amyloidosis. Amyloid. 2018;25(1):37–45.PubMed

94.

Noborn F, Ancsin JB, Ubhayasekera W, Kisilevsky R, Li JP. Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation. J Biol Chem. 2012;287(30):25669–77.PubMedPubMedCentral

95.

Sosnowska M, Skibiszewska S, Kamińska E, Wieczerzak E, Jankowska E. Designing peptidic inhibitors of serum amyloid A aggregation process. Amino Acids. 2016;48(4):1069–78.PubMed

96.

Jayaraman S, Sánchez-Quesada JL, Gursky O. Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: potential implications for treatment of apolipoprotein deposition diseases. Biochim Biophys Acta. 2017;1863(1):200–10.

97.

Stankovic Stojanovic K, Georgin-Lavialle S, Poitou C, Buob D, Amselem S, Grateau G, et al. AA amyloidosis is an emerging cause of nephropathy in obese patients. Eur J Intern Med. 2017;39:e18–20.PubMed

98.

Puscalau-Girtu I, Scheller JS, Claus S, Fändrich M. Cell assay for the identification of amyloid inhibitors in systemic AA amyloidosis. Amyloid. 2019;26(1):24–33.PubMed

99.

Zhang Q, Wei Y, Chen M, Wan Q, Chen X. Clinical analysis of risk factors for severe COVID-19 patients with type 2 diabetes. J Diabetes Complicat. 2020;107666. https://doi.org/10.1016/j.jdiacomp.2020.107666

100.

Anderson MR, Geleris J, Anderson DR, Zucker J, Nobel YR, Freedberg D, et al. Body mass index and risk for intubation or death in SARS-CoV-2 infection: a retrospective cohort study. Ann Intern Med. 2020;29:M20–3214.

101.

Pranata R, Lim MA, Yonas E, Vania R, Lukito AA, Siswanto BB, et al. Body mass index and outcome in patients with COVID-19: a dose-response meta-analysis. Diabetes Metab. 2020. https://doi.org/10.1016/j.diabet.2020.07.005

102.

Li H, Xiang X, Ren H, Xu L, Zhao L, Chen X, et al. Serum amyloid A is a biomarker of severe coronavirus disease and poor prognosis. J Inf Secur. 2020;80(6):646–55.

103.

Smith SM, Boppana A, Traupman JA, Unson E, Maddock DA, Chao K, et al. Impaired glucose metabolism in patients with diabetes, prediabetes, and obesity is associated with severe COVID-19. J Med Virol. 2020. https://doi.org/10.1002/jmv.26227.

Titel: Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve
verfasst von: Olga Gursky
Publikationsdatum: 01.11.2020
Verlag: Springer US
Erschienen in: Current Atherosclerosis Reports / Ausgabe 11/2020
Print ISSN: 1523-3804
Elektronische ISSN: 1534-6242
DOI: https://doi.org/10.1007/s11883-020-00888-y

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

^{Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag}

Kostenlos registrieren

Neu im Fachgebiet Innere Medizin

22.04.2024 | DGIM 2024 | Kongressbericht | Nachrichten

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.

Newsletter bestellen

Live-Webinar: Aktuelle Leitlinien bei Herz-Kreislauf-Erkrankungen

Springer Medizin

Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve

Abstract

Purpose of Review

Recent Findings

Summary

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Krebspatienten impfen: Was? Wen? Und wann nicht?

Nierenultraschall: Tipps vom Profi

Bei RSV-Impfung vor 60. Lebensjahr über Off-Label-Gebrauch aufklären!

„KI sieht, was wir nicht sehen“

Update Innere Medizin

Live-Webinar: Aktuelle Leitlinien bei Herz-Kreislauf-Erkrankungen

Springer Medizin

Abstract

Purpose of Review

Recent Findings

Summary

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 11/2020

Familial Chylomicronemia Syndrome (FCS): Recent Data on Diagnosis and Treatment

Biological Factors Linking ApoE ε4 Variant and Severe COVID-19

The Knowns and Unknowns of Contemporary Statin Therapy for Familial Hypercholesterolemia

Gender Differences in Residual Risk Factors for Major Adverse Cardiovascular Events Following ACS and How to Bridge the Gap

The Role of Nutraceuticals in the Optimization of Lipid-Lowering Therapy in High-Risk Patients with Dyslipidaemia

Therapeutic Apheresis for Management of Lp(a) Hyperlipoproteinemia

Leitlinien kompakt für die Innere Medizin

Neu im Fachgebiet Innere Medizin

Krebspatienten impfen: Was? Wen? Und wann nicht?

Nierenultraschall: Tipps vom Profi

Bei RSV-Impfung vor 60. Lebensjahr über Off-Label-Gebrauch aufklären!

„KI sieht, was wir nicht sehen“

Update Innere Medizin