Serum amyloid A truncations in type 2 diabetes mellitus

PLoS ONE

Volumn 10, Issue 1, 2015, Pages

  Yassine, Hussein N ^a   Trenchevska, Olgica ^b   He, Huijuan ^a   Borges, Chad R ^b   Nedelkov, Dobrin ^b   Mack, Wendy ^a   Kono, Naoko ^a   Koska, Juraj ^c   Reaven, Peter D ^c   Nelson, Randall W ^b  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b ARIZONA STATE UNIVERSITY   (United States)

^c CARL T HAYDEN VA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; AMYLOID A PROTEIN; C REACTIVE PROTEIN; GLUCOSE; GLYCOSYLATED HEMOGLOBIN; HEMOGLOBIN A1C; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; INSULIN; PROTEIN VARIANT; TRIACYLGLYCEROL; ARGININE; SERUM AMYLOID A;

ADULT; AMINO TERMINAL SEQUENCE; ARTICLE; BODY MASS; CHRONIC KIDNEY DISEASE; CONTROLLED STUDY; CORRELATIONAL STUDY; FEMALE; GLOMERULUS FILTRATION RATE; HUMAN; IMMUNOASSAY; MAJOR CLINICAL STUDY; MALE; MASS SPECTROMETRY; NON INSULIN DEPENDENT DIABETES MELLITUS; PROTEIN BLOOD LEVEL; PROTEIN MODIFICATION; PROTEIN TRUNCATION; SEX DIFFERENCE; WAIST CIRCUMFERENCE; AGED; BLOOD; CLINICAL TRIAL; METABOLISM; MIDDLE AGED; VERY ELDERLY;

ADULT; AGED; AGED, 80 AND OVER; ARGININE; CHOLESTEROL, HDL; DIABETES MELLITUS, TYPE 2; FEMALE; HUMANS; MALE; MIDDLE AGED; SERUM AMYLOID A PROTEIN;

EID: 84956664778     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0115320     Document Type: Article

References (37)

1. Malle E, De Beer FC (1996) Human serum amyloid A (SAA) protein: a prominent acute-phase reactant for clinical practice. European Journal of Clinical Investigation 26:427-435. doi: 10.1046/j.1365-2362. 1996.159291.x PMID: 8817153
2. Malle E, Steinmetz A, Raynes JG (1993) Serum amyloid A (SAA): an acute phase protein and apolipoprotein. Atherosclerosis 102:131-146. doi: 10.1016/0021-9150 (93) 90155-N PMID: 7504491
3. Kiernan UA, Tubbs KA, Nedelkov D, Niederkofler EE, Nelson RW (2003) Detection of novel truncated forms of human serum amyloid A protein in human plasma. FEBS Lett 537:166-170. doi: 10.1016/S0014-5793 (03) 00097-8 PMID: 12606051
4. Cabana V, Siegel J, Sabesin S (1989) Effects of the acute phase response on the concentration and density distribution of plasma lipids and apolipoproteins. Journal of lipid research 30:39-49. PMID: 2493057
5. Liang J, Sipe J (1995) Recombinant human serum amyloid A (apoSAAp) binds cholesterol and modulates cholesterol flux. Journal of lipid research 36:37-46. PMID: 7706946
6. Tölle M, Huang T, Schuchardt M, Jankowski V, Prüfer N, et al. (2012) High-density lipoprotein loses its anti-inflammatory capacity by accumulation of pro-inflammatory-serum amyloid A. Cardiovascular research 94:154-162. doi: 10.1093/cvr/cvs089 PMID: 22328092
7. Elliott B, Liang, Sipe, Cathcart (1998) Catabolism of Lipid-Free Recombinant Apolipoprotein Serum Amyloid A by Mouse Macrophages In Vitro Results in Removal of the Amyloid Fibril-Forming Amino Terminus. Scandinavian Journal of Immunology 48:241-247. doi: 10.1046/j.1365-3083.1998.00384.x PMID: 9743207
8. Cunnane G (2001) Amyloid precursors and amyloidosis in inflammatory arthritis. Current opinion in rheumatology 13:67-73. doi: 10.1097/00002281-200101000-00011 PMID: 11148718
9. Ristori G, Laurenti F, Stacchini P, Gasperini C, Buttinelli C, et al. (1998) Serum amyloid A protein is elevated in relapsing-remitting multiple sclerosis. Journal of neuroimmunology 88:9-12. doi: 10.1016/S0165-5728 (98) 00037-X PMID: 9688318
10. Malle E, Sodin-Semrl S, Kovacevic A (2009) Serum amyloid A: an acute-phase protein involved in tumour pathogenesis. Cell Mol Life Sci 66:9-26. doi: 10.1007/s00018-008-8321-x PMID: 18726069
11. Zhao Y, He X, Shi X, Huang C, Liu J, et al. (2010) Association between serum amyloid A and obesity: a meta-analysis and systematic review. Inflamm Res 59:323-334. doi: 10.1007/s00011-010-0163-y PMID: 20140694
12. Tolson J, Bogumil R, Brunst E, Beck H, Elsner R, et al. (2004) Serum protein profiling by SELDI mass spectrometry: detection of multiple variants of serum amyloid alpha in renal cancer patients. Laboratory Investigation 84:845-856. doi: 10.1038/labinvest.3700097 PMID: 15107802
13. Tumblin A, Tailor A, Hoehn GT, Mack AK, Mendelsohn L, et al. (2010) Apolipoprotein AI and serum amyloid A plasma levels are biomarkers of acute painful episodes in patients with sickle cell disease. haematologica 95:1467-1472. doi: 10.3324/haematol.2009.018044 PMID: 20378559
14. Avgerinos ED, Kadoglou NP, Moulakakis KG, Giannakopoulos TG, Liapis CD (2011) Current role of biomarkers in carotid disease: a systematic review. Int J Stroke 6:337-345. doi: 10.1111/j.1747-4949. 2011.00623.x PMID: 21745345
15. Beach CM, De Beer MC, Sipe JD, Loose LD, De Beer FC (1992) Human serum amyloid A protein. Complete amino acid sequence of a new variant. Biochem J 282(Pt 2):615-620. PMID: 1546977
16. Raynes JG, McAdam KP (1991) Serum amyloid A isoforms in inflammation. Scand J Immunol 33:657-666.
17. Westermark GT, Engström U, Westermark P (1992) The N-terminal segment of protein AA determines its fibrillogenic property. Biochemical and biophysical research communications 182:27-33. doi: 10. 1016/S0006-291X (05) 80107-X PMID: 1731787
18. Egashira M, Takase H, Yamamoto I, Tanaka M, Saito H (2011) Identification of regions responsible for heparin-induced amyloidogenesis of human serum amyloid A using its fragment peptides. Archives of biochemistry and biophysics 511:101-106. doi: 10.1016/j.abb.2011.04.019 PMID: 21569756
19. Farwig ZN, McNeal CJ, Little D, Baisden CE, Macfarlane RD (2005) Novel truncated isoforms of constitutive serum amyloid A detected by MALDI mass spectrometry. Biochemical and biophysical research communications 332:352-356. doi: 10.1016/j.bbrc.2005.04.129 PMID: 15910745
20. Ducret A, Bruun CF, Bures EJ, Marhaug G, Husby G, et al. (1996) Characterization of human serum amyloid A protein isoforms separated by two-dimensional electrophoresis by liquid chromatography/electrospray ionization tandem mass spectrometry. ELECTROPHORESIS 17:866-876. doi: 10.1002/elps.1150170508 PMID: 8783012
21. Nelson RW, Borges CR (2011) Mass spectrometric immunoassay revisited. J Am Soc Mass Spectrom 22:960-968. doi: 10.1007/s13361-011-0094-z PMID: 21953037
22. Nelson RW, Krone JR, Bieber AL, Williams P (1995) Mass spectrometric immunoassay. Anal Chem 67:1153-1158. doi: 10.1021/ac00103a003 PMID: 15134097
23. Levey AS, Bosch JP, Lewis JB, Greene T, Rogers N, et al. (1999) A more accurate method to estimate glomerular filtration rate from serum creatinine: a new prediction equation. Annals of internal medicine 130:461-470. doi: 10.7326/0003-4819-130-6-199903160-00002 PMID: 10075613
24. Levey AS, de Jong PE, Coresh J, El Nahas M, Astor BC, et al. (2010) The definition, classification, and prognosis of chronic kidney disease: a KDIGO Controversies Conference report. Kidney international 80:17-28.
25. Tajima M, Wakita D, Noguchi D, Chamoto K, Yue Z, et al. (2008) IL-6-dependent spontaneous proliferation is required for the induction of colitogenic IL-17-producing CD8+ T cells. The Journal of experimental medicine 205:1019-1027. doi: 10.1084/jem.20071133 PMID: 18426983
26. Sung H-J, Jeon S, Ahn J-M, Seul K-J, Kim JY, et al. (2012) Large-scale isotype-specific quantification of Serum amyloid A 1/2 by multiple reaction monitoring in crude sera. Journal of proteomics 75:2170-2180. doi: 10.1016/j.jprot.2012.01.018 PMID: 22300576
27. Igawa T, Ishii S, Tachibana T, Maeda A, Higuchi Y, et al. (2010) Antibody recycling by engineered pHdependent antigen binding improves the duration of antigen neutralization. Nature biotechnology 28:1203-1207. doi: 10.1038/nbt.1691 PMID: 20953198
28. Malik P, Berisha SZ, Santore J, Agatisa-Boyle C, Brubaker G, et al. (2011) Zymosan-mediated inflammation impairs in vivo reverse cholesterol transport. Journal of lipid research 52:951-957. doi: 10. 1194/jlr. M011122 PMID: 21335620
29. Vijay-Kumar M, Sanders CJ, Taylor RT, Kumar A, Aitken JD, et al. (2007) Deletion of TLR5 results in spontaneous colitis in mice. The Journal of clinical investigation 117:3909-3921. doi: 10.1172/JCI33084 PMID: 18008007
30. Strachan AF, Brandt WF, Woo P, van der Westhuyzen DR, Coetzee GA, et al. (1989) Human serum amyloid A protein. The assignment of the six major isoforms to three published gene sequences and evidence for two genetic loci. Journal of Biological Chemistry 264:18368-18373. PMID: 2808379
31. Dwulet FE, Wallace DK, Benson MD (1988) Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual. Biochemistry 27:1677-1682. doi: 10.1021/bi00405a044 PMID: 3130100
32. Skogen B, Natvig JB (1981) Degradation of amyloid proteins by different serine proteases. Scand J Immunol 14:389-396. doi: 10.1111/j.1365-3083.1981.tb00579.x PMID: 6461061
33. Gordon JI, Sims HF, Strauss AW, Scanu AM, Edelstein C, et al. (1986) Proteolytic Processing and Compartmentalization of the Primary Translation Products of Mammalian Apolipoprotein Mrna. Critical Reviews in Biochemistry and Molecular Biology 20:37-71. doi: 10.3109/10409238609115900 PMID: 3514123
34. Gershoni-Baruch R, Brik R, Lidar M, Shinawi M, Livneh A (2003) Male sex coupled with articular manifestations cause a 4-fold increase in susceptibility to amyloidosis in patients with familial Mediterranean fever homozygous for the M694V-MEFV mutation. The Journal of rheumatology 30:308-312. PMID: 12563686
35. Orchard TJ, Dorman JS, Maser RE, Becker DJ, Drash AL, et al. (1990) Prevalence of complications in IDDM by sex and duration: Pittsburgh Epidemiology of Diabetes Complications Study II. Diabetes 39:1116-1124. doi: 10.2337/diabetes.39.9.1116 PMID: 2384191
36. Tsun J, Shiu S, Wong Y, Yung S, Chan T, et al. (2013) Impact of serum amyloid A on cellular cholesterol efflux to serum in type 2 diabetes mellitus. Atherosclerosis 231:405-410. doi: 10.1016/j. atherosclerosis.2013.10.008 PMID: 24267259
37. Steinkasserer A, Weiss EH, Schwaeble W, Linke RP (1990) Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis. Biochem J 268:187-193. PMID: 1971508