Mouse SAA₁ and SAA₂ bind avidly to heat denatured ubiquitin

References

• Malle E, Skinmetz A, Raynes J G. Serum amyloid A (SAA): an acute phase protein and apolipoprotein. Atherosclerosis 1993; 102: 131–146
   PubMed Web of Science ®Google Scholar
• Husby G, Marhaug G, Dowton B, Sletten K, Sipe J D. Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid: Int J Clin Invest 1994; 1: 119–137
   Web of Science ®Google Scholar
• McAdam K PWJ, Sipe J D. Murine model for human secondary amyloidosis: genetic variability of acute-phase serum protein SAA to endotoxins and casein. J Exp Med 1976; 144: 1121–1127
   PubMed Web of Science ®Google Scholar
• Hoffman J S, Benditt E P. Changes in high-density lipoprotein content following endotoxin administration in the mouse. Formation of serum amyloid protein-rich subtractions. J Biol Chem 1982; 257: 10510–10517
   PubMed Web of Science ®Google Scholar
• Chronopoulos S, Lembo P, Alizadeh-Khiavi K, Normand J, Ali-Khan Z. Ubiquitin: its potential significance in murine AA amyloidosis. J Pathol 1992; 167: 249–259
   PubMed Web of Science ®Google Scholar
• Yamamoto K I, Migita S. Complete primary structures of two major murine serum amyloid A proteins deduced from cDNA sequences. Proc Natl Acad Sci USA 1985; 82: 2915–2919
   PubMed Web of Science ®Google Scholar
• Lowell C A, Potter D A, Stearman R S, Morrow J F. Structure of the murine serum amyloid A gene family. J Biol Chem 1986; 261: 8442–9452
   PubMed Web of Science ®Google Scholar
• de Beer M C, Beach C M, Shedlofsky S I, de Beer F C. Identification of a novel serum amyloid A protein in BALB/c mice. Biochem J 1991; 280: 45–49
   PubMed Web of Science ®Google Scholar
• Meek R L, Eriksen N, Benditt E P. Structural prerequisites for serum amyloid A fibril formation. J Biol Chem 1992; 269: 20606–20612, Murine serum amyloid A10 de Beer MC, de Beer FC, McCubbin W.D, Kay CM and Kindy MS (1993)
   Google Scholar
• Zahedi K, Gonnerman W A, de Beer F C, de Beer M C, Steel D M, Sipe J D, Whitehead A S. Major acute-phase reactant synthesis during chronic inflammation in amyloid-susceptible and -resistant mouse strains. Inflammation 1991; 15: 1–14
   PubMedGoogle Scholar
• Hoffman J S, Ericsson L H, Eriksen N, Walsh K A, Benditt E P. Amyloid A gene family expression in different mouse tissues. J Exp Med 1984; 164: 2006–2017, Murine tissue amyloid protein AA: NH13 Meek RL and Benditt EP (1986)
   Google Scholar
• Meek R L, Eriksen N, Benditt E P. Serum amyloid A in the mouse: sites of uptake and mRNA expression. Am J Pathol 1989; 135: 411–419
   Google Scholar
• Takahashi M, Yokota T, Yamashita Y, Ishihara T, Uchino F. Ultrastructural evidence for the synthesis of serum amyloid A protein by murine hepatocytes. Lab Invest 1985; 52: 220–233
   PubMed Web of Science ®Google Scholar
• Shirahama T, Cohen A S. Intralysosomal formation of amyloid fibrils. Am J Pathol 1975; 81: 101–106
   PubMed Web of Science ®Google Scholar
• Takahashi M, Yokato T, Kawano H. Ultrastructural evidence for intracellular formation of amyloid fibrils in macrophages. Virchows Archiv Pathol Anat 1989; 415: 411–419
   PubMedGoogle Scholar
• Alizadeh-Khiavi K, Li W, Chronopoulos S, Ali-Khan Z. Ubiquitin profile in inflammatory leukocytes and binding of ubiquitin to murine AA amyloid: immunocytochemical and immunogold electron microscopic studies. J Pathol 1994; 172: 209–217
   PubMed Web of Science ®Google Scholar
• Chronopoulos S, Laird D W, Ali-Khan Z. Immunolocalization of serum amyloid A and AA amyloid in lysosomes in murine monocytoid cells: confocal and immunogold electron microscopic studies. J Pathol 1994; 173: 361–369
   PubMed Web of Science ®Google Scholar
• Tape C, Tan R, Nesheim M, Kisilevsky R. Direct evidence for circulating apoSAA as the precursor of tissue AA amyloid deposits. Scand J Immunol 1988; 29: 317–324
   Google Scholar
• Axelrad M A, Kisilevsky R, Willmer J, Chen S J, Skinner M. Further characterization of amyloid enhancing factor. Lab Invest 1982; 47: 139–146
   PubMed Web of Science ®Google Scholar
• Alizadeh-Khiavi K, Normand J, Chronopoulos S, Ali A, Ali-Khan Z. Amyloid enhancing factor activity is associated with ubiquitin. Virchows Archiv A Pathol Anat 1992; 420: 139–148
   Google Scholar
• Alizadeh-Khiavi K, Normand J, Chronopoulos S, Ali-Khan Z. Alzheimer's brain derived ubiquitin has amyloid enhancing factor activity: behavior of ubiquitin during accelerated amyloidogenesis. Acta Neuropathol 1991; 81: 280–286
   PubMedGoogle Scholar
• Okada M, Miyazaki S, Hirasawa Y. Imunolocalization of ubiquitin and Alzheimer amyloid precursor protein derivatives in endosomal/lysosomal vacu-oles in cultured human neuroblastoma (SK-N-SH) and microglia (U-373). Amyloid and Amyloidosis, R Kisilevsky, M D Benson, B Frangione, J Gauldie, T J Muckle, I D Young. The Parthenon Publishing Group, Pearl River 1993; 377–379, Increase in plasma concentration of ubiquitin in dialysis patients: possible involvement in β25 Jung S, Chronopoulos S and Ali-Khan Z (1994) 1993
   Google Scholar
• Gregori L, Bhasin Rand Goldgaber D. Ubiquitin-mediated degradative pathway degrades the extracellular but not the intracellular form of amyloid β-protein precursor. Biochem Biophys Res Commun 1994; 203: 1731–1739
   Google Scholar
• Kudo T, Iqbal K, Ravid R, Swaab D F, Grundke-Iqbal I. Alzheimer disease: correlation of cerebro-spinal fluid and brain ubiquitin levels. Brain Res 1994; 639: 1–7
   PubMed Web of Science ®Google Scholar
• Laemmli V K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Marhaug G, Husby G. Characterization of human amyloid-related protein SAA as a polymorphic protein: associated with albumin and prealbumin in serum. Clin Exp Immunol 1981; 45: 97–106
   Google Scholar
• Hoffman J S, Benditt E P. Changes in high density lipoprotein content following endotoxin administration in the mouse. J Biol Chem 1982; 257: 10510–10517
   PubMed Web of Science ®Google Scholar
• Gollaher C J, Bausserman L L. Hepatic catabolism of serum amyloid A during an acute phase response and chronic inflammation. Proc Soc Exp Biol Med 1990; 194: 245–250
   PubMed Web of Science ®Google Scholar
• Chronopoulos S, Alizadeh-Khiavi K, Normand J, Ali-Khan Z. Binding of ubiquitin to experimentally induced murine AA amyloid. J Pathol 1991; 163: 199–203
   PubMed Web of Science ®Google Scholar
• Chan S L, Li W, Chronopoulos S, Alizadeh-Khiavi K, Ali-Khan Z. Characterization of murine A A amyloid-bound ubiquitin. Amyloid and Amyloidosis, R Kisilevsky, M D Benson, B Frangione, J Gauldie, T J Muckle, I D Young. The Parthenon Publishing Group, Pearl River 1993; 520–522, 1993
   Google Scholar
• Alizadeh-Khiavi A. Amyloid enhancing factor activity is associated with ubiquitin. Ph.D. Thesis, McGill University, MontrealCanada 1991
   Google Scholar
• Fried V A, Smith H T, Hildebrandt E, Weiner K. Ubiquitin has intrinsic proteolytic activity: implications for cellular regulation. Proc Natl Acad Sci USA 1987; 84: 3685–3698
   PubMed Web of Science ®Google Scholar
• Axelrad M A, Kisilevsky R. Biological characterizations of amyloid enhancing factor. Amyloid and Amyloidosis, G G Glenner, P P Costa, A F deFreitas. Excerpta Medica, Amsterdam-Oxford-Princeton 1980; 527–533, 1980
   Google Scholar
• Eytan E, Ganoth D, Armon T, Hershko A. ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proc Natl Acad Sci USA 1989; 86: 7751–7755
   PubMed Web of Science ®Google Scholar
• Finley D, Chan V. Ubiquination. Ann Rev Cell Biol 1991; 7: 25–69
   PubMedGoogle Scholar
• Laszlo L, Lowe J, Self T, Kenward N, Landon M, McBride T, Farquhar C, McConnel I, Brown J, Hope J, Mayer R J. Lysosomes are key organelles in the pathogenesis of prion encephalopathies. J Pathol 1992; 166: 333–341
   PubMedGoogle Scholar
• Doherty F J, Osborn N U, Wassell J A, Heggie P E, Laszlo L, Mayer R J. Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors. Biochem J 1989; 263: 47–55
   PubMedGoogle Scholar
• Mezquita J, Chiva M, Vidal S, Mezquita C. Effects of high mobility group nonhistone proteins HMG-20 (ubiquitin) and HMG-17 on histone deacetylase activity assayed in vitro. Nucl Acids Res 1982; 10: 1781–1797
   Google Scholar
• Watson D C, Levy-Wilson B, Gordon W, Dixon G H. Free ubiquitin is a nonhistone protein of trout testis chromatin. Nature 1978; 276: 196–198
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Subrahmanyan L. Serum amyloid A changes high density lipoproteins' cellular affinitya clue to serum amyloid A's principal function. Lab Invest 1992; 66: 778–785
   PubMed Web of Science ®Google Scholar
• Badolato R, Wang J M, Murphy W J, Lloyd A R, Michiel D F, Bausserman L L, Kelvin D J, Oppenheim J J. Serum amyloid A is a chemoattractant: Induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 1994; 180: 203–209
   PubMed Web of Science ®Google Scholar