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Gene Review

Saa1  -  serum amyloid A 1

Mus musculus

Synonyms: Saa-1, Saa2, Serum amyloid A-1 protein
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Disease relevance of Saa1


High impact information on Saa1


Chemical compound and disease context of Saa1


Biological context of Saa1

  • Our results suggest that SAF is a key regulator of cytokine-mediated SAA gene expression in some nonhepatic cells [14].
  • Transfection and DNA-binding studies were performed to investigate the mechanism controlling cytokine-induced, nonhepatic expression of the SAA gene [14].
  • In order to explore the mechanism of SAA isotype-specific amyloid protein AA deposition, the molecular kinetics of the serum amyloid proteins were examined in CBA mice during casein induction of amyloidosis [15].
  • The serum amyloid A (SAA) proteins make up a multigene family of apolipoproteins associated with high density lipoproteins [16].
  • Starting with induced liver RNA, we have constructed a recombinant plasmid containing most of the DNA sequence encoding the serum amyloid A polypeptide [17].

Anatomical context of Saa1

  • These results indicate that fibronectin plays an important role in the development of amyloidosis by working as a linking protein between SAA and the cell surface of macrophages [18].
  • Extrahepatic SAA1 and SAA2 mRNA were induced by lipopolysaccharide in kidney proximal and distal convoluted tubule epithelia, and SAA1 mRNA was induced in epithelial lining the mucosa of the ileum and large intestine, indicating that there may be more than one function for the apoSAA gene family related to site of and stimulus for expression [19].
  • Induction of serum amyloid A inflammatory response genes in irradiated bone marrow cells [20].
  • The small intestine, primarily the ileum, and the large intestine of unstimulated control animals contained 5- and 15-fold higher SAA mRNA levels than control liver [21].
  • Adrenal gland expressed SAA mRNA at a low level (0.5% of hepatic level), and was the only extrahepatic tissue with elevated SAA mRNA after casein injection [21].

Associations of Saa1 with chemical compounds


Regulatory relationships of Saa1

  • This suggested that suppression of SAA levels was not the primary event inhibiting amyloid deposition [26].
  • METHODS AND RESULTS: A cytokine mixture (tumor necrosis factor [TNF]-alpha, interleukin [IL]-1beta, and IL-6) simultaneously induced SAA and repressed apoA-I and PON-1 expression levels [27].
  • The injection of IL-2 induced SAA gene expression in the liver [28].
  • Only liposomes containing intact SAA2.1 or its residues 1-20 or 74-103 promoted the efflux of cholesterol in vivo [29].
  • Epithelial induction of serum amyloid A is possibly relevant to mucosal inflammation because that was observed in bacteria-reconstituted and dextran sulfate sodium-induced colitis in vivo and because interleukin-beta and lipopolysaccharide induced its mRNA in vitro [30].

Other interactions of Saa1


Analytical, diagnostic and therapeutic context of Saa1


  1. Monokine-induced synthesis of serum amyloid A protein by hepatocytes. Selinger, M.J., McAdam, K.P., Kaplan, M.M., Sipe, J.D., Vogel, S.N., Rosenstreich, D.L. Nature (1980) [Pubmed]
  2. Hepatic catabolism of serum amyloid A during an acute phase response and chronic inflammation. Gollaher, C.J., Bausserman, L.L. Proc. Soc. Exp. Biol. Med. (1990) [Pubmed]
  3. N-terminal sequence analysis of SAA-derivatives purified from murine inflammatory macrophages. Bell, A.W., Chan, S.L., Ali-Khan, Z. Amyloid (1999) [Pubmed]
  4. Assessment of the efficacy of different statins in murine collagen-induced arthritis. Palmer, G., Chobaz, V., Talabot-Ayer, D., Taylor, S., So, A., Gabay, C., Busso, N. Arthritis Rheum. (2004) [Pubmed]
  5. Protective effects of alpha1-acid glycoprotein and serum amyloid A on concanavalin A-induced liver failure via interleukin-6 induction by ME3738. Kuzuhara, H., Nakano, Y., Yamashita, N., Imai, M., Kawamura, Y., Kurosawa, T., Nishiyama, S. Eur. J. Pharmacol. (2006) [Pubmed]
  6. Diverse gene expression for isotypes of murine serum amyloid A protein during acute phase reaction. Yamamoto, K., Shiroo, M., Migita, S. Science (1986) [Pubmed]
  7. Linkage of protection against amyloid fibril formation in the mouse to a single, autosomal dominant gene. Gonnerman, W.A., Elliott-Bryant, R., Carreras, I., Sipe, J.D., Cathcart, E.S. J. Exp. Med. (1995) [Pubmed]
  8. Expression of the third member of the serum amyloid A gene family in mouse adipocytes. Benditt, E.P., Meek, R.L. J. Exp. Med. (1989) [Pubmed]
  9. Mucosal production of complement C3 and serum amyloid A is differentially regulated in different parts of the gastrointestinal tract during endotoxemia in mice. Wang, Q., Wang, J.J., Fischer, J.E., Hasselgren, P.O. J. Gastrointest. Surg. (1998) [Pubmed]
  10. Fenofibrate inhibits reactive amyloidosis in mice. Murai, T., Yamada, T., Miida, T., Arai, K., Endo, N., Hanyu, T. Arthritis Rheum. (2002) [Pubmed]
  11. Tissue-specific expression of novel messenger ribonucleic acids cloned from a renin-expressing kidney tumor cell line (As4.1). Thompson, H.A., Burson, J.M., Lang, J.A., Gross, K.W., Sigmund, C.D. Endocrinology (1995) [Pubmed]
  12. Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1. Tam, S.P., Flexman, A., Hulme, J., Kisilevsky, R. J. Lipid Res. (2002) [Pubmed]
  13. Effect of poly(vinylsulfonate) on murine AA amyloid: a high-resolution ultrastructural study. Inoue, S., Hultin, P.G., Szarek, W.A., Kisilevsky, R. Lab. Invest. (1996) [Pubmed]
  14. A novel cis-acting element is essential for cytokine-mediated transcriptional induction of the serum amyloid A gene in nonhepatic cells. Ray, A., Ray, B.K. Mol. Cell. Biol. (1996) [Pubmed]
  15. Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation. Meek, R.L., Hoffman, J.S., Benditt, E.P. J. Exp. Med. (1986) [Pubmed]
  16. Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages. Meek, R.L., Eriksen, N., Benditt, E.P. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  17. Induction of hepatic synthesis of serum amyloid A protein and actin. Morrow, J.F., Stearman, R.S., Peltzman, C.G., Potter, D.A. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  18. The role of fibronectin in the development of experimental amyloidosis. Evidence of immunohistochemical codistribution and binding property with serum amyloid protein A. Kawahara, E., Shiroo, M., Nakanishi, I., Migita, S. Am. J. Pathol. (1989) [Pubmed]
  19. Serum amyloid A in the mouse. Sites of uptake and mRNA expression. Meek, R.L., Eriksen, N., Benditt, E.P. Am. J. Pathol. (1989) [Pubmed]
  20. Induction of serum amyloid A inflammatory response genes in irradiated bone marrow cells. Goltry, K.L., Epperly, M.W., Greenberger, J.S. Radiat. Res. (1998) [Pubmed]
  21. Amyloid A gene family expression in different mouse tissues. Meek, R.L., Benditt, E.P. J. Exp. Med. (1986) [Pubmed]
  22. Intracerebroventricular injection of anti-Fas activates the hypothalamus-pituitary-adrenal axis and induces peripheral interleukin-6 and serum amyloid A in mice: comparison with other ligands of the tumor necrosis factor/nerve growth factor receptor superfamily. Benigni, F., Sacco, S., Aloe, L., Ghezzi, P. Am. J. Pathol. (1998) [Pubmed]
  23. Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin. Yamada, T., Liepnieks, J., Benson, M.D., Kluve-Beckerman, B. J. Immunol. (1996) [Pubmed]
  24. Interleukin-1 and interleukin-6 stimulate acute-phase protein production in primary mouse hepatocytes. Prowse, K.R., Baumann, H. J. Leukoc. Biol. (1989) [Pubmed]
  25. Enhancement of murine serum amyloid A3 mRNA expression by glucocorticoids and its regulation by cytokines. Ishida, T., Matsuura, K., Setoguchi, M., Higuchi, Y., Yamamoto, S. J. Leukoc. Biol. (1994) [Pubmed]
  26. Effect of colchicine on experimental amyloidosis in two CBA/J mouse models. Chronic inflammatory stimulation and administration of amyloid-enhancing factor during acute inflammation. Brandwein, S.R., Sipe, J.D., Skinner, M., Cohen, A.S. Lab. Invest. (1985) [Pubmed]
  27. Reciprocal and coordinate regulation of serum amyloid A versus apolipoprotein A-I and paraoxonase-1 by inflammation in murine hepatocytes. Han, C.Y., Chiba, T., Campbell, J.S., Fausto, N., Chaisson, M., Orasanu, G., Plutzky, J., Chait, A. Arterioscler. Thromb. Vasc. Biol. (2006) [Pubmed]
  28. Suppression of IL-2-induced SAA gene expression in mice by the administration of an IL-1 receptor antagonist. Numerof, R.P., Sipe, J.D., Trehu, E.G., Dinarello, C.A., Mier, J.W. Cytokine (1992) [Pubmed]
  29. Macrophage cholesterol efflux and the active domains of serum amyloid A 2.1. Kisilevsky, R., Tam, S.P. J. Lipid Res. (2003) [Pubmed]
  30. Epithelial induction of serum amyloid A in experimental mucosal inflammation. Fukushima, K., Ogawa, H., Kitayama, T., Yamada, T., Naito, H., Funayama, Y., Matsuno, S., Sasaki, I. Dig. Dis. Sci. (2002) [Pubmed]
  31. Generation and use of site-specific antibodies to serum amyloid A for probing amyloid A development. Miura, K., Ju, S.T., Cohen, A.S., Shirahama, T. J. Immunol. (1990) [Pubmed]
  32. CpG-DNA upregulates the major acute-phase proteins SAA and SAP. Schmidt, U., Wagner, H., Miethke, T. Cell. Microbiol. (1999) [Pubmed]
  33. Extrahepatic expression of plasma protein genes during inflammation. Kalmovarin, N., Friedrichs, W.E., O'Brien, H.V., Linehan, L.A., Bowman, B.H., Yang, F. Inflammation (1991) [Pubmed]
  34. Circular-dichroism studies on two murine serum amyloid A proteins. McCubbin, W.D., Kay, C.M., Narindrasorasak, S., Kisilevsky, R. Biochem. J. (1988) [Pubmed]
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