Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
SAA2
Introduction
Serum amyloid A protein is a protein that in humans is encoded by the SAA2 gene.[1][2]
References
References
- ↑ Steel DM, Sellar GC, Uhlar CM, Simon S, DeBeer FC, Whitehead AS (Jul 1993). “A constitutively expressed serum amyloid A protein gene (SAA4) is closely linked to, and shares structural similarities with, an acute-phase serum amyloid A protein gene (SAA2)”. Genomics. 16 (2): 447–54. doi:10.1006/geno.1993.1209. PMID 7686132.
- ↑ “Entrez Gene: SAA2 Serum amyloid A2”.
Further reading
Further reading
- Betts JC, Edbrooke MR, Thakker RV, Woo P (1991). “The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells”. Scand. J. Immunol. 34 (4): 471–82. doi:10.1111/j.1365-3083.1991.tb01570.x. PMID 1656519.
- Zimlichman S, Danon A, Nathan I, et al. (1990). “Serum amyloid A, an acute phase protein, inhibits platelet activation”. J. Lab. Clin. Med. 116 (2): 180–6. PMID 1697614.
- 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 (1): 187–93. doi:10.1042/bj2680187. PMC 1131410. PMID 1971508.
- Woo P, Sipe J, Dinarello CA, Colten HR (1987). “Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells”. J. Biol. Chem. 262 (32): 15790–5. PMID 2890635.
- Kluve-Beckerman B, Dwulet FE, Benson MD (1988). “Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person”. J. Clin. Invest. 82 (5): 1670–5. doi:10.1172/JCI113779. PMC 442736. PMID 3183061.
- Kluve-Beckerman B, Long GL, Benson MD (1987). “DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA)”. Biochem. Genet. 24 (11–12): 795–803. doi:10.1007/BF00554519. PMID 3800865.
- Meek RL, Hoffman JS, Benditt EP (1986). “Amyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation”. J. Exp. Med. 163 (3): 499–510. doi:10.1084/jem.163.3.499. PMC 2188051. PMID 3950541.
- Badolato R, Wang JM, Murphy WJ, et al. (1994). “Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes”. J. Exp. Med. 180 (1): 203–9. doi:10.1084/jem.180.1.203. PMC 2191543. PMID 7516407.
- Badolato R, Johnston JA, Wang JM, et al. (1995). “Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway”. J. Immunol. 155 (8): 4004–10. PMID 7561109.
- Xu L, Badolato R, Murphy WJ, et al. (1995). “A novel biologic function of serum amyloid A. Induction of T lymphocyte migration and adhesion”. J. Immunol. 155 (3): 1184–90. PMID 7636186.
- Liepnieks JJ, Kluve-Beckerman B, Benson MD (1995). “Characterization of amyloid A protein in human secondary amyloidosis: the predominant deposition of serum amyloid A1”. Biochim. Biophys. Acta. 1270 (1): 81–6. doi:10.1016/0925-4439(94)00076-3. PMID 7827140.
- Arai K, Miura K, Baba S, Shirasawa H (1994). “Transformation from SAA2-fibrils to AA-fibrils in amyloid fibrillogenesis: in vivo observations in murine spleen using anti-SAA and anti-AA antibodies”. J. Pathol. 173 (2): 127–34. doi:10.1002/path.1711730209. PMID 8089807.
- Meek RL, Urieli-Shoval S, Benditt EP (1994). “Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function”. Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3186–90. doi:10.1073/pnas.91.8.3186. PMC 43540. PMID 8159722.
- Sellar GC, Jordan SA, Bickmore WA, et al. (1994). “The human serum amyloid A protein (SAA) superfamily gene cluster: mapping to chromosome 11p15.1 by physical and genetic linkage analysis”. Genomics. 19 (2): 221–7. doi:10.1006/geno.1994.1051. PMID 8188252.
- Ducret A, Bruun CF, Bures EJ, 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 (5): 866–76. doi:10.1002/elps.1150170508. PMID 8783012.
- Ancsin JB, Kisilevsky R (1997). “Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A”. J. Biol. Chem. 272 (1): 406–13. doi:10.1074/jbc.272.1.406. PMID 8995276.
- Hershkoviz R, Preciado-Patt L, Lider O, et al. (1997). “Extracellular matrix-anchored serum amyloid A preferentially induces mast cell adhesion”. Am. J. Physiol. 273 (1 Pt 1): C179–87. PMID 9252455.
- Migita K, Kawabe Y, Tominaga M, et al. (1998). “Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts”. Lab. Invest. 78 (5): 535–9. PMID 9605178.
- Urieli-Shoval S, Cohen P, Eisenberg S, Matzner Y (1999). “Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium”. J. Histochem. Cytochem. 46 (12): 1377–84. doi:10.1177/002215549804601206. PMID 9815279.