SAA2

SAA2
Identifiers
Aliases	SAA2
External IDs	GeneCards: SAA2
Gene ontology Molecular function • chemoattractant activity Cellular component • extracellular exosome • extracellular region • extracellular fluid • high-density lipoprotein particle Biological process • acute-phase response • cell chemotaxis • positive chemotaxis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6289	n/a
Ensembl	ENSG00000134339	n/a
UniProt	P0DJI9	n/a
RefSeq (mRNA)	NM_030754 NM_001127380	n/a
RefSeq (protein)	NP_001120852.1 NP_110381.2	n/a
Location (UCSC)	Chr 11: 18.24 – 18.25 Mb	n/a
PubMed search	[1]	n/a
Wikidata

View/Edit Human

Serum amyloid A protein is a protein that in humans is encoded by the SAA2 gene.^[2][3]

References

1. "Human PubMed Reference:".
2. 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.
3. "Entrez Gene: SAA2 Serum amyloid A2".

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.