Disease relevance of Apcs

• Serum amyloid P component enhances induction of murine amyloidosis [1].
• A murine scrapie model was evaluated for changes in plasma concentration of serum amyloid P component (SAP), a protein that is up-regulated in infected and/or injured mice during the acute phase response (APR) [2].
• Influenza virus infection is not affected by serum amyloid P component [3].
• Mice lacking serum amyloid P component do not necessarily develop severe autoimmune disease [4].
• Autoimmunity and glomerulonephritis in mice with targeted deletion of the serum amyloid P component gene: SAP deficiency or strain combination [5]?

Psychiatry related information on Apcs

• Serum amyloid P component (SAP) is associated with amyloid beta (A beta) deposition in Alzheimer disease (AD) [6].

High impact information on Apcs

• In response to ER stress, CREBH is cleaved by site-1 and site-2 proteases to liberate an amino-terminal fragment that transits to the nucleus to activate transcription of the genes encoding serum amyloid P-component (SAP) and C-reactive protein (CRP) [7].
• Avoiding the effect of linked genes is crucial to elucidate the role of Apcs in autoimmunity [8].
• Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis [9].
• Highly specific, high-resolution scintigraphic images of amyloid-laden organs in mice with experimentally induced amyloid A protein (AA) amyloidosis were obtained after intravenous injection of 123I-labeled serum amyloid P component (SAP) [10].
• Binding specificity of serum amyloid P component for the pyruvate acetal of galactose [11].

Chemical compound and disease context of Apcs

• Serum amyloid P component (SAP) binds to Streptococcus pyogenes, and we show here that it also binds to Neisseria meningitidis, including a lipopolysaccharide (LPS)-negative mutant, and to rough variants of Escherichia coli [12].
• The concentration of immunoglobulins, anti-ssDNA, anti-dsDNA, anti-TNP antibodies, IgM rheumatoid factor, C3, immune complexes and serum amyloid P component (SAP), in the serum were measured in 68 male and female MRL/lpr/lpr mice, a strain affected with a systemic autoimmune disease [13].
• The Syrian hamster (Mesocricetus auratus) has been widely used as an experimental animal and is a unique model for three sex hormone-regulated events: 1) estrogen-initiated renal carcinogenesis, 2) sex-limited expression of amyloidosis, a ubiquitous disease, and 3) sex hormone control of a serum amyloid P component (SAP) called female protein (FP) [14].

Biological context of Apcs

• Physical mapping of a family of interferon-activated genes, serum amyloid P-component, and alpha-spectrin on mouse chromosome 1 [15].
• Because of background genetic variation it was not possible to detect any crossovers between Sap and Ly-9 [16].
• Serum amyloid P component and C-reactive protein mediate phagocytosis through murine Fc gamma Rs [17].
• As a first step in studying the regulation and biosynthesis of serum amyloid P component in the mouse, cDNA clones have been isolated from a liver cDNA library and sequenced [18].
• Serum amyloid A (SAA) and the pentraxins C-reactive protein (CRP) and serum amyloid P component (SAP) are major AP proteins: their serum levels can rise by 1000-fold, indicating that they play a critical role in defense and/or the restoration of homeostasis [19].

Anatomical context of Apcs

• Spleens were examined for Congo red staining and serum amyloid A, serum amyloid P component, and apoE immunostaining [20].
• Ptx1 expression overlaps with that of Ptx2 in stomodeum and in posterior left lateral plate mesoderm [21].
• Ptx2 is expressed in both developing and adult pituitary gland, eye and brain tissues, suggesting an important role in development and maintenance of anterior structures [22].
• The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo [23].
• This impairment correlates with decreased circular transcript levels of Ialpha, Igamma2a, Igamma2b, and Igamma3 after stimulation, which indicate a defective Ig switch recombination in Sap-deficient B cells [24].

Associations of Apcs with chemical compounds

• Hepatic mRNA levels of the other mouse acute phase reactants (APRs), serum amyloid P component, C-reactive protein, alpha1-acid glycoprotein, and C3 were also induced with casein after 12 h, as were serum protein levels of SAP and C3 [25].
• By binding assay on the microtiter plate, SAA had more affinity to fibronectin than those of heparan sulfate, collagen type I, or serum amyloid P component [26].
• AEF can be solubilized in 4 M glycerol, is not the amyloid A protein, and is not likely to be the serum amyloid P component [27].
• We examined serum changes of four acute phase reactants: alpha 1-proteinase inhibition (alpha 1Pi); complement C3; serum amyloid A protein (SAA); and serum amyloid P component (SAP), in mice undergoing a primary infection with Nippostrongylus brasiliensis [28].
• Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS [29].

Other interactions of Apcs

• Recombinant inbred strain mapping has linked the P0 gene to Ly-9/Ly/Sap in a region corresponding to band 1H3 [30].
• We have described earlier a gene cluster, including at least six interferon-activatable genes closely linked to the erythroid alpha spectrin locus and the serum amyloid P-component locus on murine chromosome 1 [31].
• Involvement of CD14 and toll-like receptor 4 in the acute phase response of serum amyloid A proteins and serum amyloid P component in the liver after burn injury [32].
• The major acute-phase protein, serum amyloid P component, in mice is not involved in endogenous resistance against tumor necrosis factor alpha-induced lethal hepatitis, shock, and skin necrosis [33].
• To understand the role of interferon-gamma in the regulation of inflammation and to establish a mouse model of chronic active hepatitis, we produced transgenic mice in which the mouse interferon-gamma gene was regulated by a liver-specific promoter, the serum amyloid P component gene promoter [34].

Analytical, diagnostic and therapeutic context of Apcs

• Northern-blot analysis demonstrated that murine serum amyloid P component synthesis in the liver is directed by a 1.2-kb mRNA that is elevated in high responder (C57BL/6J) mice after thioglycollate-induced inflammation [18].
• Molecular genetics of mouse serum amyloid P component (SAP): cloning and gene mapping [35].
• Distinctive images of this amyloid-specific deposition of labeled serum amyloid P component were derived from whole body scanning, in vivo, of amyloidotic mice [36].
• Different Sap polyclonal antibodies were raised in rabbits and tested before further application by enzyme-linked immunosorbent assay (ELISA) against each recombinant Sap [37].
• Quantitation of the murine acute-phase reactant, serum amyloid P component (SAP), by Western blot is described [38].

References