Disease relevance of LOC506412

• The murine model of casein-induced amyloidosis was studied to determine the relationship between SAA production and amyloid deposition [1].
• Significantly raised milk concentrations of SAA were also found during chronic subclinical mastitis [2].
• The presence of a systemic acute-phase reaction was documented by fever, increase in serum amyloid A, and decrease in serum albumin [3].
• In conclusion, experimentally induced E. coli mastitis is accompanied by a prominent SAA response [4].
• Haptoglobin and serum amyloid A in milk and serum during acute and chronic experimentally induced Staphylococcus aureus mastitis [2].

High impact information on LOC506412

• Therefore, thymus-derived lymphocytes are not necessary for the synthesis of SAA [1].
• These factors may include alterations in the degradation of SAA by the reticuloendothelial system caused by substances such as casein [1].
• SAA levels measured by radioimmunoassay were found to be as high as 200 times the normal level in CBA/J mice receiving daily parenteral casein [1].
• During acute inflammation, the serum amyloid A (apoSAA) proteins apoSAA1 and apoSAA2 are transiently associated with high density lipoproteins (HDL) in concentrations of as much as 1000-fold more than their concentrations during homeostasis; however, their effect on HDL function is unclear [5].
• In various mammalian species, an isoform of serum amyloid A is secreted at high concentrations into colostrum [6].

Biological context of LOC506412

• Production of a third acute phase proteins, serum amyloid A, had very similar kinetics in both breeds [7].
• After parturition, SAA concentration increased significantly (P < 0.05) in maternal plasma [8].
• A classical acute phase response, as assessed by SAA, was observed during the expulsive stage, but not during luteolysis [9].
• Systemic changes were characterized by elevated body temperature, induction of the acute phase protein synthesis of serum amyloid A and LBP, and a transient decrease in circulating neutrophils and lymphocytes [10].
• This study compared concentrations of amyloid A in bovine milk with the cell-based indicators of intramammary inflammation, somatic cell count and California Mastitis Test. Mammary quarter data pertaining to 180 cows were categorised according to concentrations of serum amyloid A in the cow of origin [11].

Anatomical context of LOC506412

• In udder quarter samples from healthy cows, 42 out of 44 samples belonged to the ATP-Hp-SAA- group [12].
• Peripartum acute-phase protein serum amyloid-A concentration in plasma of cows and fetuses [8].
• Amino acids at concentrations in oviductal fluid tested by Elhanssan (EOAA) significantly improved development to the hatched blastocyst stage, compared to Sigma amino acid solutions BME and MEM (SAA) [13].
• Sonically disrupted normal erythrocyte stroma (SES) and two anaplasma antigens (sonically disrupted anaplasma antigen; SAA, and French pressure cell disrupted anaplasma antigen; FAA) were prepared from normal and Anaplasma marginale-infected blood [14].
• Serum amyloid A (SAA) proteins were originally identified as prominent acute phase serum reactants synthesized predominately by hepatocytes in response to infection, inflammation and trauma [15].

Associations of LOC506412 with chemical compounds

• These findings indicate possible suppressive action of fetal cortisol on fetal SAA production [8].
• Additionally, serum amyloid-A and alpha-acid glycoprotein concentrations were determined in Exp. 1 and 2, respectively [16].
• The SAA and FAA antigens were chemically modified by conjugation with dodecanoic acid (SAADA and FAADA) [14].
• The antiserum raised against the purified SAA stained Congo red positive regions in the kidney of an AA-amyloidotic cow and reacted on Western blot with an AA-related protein of approximately 14 kDa [17].

Other interactions of LOC506412

• Serum amyloid A had a maximum (100 per cent) clinical sensitivity in discriminating between the acute and chronic cases, and haptoglobin had the highest clinical specificity of 76 per cent; counts of neutrophils and band neutrophils had sensitivities of 71 per cent and 42 per cent and specificities of 30 per cent and 72 per cent, respectively [18].
• Serum amyloid A and TNF alpha in serum and milk during experimental endotoxin mastitis [19].

Analytical, diagnostic and therapeutic context of LOC506412

• Concentrations of serum amyloid A (SAA) increased significantly 3 h after both the primary (P <0.05) and booster (P <0.001) i.m. vaccinations, but not in i.n. vaccinated calves [20].
• Quantitative dot-blot enzyme immunoassay for serum amyloid A protein [21].
• Isoelectric focusing of SAA isolated from sera, obtained from cows affected with different diseases, showed a variable ratio of the isoforms [17].
• Moreover, it immunostained two to three bands, of approximately 14 kDa, present in serum from diseased cows, proportionally to the serum SAA concentration as measured by ELISA [17].
• The identity of the isolated protein was checked by Western blotting following SDS-urea-PAGE using antisera raised against the purified protein fraction (SAA) and Amyloid A (AA) [17].

References