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Topic:Serum Amyloid A

Serum Amyloid A (SAA) is a prominent acute phase protein in horses, synthesized predominantly by the liver in response to inflammatory stimuli, infections, or tissue damage. SAA is a component of the equine immune response and serves as a biomarker for the detection and monitoring of various health conditions. Its concentration in the bloodstream can increase significantly during inflammatory episodes, providing a measurable indicator of physiological stress and disease activity. This topic page aggregates peer-reviewed research studies and scholarly articles that explore the role, regulation, and clinical relevance of Serum Amyloid A in equine health, offering insights into its application in veterinary diagnostics.
Serum amyloid A protein (SAA) in horses: objective measurement of the acute phase response.
Equine veterinary journal    March 1, 1989   Volume 21, Issue 2 106-109 doi: 10.1111/j.2042-3306.1989.tb02108.x
Pepys MB, Baltz ML, Tennent GA, Kent J, Ousey J, Rossdale PD.A sensitive and precise immunoassay for equine serum amyloid A protein (SAA) was established and used to determine, for the first time, the circulating concentration of this protein in health and disease. As in other species, equine SAA was present only at trace levels in healthy animals but behaved as an extremely sensitive and rapidly responding acute phase reactant following most forms of tissue injury, infection and inflammation, objectively reflecting the extent and activity of disease. Measurements of SAA should make a significant contribution to diagnosis and management of viral and bac...
Characterization of amyloid protein AA and its serum precursor SAA in the horse.
Scandinavian journal of immunology    June 1, 1986   Volume 23, Issue 6 703-709 doi: 10.1111/j.1365-3083.1986.tb02007.x
Husebekk A, Husby G, Sletten K, Marhaug G, Nordstoga K.Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to be of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to...
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