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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.
Influence of age and foaling on plasma protein electrophoresis and serum amyloid A and their possible role as markers of equine neonatal septicaemia.
Veterinary journal (London, England : 1997)    July 17, 2007   Volume 176, Issue 3 393-396 doi: 10.1016/j.tvjl.2007.05.018
Paltrinieri S, Giordano A, Villani M, Manfrin M, Panzani S, Veronesi MC.A field study was undertaken to investigate plasma protein electrophoresis (PPE) and serum amyloid A (SAA) concentrations at 1, 3 and 7 days of age in foals born by oxytocin-induced (group A, n =17) or spontaneous (group B, n =12) parturition. The putative diagnostic role of PPE and SAA in four septicaemic foals was also examined. At birth, beta-gamma-globulins were higher in group B, and then increased in both groups, probably due to colostrum intake. At day 3, no significant differences between the groups were detectable. In both groups, SAA values increased from day 0 to day 3, then decreas...
Amyloid A in equine colostrum and early milk.
Veterinary immunology and immunopathology    June 29, 2007   Volume 121, Issue 1-2 150-155 doi: 10.1016/j.vetimm.2007.06.030
Duggan VE, Holyoak GR, MacAllister CG, Cooper SR, Confer AW.The objective of this study was to investigate the protein, amyloid A3 (AA3), in equine colostrum and early milk. We hypothesized that AA3 was consistently present in equine colostrum and early milk, that no correlation existed between serum and colostrum concentrations of this protein in individual mares at parturition and that colostrum/milk concentrations of this mammary protein may be affected by age, breed, length of gestation and/or induction of parturition. Thirty-eight peripartum mares and seven non-pregnant, non-lactating mares were included in the study. Mean serum concentrations of ...
Concentrations of serum amyloid A in serum and synovial fluid from healthy horses and horses with joint disease.
American journal of veterinary research    October 4, 2006   Volume 67, Issue 10 1738-1742 doi: 10.2460/ajvr.67.10.1738
Jacobsen S, Thomsen MH, Nanni S.To determine serum amyloid A (SAA) concentrations in serum and synovial fluid from healthy horses and horses with joint disease and assess the effect of repeated arthrocentesis on SAA concentrations in synovial fluid. Animals-10 healthy horses and 21 horses with various types of joint disease. Methods: Serum and synovial fluid samples were obtained from each horse. In 5 of the 10 healthy horses, arthrocentesis was repeated 9 times. Concentrations of SAA were determined via immunoturbidometry. Results: Serum and synovial fluid SAA concentrations were less than the assay detection limit in healt...
Influence of induction of parturition on the neonatal acute phase response in foals.
Theriogenology    September 18, 2006   Volume 67, Issue 2 372-381 doi: 10.1016/j.theriogenology.2006.06.015
Duggan VE, Holyoak GR, MaCallister CG, Confer AW.The objectives of the present study were to determine whether induction of parturition in mares at term with low doses of oxytocin (2.5 i.u. i.v. every 20 min) affected the incidence of peri-partum complications or inflammatory responses in the neonatal foal. Parturition was induced in 11 of 26 mares and the remainder foaled spontaneously. Serum concentrations of amyloid A (AA; an acute phase protein) were measured (with a commercial ELISA) from 0 to 72 h postpartum in 18 of the neonatal foals. The incidence of dystocia and premature placental separation was higher in induced mares (2 of 11 an...
Serum amyloid A isoforms in serum and synovial fluid in horses with lipopolysaccharide-induced arthritis.
Veterinary immunology and immunopathology    December 5, 2005   Volume 110, Issue 3-4 325-330 doi: 10.1016/j.vetimm.2005.10.012
Jacobsen S, Niewold TA, Halling-Thomsen M, Nanni S, Olsen E, Lindegaard C, Andersen PH.The aim of the study was to determine the intraarticular serum amyloid A (SAA) response pattern in horses with inflammatory arthritis. Inflammatory arthritis was induced by injection of lipopolysaccharide (LPS) into the radiocarpal joint of four horses. Serum and synovial fluid (SF) samples were collected before and at 4, 8, 12, 24, 48, 72, 96, and 144 h after injection. Concentrations of SAA were measured by immunoturbidometry, and expression of SAA isoforms was visualized by denaturing isoelectric focusing and Western blotting. The LPS injection caused systemic and local clinical signs of in...
Use of serum amyloid A and other acute phase reactants to monitor the inflammatory response after castration in horses: a field study.
Equine veterinary journal    November 22, 2005   Volume 37, Issue 6 552-556 doi: 10.2746/042516405775314853
Jacobsen S, Jensen JC, Frei S, Jensen AL, Thoefner MB.Early recognition of excessive inflammation and infectious complications after surgery, leading to early institution of therapy, reduces post operative discomfort and facilitates recovery. Because serum amyloid A (SAA) is a highly sensitive marker of inflammation, measurements of SAA and other acute phase reactants in the equine surgical patient may be valuable in assisting clinical assessment of post operative inflammation. Objective: To investigate changes in inflammatory markers after castration and to correlate levels of acute phase reactants with clinical severity of inflammation after ca...
Concentrations of serum amyloid A and lipopolysaccharide-binding protein in horses with colic.
American journal of veterinary research    November 3, 2005   Volume 66, Issue 9 1509-1516 doi: 10.2460/ajvr.2005.66.1509
Vandenplas ML, Moore JN, Barton MH, Roussel AJ, Cohen ND.To determine concentrations of 2 acute-phase proteins (serum amyloid A [SAA] and lipopolysaccharide-binding protein [LBP]) in serum samples obtained from horses with colic and identify relationships among these acute-phase proteins and clinical data. Methods: 765 horses with naturally developing gastrointestinal tract diseases characterized by colic (ie, clinical signs indicative of abdominal pain) and 79 healthy control horses; all horses were examined at 2 university teaching hospitals. Methods: Serum concentrations of SAA and LBP were determined by immunoturbidometric and dot-blot assays, r...
Evaluation of a commercially available human serum amyloid A (SAA) turbidometric immunoassay for determination of equine SAA concentrations.
Veterinary journal (London, England : 1997)    June 13, 2005   Volume 172, Issue 2 315-319 doi: 10.1016/j.tvjl.2005.04.021
Jacobsen S, Kjelgaard-Hansen M, Hagbard Petersen H, Jensen AL.The aim of the present study was to evaluate whether equine serum amyloid A (SAA) concentrations could be measured reliably with a turbidometric immunoassay (TIA) developed for use with human serum. Intra- and inter-assay imprecision were evaluated by multiple measurements on equine serum pools. Assay inaccuracy was determined by linearity under dilution. The assay was subsequently used for measuring SAA concentrations in clinically healthy horses, horses with inflammatory diseases, horses with non-inflammatory diseases, and in horses before and after castration. In pools with low, intermediat...
Study of serum amyloid A concentrations as a means of achieving early diagnosis of Rhodococcus equi pneumonia.
Equine veterinary journal    May 17, 2005   Volume 37, Issue 3 212-216 doi: 10.2746/0425164054530704
Cohen ND, Chaffin MK, Vandenplas ML, Edwards RF, Nevill M, Moore JN, Martens RJ.Prognosis of Rhodococcus equi pneumonia can be challenging because the course of the disease is often insidious and overt clinical signs are subtle. Early diagnosis is considered desirable because it may offer the chance of more successful implementation of treatment and, thereby, improved outcome. Serological tests have previously failed to be accurate for early detection or diagnosis. Measurement of serum amyloid A (SAA) prior to and at the time of clinical signs was therefore chosen in order to assess its potential clinical use. Objective: To determine whether SAA concentrations differentia...
Effects of surgery on the acute phase response in clinically normal and diseased horses.
The Veterinary record    April 26, 2005   Volume 156, Issue 17 538-542 doi: 10.1136/vr.156.17.538
Pollock PJ, Prendergast M, Schumacher J, Bellenger CR.The serum concentrations of serum amyloid A, haptoglobin and fibrinogen were measured in a group of horses before and at intervals after elective and non-elective surgery, and in a control group of normal horses. There was a significant, rapid and repeatable increase in the concentration of serum amyloid A in response to both elective and non-elective surgery. In the control horses its serum concentration was within the normal range, from 0 to 0.2 microg/ml. Twenty-four hours after elective surgery its mean peak concentration was 16.4 microg/ml, and after non-elective surgery it was 27.3 micro...
Serum amyloid A (SAA) as an aid in the management of infectious disease in the foal: comparison with total leucocyte count, neutrophil count and fibrinogen.
Equine veterinary journal    November 29, 2002   Volume 34, Issue 7 693-698 doi: 10.2746/042516402776250360
Hultén C, Demmers S.Differentiation between infectious and noninfectious disease and rapid initiation of accurate treatment are essential in managing diseases in the neonatal and young foal. Identification of useful inflammatory markers for these purposes is, therefore, of great importance. The aim of this study was to compare the responses of the acute phase protein serum amyloid A (SAA) with the responses of fibrinogen and total leucocyte and neutrophil counts in infectious diseases encountered in the young foal, and to assess whether SAA measurements give additional information useful in the management of thes...
Dynamics in serum of the inflammatory markers serum amyloid A (SAA), haptoglobin, fibrinogen and alpha2-globulins during induced noninfectious arthritis in the horse.
Equine veterinary journal    November 29, 2002   Volume 34, Issue 7 699-704 doi: 10.2746/042516402776250405
Hultén C, Grönlund U, Hirvonen J, Tulamo RM, Suominen MM, Marhaug G, Forsberg M.Despite the importance of noninfectious joint diseases in equine medicine, little is known about the acute phase response which may be elicited if the local inflammatory process of noninfectious arthritis is sufficiently strong, Therefore the aim of this study was to monitor the systemic inflammatory response during experimentally-induced noninfectious arthritis by studying the dynamics in serum of the acute phase proteins serum amyloid A (SAA), haptoglobin, fibrinogen and alpha2-globulins. Twenty-four Standardbred horses, age 3-7 years, found healthy on thorough clinical, radiological, haemat...
Neutrophil functions and serum IgG in growing foals.
Equine veterinary journal    January 5, 2002   Volume 33, Issue 7 676-680 doi: 10.2746/042516401776249327
Demmers S, Johannisson A, Gröndahl G, Jensen-Waern M.The aim of this study was to investigate the phagocytic and killing capacities as well as expression of CD18 of neutrophils obtained from healthy foals from birth to age 8 months. Blood was taken from 6 Standardbred foals at 7 time-points between ages 2-56 days and thereafter once a month. For comparison, cells from 16 mature horses were evaluated. Neutrophil phagocytosis of yeast cells was assessed by flow cytometry after opsonisation with mature pooled serum, autologous serum or anti-yeast IgG. The killing capacity of the neutrophils, as indicated by the oxidative burst, was monitored by che...
Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum.
Veterinary immunology and immunopathology    December 4, 2001   Volume 83, Issue 3-4 203-211 doi: 10.1016/s0165-2427(01)00380-4
McDonald TL, Larson MA, Mack DR, Weber A.Mammary-associated serum amyloid A 3 (M-SAA3) was secreted at highly elevated levels in bovine, equine and ovine colostrum and found at lower levels in milk 4 days postparturition. N-terminal sequencing of the mature M-SAA3 protein from all the three species revealed a conserved four amino acid motif (TFLK) within the first eight residues. This motif has not been reported to be present in any of the hepatically-produced acute phase SAA (A-SAA) isoforms. Cloning of the bovine M-Saa3 cDNA from mammary gland epithelial cells revealed an open reading frame that encoded a precursor protein of 131 a...
Measurement of serum amyloid A in the neonatal foal using a latex agglutination immunoturbidimetric assay: determination of the normal range, variation with age and response to disease.
Equine veterinary journal    November 27, 2001   Volume 33, Issue 6 599-603 doi: 10.2746/042516401776563472
Stoneham SJ, Palmer L, Cash R, Rossdale PD.This paper describes the use of a latex agglutination assay to measure serum amyloid A (SAA) in the neonatal foal. The normal range and response to clinical disease was determined. This retrospective study evaluated SAA concentrations over the first 3 days postpartum of 226 Thoroughbred foals judged to be clinically healthy. The normal range for each day was determined; levels were found to be significantly highest on Day 2 (Day 1 vs. Day 2 P<0.0001). The 95th percentile for Days 1-3 was 27.1 mg/l. Clinical records of 133 foals, presented as first or second opinion cases, were evaluated. Fo...
Molecular cloning and sequencing of equine cDNA encoding serum amyloid A (SAA).
Veterinary immunology and immunopathology    January 4, 2001   Volume 77, Issue 3-4 321-327 doi: 10.1016/s0165-2427(00)00239-7
Ma Z, Mizukoshi T, Khatlani TS, Okuda M, Onishi T.The serum amyloid A (SAA) protein is a characteristic and sensitive acute phase reactant in all vertebrates investigated. We molecularly cloned the equine cDNA encoding SAA from the liver of a healthy horse by polymerase chain reaction (PCR). The cloned cDNA is 480 bases in length, and contains an open reading frame (ORF) of 387 nucleotides encoding a precursor SAA protein of 128 amino acids. The precursor of horse SAA seems to have an 18-residue signal peptide and differs from the reported amino acid sequences of the horse SAA by substitution of valine at residue 81. It shows high homology wi...
The acute phase protein serum amyloid A (SAA) as an inflammatory marker in equine influenza virus infection.
Acta veterinaria Scandinavica    August 5, 2000   Volume 40, Issue 4 323-333 doi: 10.1186/BF03547012
Hultén C, Sandgren B, Skiöldebrand E, Klingeborn B, Marhaug G, Forsberg M.The acute phase protein serum amyloid A (SAA) has proven potentially useful as an inflammatory marker in the horse, but the knowledge of SAA responses in viral diseases is limited. The aim of this study was to evaluate SAA as a marker for acute equine influenza A2 (H3N8) virus infection. This is a highly contagious, serious condition that inflicts suffering on affected horses and predisposes them to secondary bacterial infections and impaired performance. Seventy horses, suffering from equine influenza, as verified by clinical signs and seroconversion, were sampled in the acute (the first 48 h...
A non-competitive chemiluminescence enzyme immunoassay for the equine acute phase protein serum amyloid A (SAA) — a clinically useful inflammatory marker in the horse.
Veterinary immunology and immunopathology    August 7, 1999   Volume 68, Issue 2-4 267-281 doi: 10.1016/s0165-2427(99)00027-6
Hultén C, Tulamo RM, Suominen MM, Burvall K, Marhaug G, Forsberg M.A non-competitive chemiluminescence enzyme immunoassay for measuring serum amyloid A (SAA) in equine serum was developed. A polyclonal anti-equine-amyloid A antiserum specific for equine SAA was utilized, and the assay was standardized using highly purified equine SAA. An acute phase horse serum was calibrated against the purified SAA and was used as standard when running the assay. Serum SAA concentrations in the range of 3-1210 mg/l could be measured. The reference range of SAA in clinically healthy adult horses was <7 mg/l. The clinical validation of the assay comprised the SAA responses...
The acute phase serum amyloid A protein (SAA) in the horse: isolation and characterization of three isoforms.
Veterinary immunology and immunopathology    July 1, 1997   Volume 57, Issue 3-4 215-227 doi: 10.1016/s0165-2427(97)00021-4
Hultén C, Sletten K, Foyn Bruun C, Marhaug G.Serum amyloid A (SAA) from acute phase horse serum was isolated using hydrophobic interaction chromatography, gel filtration and ion exchange chromatography. Three SAA isoforms with different isoelectric points, i.e. SAA pI 8.0, SAA pI 9.0 and SAA pI 9.7, were identified by two-dimensional electrophoresis and further characterized with amino acid sequence analysis. These isoforms were found in similar concentrations in all animals investigated, with SAA pI 9.7 constituting about half of the total SAA content. Partial amino acid sequence analysis verified the previously published heterogeneous ...
Sandwich enzyme-linked immunosorbent assay for quantitative measurement of serum amyloid A protein in horses.
American journal of veterinary research    October 1, 1995   Volume 56, Issue 10 1286-1291 
Satoh M, Fujinaga T, Okumura M, Hagio M.To measure the concentration of serum amyloid A (sAA) protein in horses, a sensitive and highly reproducible sandwich (ELISA) was established, using affinity purified SAA antibody. Results of the ELISA were found to have a high correlation (r = 0.95) with those of the single radial immunodiffusion test. Equine SAA concentration was measured by use of this ELISA. In clinically normal horses, the concentration of SAA was high immediately after birth to 2 weeks of age. After that, SAA concentration had periodic fluctuations in the range of approximately 1.0 to 30 micrograms/ml. Mean (+/- SD)) con...
Evaluation of serum amyloid A protein as an acute-phase reactive protein in horses.
The Journal of veterinary medical science    December 1, 1993   Volume 55, Issue 6 1011-1016 doi: 10.1292/jvms.55.1011
Nunokawa Y, Fujinaga T, Taira T, Okumura M, Yamashita K, Tsunoda N, Hagio M.Serum amyloid A protein (SAA) was isolated from equine acute-phase serum by repeating Sephadex G-75 gel filtration 3 times. Quantitative measurement of equine SAA was performed by the single radial immunodiffusion technique with rabbit anti-equine SAA serum. In clinically normal horses, the SAA concentration remained relatively high from immediately after birth up to 1 week of age. After this the concentration showed periodic fluctiation in the range of approximately 13 to 30 micrograms/ml. The mean (+/- SD) concentration of SAA in foals ( or = 18 months old) was 19.37 +/- 9.41 and 21.53 +/- 9...
Diagnostic and prognostic value of serum protein electrophoresis in horses with chronic diarrhoea.
Equine veterinary journal    July 1, 1993   Volume 25, Issue 4 324-326 doi: 10.1111/j.2042-3306.1993.tb02973.x
Mair TS, Cripps PJ, Ricketts SW.No abstract available
Isolation, characterization, and quantitative analysis of C-reactive protein from horses.
American journal of veterinary research    August 1, 1990   Volume 51, Issue 8 1215-1220 
Takiguchi M, Fujinaga T, Naiki M, Mizuno S, Otomo K.C-reactive protein (CRP) was isolated from equine serum by use of calcium-dependent affinity chromatography conjugated pneumococcal C-polysaccharide, anion exchange chromatography, and gel filtration. It was identified as genuine CRP by its immunochemical cross-reactivity with anti-human CRP, its homology with human CRP in amino acid composition, and its pentameric structure as revealed by electron microscopy. Purified equine CRP had a molecular weight of approximately 118,000 and was composed of 5 identical, nonglycosylated and noncovalently associated subunits with molecular weight of approx...
The primary structure of equine serum amyloid A (SAA) protein.
Scandinavian journal of immunology    July 1, 1989   Volume 30, Issue 1 117-122 doi: 10.1111/j.1365-3083.1989.tb01195.x
Sletten K, Husebekk A, Husby G.The complete amino acid sequence of equine serum amyloid A (SAA) was elucidated. The protein consists of 110 amino acid residues and contains an 8-amino acid residue insertion tentatively located between positions 69 and 70, as compared with human SAA. Microheterogeneities were detected at positions 16, 44, and 59, compatible with the existence of more than one SAA gene in the horse. This corresponds to the situation in man and mouse. Pronounced homology with SAA from man and several animal species was observed, thus confirming the conserved structure of this acute phase reactant and apoprotei...
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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