Characterization of amyloid protein AA and its serum precursor SAA in the horse.
Abstract: 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 antigenicity and the 10 first N-terminal amino acid residues that have been studied up to now. The bulk of SAA was present in the high-density lipoprotein complex in serum. Also SAA was heterogeneous with respect to size, most molecules having a molecular weight of 11,000, and a minority 9000.
Publication Date: 1986-06-01 PubMed ID: 3715410DOI: 10.1111/j.1365-3083.1986.tb02007.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study examines the characteristics of amyloid protein AA and its precursor, serum amyloid A (SAA), in horses. The researchers identified and analyzed these proteins from an afflicted horse and found similar structural characteristics between horse and human AA proteins, though distinct species-related antigenic specificity was observed.
Study Procedure
- The research began with the extraction of amyloid from the liver of a horse suffering from amyloidosis. This condition developed after several years of the horse being used for antibodies production to fight bacterial antigens.
- The identified amyloid fibrils were classified as the AA, or Amyloid A, type.
Protein Characterization
- The research team then identified two AA proteins which had molecular weights of 9000 and 11,000.
- These proteins showed identical partial N-terminal amino acid sequences.
Homology and Specificity Observations
- They further analyzed the structure of the AA proteins and saw a distinct similarity in their structures with AA proteins from other species, including humans.
- Even though resemblance was observed, unique species-related antigenic specificity was also seen.
Serum Amyloid A (SAA)
- Serum amyloid A (SAA), the precursor to AA was studied as well. SAA was harvested from horse serum during the acute phase of septic abortion.
- The SAA was found to have identical antigenicity and initial 10 N-terminal amino acid residues characteristics as AA.
- Most of the SAA was present as part of the high-density lipoprotein complex in serum.
- SAA demonstrated heterogeneity in size, with most molecules having molecular weight of 11,000, and a minority having molecular weight of 9000.
Cite This Article
APA
Husebekk A, Husby G, Sletten K, Marhaug G, Nordstoga K.
(1986).
Characterization of amyloid protein AA and its serum precursor SAA in the horse.
Scand J Immunol, 23(6), 703-709.
https://doi.org/10.1111/j.1365-3083.1986.tb02007.x Publication
Researcher Affiliations
MeSH Terms
- Amino Acid Sequence
- Amyloid / analysis
- Amyloidosis / metabolism
- Amyloidosis / veterinary
- Animals
- Horse Diseases / metabolism
- Horses / blood
- Horses / physiology
- Liver / analysis
- Molecular Weight
- Serum Amyloid A Protein / analysis
- Species Specificity
Citations
This article has been cited 4 times.- Palmisano M, Javsicas L, McNaughten J, Gamsjäger L, Renaud DL, Gomez DE. Effect of plasma transfusion on serum amyloid A concentration in healthy neonatal foals and foals with failure of transfer of passive immunity. J Vet Intern Med 2023 Mar;37(2):697-702.
- Witkowska-Piłaszewicz OD, Żmigrodzka M, Winnicka A, Miśkiewicz A, Strzelec K, Cywińska A. Serum amyloid A in equine health and disease. Equine Vet J 2019 May;51(3):293-298.
- Meek RL, Eriksen N, Benditt EP. Serum amyloid A in the mouse. Sites of uptake and mRNA expression. Am J Pathol 1989 Aug;135(2):411-9.
- Linke RP, Trautwein G. Immunoglobulin lambda-light-chain-derived amyloidosis (A lambda) in two horses. Blut 1989 Mar;58(3):129-32.
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