Molecular cloning and sequencing of equine cDNA encoding serum amyloid A (SAA).
Abstract: 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 with SAA amino acid sequence of other species such as dog (80.6%), mink (77.5%), human (76.9%) and duck (71.9%). An insertion of eight amino acids at residues between 85 and 92, as compared to human SAA, has also been found in horse SAA. The availability of the equine SAA cDNA will provide a useful reagent for studying its role in diseased horses.
Publication Date: 2001-01-04 PubMed ID: 11137129DOI: 10.1016/s0165-2427(00)00239-7Google Scholar: Lookup
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- Journal Article
Summary
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The research involves the successful cloning and sequencing of the DNA sequence that codes for the Serum Amyloid A (SAA) protein in horses. This protein is known to play a key role in the acute phase response in all animals, thus, understanding its genetic basis may provide clues on how to manage diseases in animals, particularly horses.
Methods and Findings
- The researchers extracted the Serum Amyloid A (SAA) gene from the liver of a healthy horse and cloned it using a laboratory technique called Polymerase Chain Reaction (PCR).
- The cloned sequence (cDNA) was found to be 480 bases long and contained an open reading frame (ORF) of 387 nucleotides. This implies the protein which this sequence encodes is 128 amino acids long.
- Compared to prior research findings, a notable difference in the horse’s SAA protein sequence was observed at residue 81 where valine had been substituted.
- The team observed similarities between the horse SAA protein and those from dogs, minks, humans, and ducks. These similarities ranged from 71.9% (with ducks) up to 80.6% (with dogs).
- Unique from human SAA, there was an insertion of eight additional amino acids in the horse SAA between residues 85 and 92.
Implications of Research
- This cloned gene sequence provides a useful medical tool to further understand the SAA protein and its function in horses.
- As the SAA protein is a primary reactive for acute phase response in animals, this generated sequence can assist in the investigation of associated diseases in horses.
- The high sequence similarity between species highlights the universality of the SAA protein’s structure and function across different animals, showcasing potential relevance beyond equine health.
- The relative differences observed in the horse SAA protein, such as the substitution at residue 81 and the insertion between residues 85 and 92, suggest possible specificities in how acute phase response occurs in horses.
Cite This Article
APA
Ma Z, Mizukoshi T, Khatlani TS, Okuda M, Onishi T.
(2001).
Molecular cloning and sequencing of equine cDNA encoding serum amyloid A (SAA).
Vet Immunol Immunopathol, 77(3-4), 321-327.
https://doi.org/10.1016/s0165-2427(00)00239-7 Publication
Researcher Affiliations
- Laboratory of Veterinary Internal Medicine, Faculty of Agriculture, Yamaguchi University, 1677-1 Yoshida, 753-8515, Yamaguchi, Japan.
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Cloning, Molecular
- DNA, Complementary / chemistry
- Dogs
- Horses
- Humans
- Molecular Sequence Data
- Serum Amyloid A Protein / chemistry
- Serum Amyloid A Protein / genetics
Citations
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