Related Experiment Videos
DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA)
Biochemical Genetics
|December 1, 1986
Summary
Researchers cloned and sequenced human Serum Amyloid A (SAA) cDNAs to understand its role in amyloidosis. This study investigates primary SAA structures potentially linked to amyloid fibril formation.
Area of Science:
- Molecular Biology
- Biochemistry
- Genetics
Background:
- Serum amyloid A (SAA) is an acute-phase reactant and precursor to amyloid A protein.
- SAA forms the major component of fibril deposits in reactive amyloidosis.
- The specific factors driving SAA conversion to amyloid A protein and fibril deposition remain unknown.
Purpose of the Study:
- To investigate the role of SAA primary structure in amyloid formation.
- To clone and determine the nucleotide sequence of human SAA-specific cDNAs.
Main Methods:
- Oligonucleotide probe selection of SAA-specific cDNAs.
- Differential screening using a PstI site to identify distinct SAA cDNA clones (pSAA21 and pSAA82).
- Complete nucleotide sequence determination of pSAA82 cDNA.
Main Results:
- Successfully cloned and sequenced human SAA-specific cDNAs.
- Identified two distinct full-length SAA cDNAs, pSAA21 and pSAA82, differing by a PstI site.
- Determined the complete nucleotide sequence of pSAA82 cDNA.
Conclusions:
- The nucleotide sequences of human SAA cDNAs have been elucidated.
- Multiple human SAA alleles may exist.
- Differential expression of SAA alleles could be crucial for amyloid formation.