Serum amyloid A (SAA) protein is one of the two major human acute phase reactants and an apoprotein of high density lipoprotein. Its function is still obscure. An undesirable consequence of a prolonged acute phase response is reactive amyloidosis, in susceptible individuals. The protein subunit (AA) of amyloid fibrils has sequence homology to the 76 amino acid residues from the N-terminus of SAA, and product precursor relationship has recently been demonstrated (1). However, the mechanism for amyloidogenesis is still far from clear, and is likely to be multifactorial. Amino acid sequence determination of the protein subunit of murine amyloid fibrils was shown to be the same: SAA2, although there is a gene family of SAA (2) consisting of 3 genes and 1 pseudogene. Moreover, individual gene expression in the liver and other tissues during an inflammatory response is different (3). Thus, raising the possibility that one gene product is more amyloidogenic. The predisposing factor may be related to local clearance. It is therefore important to elucidate the control of isotype expression as well as cleavage mechanisms.
KeywordsAmyloid Fibril Nuclear Protein Extract Aminoacid Sequence Individual Gene Expression Retarded Band
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