Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor

Ericsson, Lowell H.; Eriksen, Nils; Walsh, Kenneth A.; Benditt, Earl P.

doi:10.1016/0014-5793(87)81008-6

Cited by 65 publications

(36 citation statements)

References 21 publications

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“…Serum amyloid A (SAA) is a family of highly homologous high density lipoprotein (HDL) apoproteins found in mammals and ducks (1)(2)(3)(4). They are normally present in only trace amounts but are elevated up to 1000-fold and reach concentrations of 1 mg/ml during an acute-phase response (5,6).…”

mentioning

confidence: 99%

Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages.

Meek

Eriksen

Benditt

1992

Proc. Natl. Acad. Sci. U.S.A.

145

102

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The serum amyloid A (SAA) proteins make up a multigene family of apolipoproteins associated with high density lipoproteins. They are of ancient origin; the filnding of a highly homologous protein in mammals and ducks indicates that SAAs have been in existence for at least 300 million years. The interspecies similarity among the SAAs makes the mouse, in which they have been most thoroughly studied, a reasonable model to use for defining the function(s) of this family of proteins in humans. Originally it was observed that the SAA proteins were made in the liver and represented a set ofproteins belonging to acute-phase reactants. SAA3 is a unique member of the SAA multigene family in mice in that its mRNA is also expressed in extrahepatic tissues by a variety of cell types, mainly macrophages and adipocytes. To date, nothing has been reported regarding the fate or function of the SAA3 translation product. To identify the SAA3 protein, we developed SAA3-specific antibodies by immunizing rabbits against a portion of SAA3 protein synthesized in a bacterial fusion protein expression system. Electroimmunoblot analysis of serum and lipoprotein fractions of it showed SAA3 to be associated with high density lipoproteins of mice treated with lipopolysaccharide. Furthermore, a continuous mouse macrophage cell line (J-774.1), when exposed to lipopolysaccharide, expressed SAA3 mRNA in a dose-dependent manner and secreted SAA3 protein. The expression and secretion of SAA3 by macrophages stimulated with lipopolysaccharide suggest a role for this SAA in local responses to injury and inflammation.

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mentioning

confidence: 99%

Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages.

Meek

Eriksen

Benditt

1992

Proc. Natl. Acad. Sci. U.S.A.

145

102

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“…However, rats do not develop amyloidosis and no SAA has been found in rat HDL following injury. The apparent absence ofexpression in the rat has been puzzling because of the high degree of conservation of the SAA gene(s) in other mammals and the duck (8)(9)(10)(11)(12).…”

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confidence: 99%

Rat tissues express serum amyloid A protein-related mRNAs.

Meek

Benditt

1989

Proc. Natl. Acad. Sci. U.S.A.

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Serum amyloid A (SAA) is a small (12 kDa) acute-phase apoprotein of high density lipoprotein found in mammals. It is also the precursor to amyloid protein A, the main protein constituent of fibrils found in amyloidosis secondary to chronic or recurrent inflammation-e.g., rheumatoid arthritis. However, rats do not develop amyloidosis and SAA is not an apoprotein of rat high density lipoprotein; thus rats appear to be an exception in regard to expression of SAA genes. We report here that rats do have representatives of the SAA gene family and express two distinct SAA mRNAs. Moreover, the pattern of genes expressed among tissues, and their induction by inflammatory agents, is similar to that of related mouse genes. RNA from various tissues of normal and injured rats was examined by RNA blot hybridization with SAA cDNA and complementary RNA probes for the three murine SAA genes. A SAA mRNA of '400 nucleotides related to mouse SAA1 and SAA2 mRNAs reached a high level in liver 24 hr after injection of bacterial lipopolysaccharide. No extrahepatic tissues were found to express the SAA1/SAA2-related mRNA. Turpentine induced two hepatic SAA1/SAA2-related mRNAs of "400 and -"500 nucleotides in length. Liver SAA,/SAA2-related mRNA hybrid selected and translated in a wheat germ protein-synthesizing system, from lipopolysaccharide-and turpentine-injected rats, produced a single protein with an estimated molecular mass of 8 kDa. This rat liver SAA-related mRNA appears to lack a highly conserved coding region for portions of two amphipathic helical domains and the joining sequence. An mRNA related to mouse SAA3 was found expressed at a high level in lung after lipopolysaccharide but not following turpentine injection. This mRNA was also expressed at high levels in ileum and large intestine of control rats and was not found in the liver of control or challenged rats. These observations show that the SAA gene family is present and expressed in rats and that its expression is found under situations similar to those found in mice. This lends support for the importance of the SAA gene family in the response to injury by vertebrates.A complex series of systemic and metabolic changes occur in vertebrates in response to injury or infection. These reactions are collectively termed the acute-phase response. Conspicuous among these events is the rise in concentration of certain plasma proteins of hepatic origin termed acute-phase proteins (1). Serum amyloid A (SAA) is a family of apolipoproteins found mainly associated with high density lipoprotein (HDL) (2, 3). Members of this family are acute-phase proteins (1,4,5). In addition, part of the SAA is a component of amyloid deposits associated with inflammatory disease. The major protein of these deposits is amyloid A protein (AA), comprising the NH2-terminal 76 residues of the circulating precursor SAA (6, 7). However, rats do not develop amyloidosis and no SAA has been found in rat HDL following injury. The apparent absence ofexpression in the rat has been puzzling because of the...

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“…In addition, the falcon sequence was compared with the five published sequences that have been determined from tissue amyloid protein and/or from the nucleotide sequences of ducks, geese, and chickens [27][28][29][30][31] and compared with humans [54].…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

“…The 8-23 segment represents a relatively variable region of avian AA when compared with the other more complete sequences of 109 amino acids of ducks and geese [27][28][29][30], of 106 amino acids in a duck [28] and 57 residues in a chicken AA protein (31). So, within the sequence from position 24 to the C-terminus, only one single amino acid exchange occurs at position 70 between ducks and geese (marked in red) ( Figure 6).…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

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Increasing fatal AA amyloidosis in hunting falcons and how to identify the risk: a report from the United Arab Emirates

Hampel

Kinne

Wernery

et al. 2009

Amyloid

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Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor

Cited by 65 publications

References 21 publications

Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages.

Murine serum amyloid A3 is a high density apolipoprotein and is secreted by macrophages.

Rat tissues express serum amyloid A protein-related mRNAs.

Increasing fatal AA amyloidosis in hunting falcons and how to identify the risk: a report from the United Arab Emirates

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