Mink Serum Amyloid a Protein — Expression and Primary Structure of Amyloidogenic and Non-Amyloidogenic Isotypes

Marhaug, G.; Husby, Gunnar; Nordstoga, K.; Dowton, S. Bruce

doi:10.1007/978-94-011-3284-8_9

Cited by 10 publications

(29 citation statements)

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“…In other mammalian species the SAA family members are less well defined. There are at least three transcribed A‐SAA genes in dog [21], mink [22,23] and rabbit (for references, see [24,25,26,27]). In the case of horse, three SAA isoforms have been found in acute‐phase serum [28,29].…”

Section: The Serum Amyloid a (Saa) Familymentioning

confidence: 99%

Serum amyloid A, the major vertebrate acute‐phase reactant

Uhlar

Whitehead

1999

European Journal of Biochemistry

950

951

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The serum amyloid A (SAA) family comprises a number of differentially expressed apolipoproteins, acute-phase SAAs (A-SAAs) and constitutive SAAs (C-SAAs). A-SAAs are major acute-phase reactants, the in vivo concentrations of which increase by as much as 1000-fold during inflammation. A-SAA mRNAs or proteins have been identified in all vertebrates investigated to date and are highly conserved. In contrast, C-SAAs are induced minimally, if at all, during the acute-phase response and have only been found in human and mouse. Although the liver is the primary site of synthesis of both A-SAA and C-SAA, extrahepatic production has been reported for most family members in most of the mammalian species studied. In vitro, the dramatic induction of A-SAA mRNA in response to pro-inflammatory stimuli is due largely to the synergistic effects of cytokine signaling pathways, principally those of the interleukin-1 and interleukin-6 type cytokines. This induction can be enhanced by glucocorticoids. Studies of the A-SAA promoters in several mammalian species have identified a range of transcription factors that are variously involved in defining both cytokine responsiveness and cell specificity. These include NF-kB, C/EBP, YY1, AP-2, SAF and Sp1. A-SAA is also post-transcriptionally regulated. Although the precise role of A-SAA in host defense during inflammation has not been defined, many potential clinically important functions have been proposed for individual SAA family members. These include involvement in lipid metabolism/transport, induction of extracellular-matrix-degrading enzymes, and chemotactic recruitment of inflammatory cells to sites of inflammation. A-SAA is potentially involved in the pathogenesis of several chronic inflammatory diseases: it is the precursor of the amyloid A protein deposited in amyloid A amyloidosis, and it has also been implicated in the pathogenesis of atheroscelerosis and rheumatoid arthritis.

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Section: The Serum Amyloid a (Saa) Familymentioning

confidence: 99%

Serum amyloid A, the major vertebrate acute‐phase reactant

Uhlar

Whitehead

1999

European Journal of Biochemistry

950

951

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“…The plasma concentration of SAA may increase by 100-to 1000-fold [1] as a result mainly of enhanced transcription, but also by altered post-translational processing [3,4]. SAA is encoded by a family of genes in many animals [5,6] including man [7] and rabbit [8]. Several studies of the biosynthesis of SAA have identified the hepatocyte as the primary source of this protein [9], but expression of SAA in other cells is also found [10].…”

Section: Introductionmentioning

confidence: 99%

Cytokine-induced differential expression of serum amyloid A genes in fetal and neonatal rabbits

Rygg

1996

Clinical and Experimental Immunology

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SUMMARYSerum amyloid A (SAA) is an acute-phase plasma protein which increases 100-to 1000-fold in response to inflammatory stimuli. In this study pregnant rabbits were subjected to laparotomy and their fetuses were injected with lipopolysaccharide (LPS) or various cytokines. Newborn rabbits were likewise stimulated. Hepatic SAA mRNA was studied using Northern blot analyses and scanning densitometry. In vitro derived RNA was used as standard for quantitative mRNA analyses. Cytokine concentrations in amniotic fluid and serum were analysed by biological assays. Fetal rabbits responded to cytokine stimulation by increased hepatic SAA mRNA expression, both during late gestation and in the early neonatal period. However, differences in dose-responses, kinetics and mRNA concentrations were seen dependent on gestational age. IL-1 and tumour necrosis factor (TNF) induced hepatic accumulation of both SAA1, SAA2 and SAA3, while only SAA1 and SAA2 mRNA accumulation was seen after IL-6 stimulation. High levels of IL-1 and TNF found in amniotic fluid from LPS-stimulated fetal rabbits corresponded with high levels in fetal, but not in maternal, serum. High levels of IL-1 and TNF, but no IL-6, were seen in newborn control sera and in adult serum 1 day after a normal delivery. The study details the complexity of the cytokine-induced in vivo response of SAA mRNA in fetal and neonatal rabbits.

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“…We published the original amino acid sequence of mink SAA in 1987 [2] and the corresponding cDNA sequences in 1990 [3]. Certain discrepancies between the protein sequence and those deduced from cDNA prompted us to re-examine the former sequence.…”

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confidence: 99%

“…In Fig. 1 the revised amino acid sequence of mink SAA is compared with that originally published [2], the mink protein AA [4] and the two known cDNA sequences of mink SAA [3].…”

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confidence: 99%

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The Revised Amino Acid Sequence of Serum Amyloid A (SAA) Protein in Mink

Syversen¹,

Sletten²,

Marhaug

et al. 1993

Scand J Immunol

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The revised amino acid sequence of mink protein SAA was shown to be composed of 111 amino acid residues. The protein has an insertion of eight amino acid residues compared with that reported earlier. Microheterogeneities were observed in positions 6, 10, 24, 27, 67 and 71. The amino acid sequence is in accordance with the SAA mink cDNA sequences, except for the phenylalanine in position 6. The data indicate a third SAA gene in mink.

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Mink Serum Amyloid a Protein — Expression and Primary Structure of Amyloidogenic and Non-Amyloidogenic Isotypes

Cited by 10 publications

References 9 publications

Serum amyloid A, the major vertebrate acute‐phase reactant

Serum amyloid A, the major vertebrate acute‐phase reactant

Cytokine-induced differential expression of serum amyloid A genes in fetal and neonatal rabbits

The Revised Amino Acid Sequence of Serum Amyloid A (SAA) Protein in Mink

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