Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily

Christine Rossmann; Christian Windpassinger; Daniela Brunner; Alenka Kovacevic; Natascha Schweighofer; Roland Malli; Rufina Schuligoi; Andreas Prokesch; Barbara Kluve-Beckerman; Wolfgang F. Graier; Dagmar Kratky; Wolfgang Sattler; Ernst Malle

doi:10.1016/j.bbrc.2014.07.054

Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily

Christine Rossmann, Christian Windpassinger, Daniela Brunner, Alenka Kovacevic, Natascha Schweighofer, Roland Malli, Rufina Schuligoi, Andreas Prokesch, Barbara Kluve-Beckerman, Wolfgang F. Graier, Dagmar Kratky, Wolfgang Sattler, Ernst Malle^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie (6480)

Publikation: Beitrag in einer Fachzeitschrift › Artikel › Begutachtung

Abstract

The serum amyloid A (SAA) family of proteins is encoded by multiple genes, which display allelic variation and a high degree of homology in mammals. The SAA1/2 genes code for non-glycosylated acute-phase SAA1/2 proteins, that may increase up to 1000-fold during inflammation. The SAA4 gene, well characterized in humans (hSAA4) and mice (mSaa4) codes for a SAA4 protein that is glycosylated only in humans. We here report on a previously uncharacterized SAA4 gene (rSAA4) and its product in Rattus norvegicus, the only mammalian species known not to express acute-phase SAA. The exon/intron organization of rSAA4 is similar to that reported for hSAA4 and mSaa4. By performing 5′- and 3′RACE, we identified a 1830-bases containing rSAA4 mRNA (including a GA-dinucleotide tandem repeat). Highest rSAA4 mRNA expression was detected in rat liver. In McA-RH7777 rat hepatoma cells, rSAA4 transcription was significantly upregulated in response to LPS and IL-6 while IL-1α/β and TNFα were without effect. Luciferase assays with promoter-truncation constructs identified three proximal C/EBP-elements that mediate expression of rSAA4 in McA-RH7777 cells. In line with sequence prediction a 14-kDa non-glycosylated SAA4 protein is abundantly expressed in rat liver. Fluorescence microscopy revealed predominant localization of rSAA4-GFP-tagged fusion protein in the ER.

Originalsprache	englisch
Seiten (von - bis)	1643-1649
Seitenumfang	7
Fachzeitschrift	Biochemical and Biophysical Research Communications
Jahrgang	450
Ausgabenummer	4
DOIs	https://doi.org/10.1016/j.bbrc.2014.07.054
Publikationsstatus	Veröffentlicht - 8 Aug. 2014

ASJC Scopus subject areas

Biophysik
Biochemie
Molekularbiologie
Zellbiologie

Fields of Expertise

Human- & Biotechnology

Treatment code (Nähere Zuordnung)

Basic - Fundamental (Grundlagenforschung)
Experimental

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10.1016/j.bbrc.2014.07.054Lizenz: CC BY-NC-ND 3.0

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Verknüpfung zur Publikation in Scopus

FWF - APMAP in adipogenesis - Die Rolle von APMAP in der Adipogenese und im Energiehaushal
Huber, K., Pessentheiner, A., Prokesch, A. & Bogner-Strauß, J. G.
1/03/12 → 31/12/15
Projekt: Forschungsprojekt

Dieses zitieren

Rossmann, C., Windpassinger, C., Brunner, D., Kovacevic, A., Schweighofer, N., Malli, R., Schuligoi, R., Prokesch, A., Kluve-Beckerman, B., Graier, W. F., Kratky, D., Sattler, W., & Malle, E. (2014). Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily. Biochemical and Biophysical Research Communications, 450(4), 1643-1649. https://doi.org/10.1016/j.bbrc.2014.07.054

Rossmann, C, Windpassinger, C, Brunner, D, Kovacevic, A, Schweighofer, N, Malli, R, Schuligoi, R, Prokesch, A, Kluve-Beckerman, B, Graier, WF , Kratky, D, Sattler, W & Malle, E 2014, 'Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily', Biochemical and Biophysical Research Communications, Jg. 450, Nr. 4, S. 1643-1649. https://doi.org/10.1016/j.bbrc.2014.07.054

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title = "Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily",

abstract = "The serum amyloid A (SAA) family of proteins is encoded by multiple genes, which display allelic variation and a high degree of homology in mammals. The SAA1/2 genes code for non-glycosylated acute-phase SAA1/2 proteins, that may increase up to 1000-fold during inflammation. The SAA4 gene, well characterized in humans (hSAA4) and mice (mSaa4) codes for a SAA4 protein that is glycosylated only in humans. We here report on a previously uncharacterized SAA4 gene (rSAA4) and its product in Rattus norvegicus, the only mammalian species known not to express acute-phase SAA. The exon/intron organization of rSAA4 is similar to that reported for hSAA4 and mSaa4. By performing 5′- and 3′RACE, we identified a 1830-bases containing rSAA4 mRNA (including a GA-dinucleotide tandem repeat). Highest rSAA4 mRNA expression was detected in rat liver. In McA-RH7777 rat hepatoma cells, rSAA4 transcription was significantly upregulated in response to LPS and IL-6 while IL-1α/β and TNFα were without effect. Luciferase assays with promoter-truncation constructs identified three proximal C/EBP-elements that mediate expression of rSAA4 in McA-RH7777 cells. In line with sequence prediction a 14-kDa non-glycosylated SAA4 protein is abundantly expressed in rat liver. Fluorescence microscopy revealed predominant localization of rSAA4-GFP-tagged fusion protein in the ER.",

keywords = "Inflammation, Luciferase assay, Promoter activity, Rat SAA",

author = "Christine Rossmann and Christian Windpassinger and Daniela Brunner and Alenka Kovacevic and Natascha Schweighofer and Roland Malli and Rufina Schuligoi and Andreas Prokesch and Barbara Kluve-Beckerman and Graier, {Wolfgang F.} and Dagmar Kratky and Wolfgang Sattler and Ernst Malle",

note = "Funding Information: Supported by the Austrian Science Fund (FWF-Austria) P19074 and SFB F3004 and F3007. ",

year = "2014",

month = aug,

day = "8",

doi = "10.1016/j.bbrc.2014.07.054",

language = "English",

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pages = "1643--1649",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Characterization of rat serum amyloid A4 (SAA4)

T2 - A novel member of the SAA superfamily

AU - Rossmann, Christine

AU - Windpassinger, Christian

AU - Brunner, Daniela

AU - Kovacevic, Alenka

AU - Schweighofer, Natascha

AU - Malli, Roland

AU - Schuligoi, Rufina

AU - Prokesch, Andreas

AU - Kluve-Beckerman, Barbara

AU - Graier, Wolfgang F.

AU - Kratky, Dagmar

AU - Sattler, Wolfgang

AU - Malle, Ernst

N1 - Funding Information: Supported by the Austrian Science Fund (FWF-Austria) P19074 and SFB F3004 and F3007.

PY - 2014/8/8

Y1 - 2014/8/8

N2 - The serum amyloid A (SAA) family of proteins is encoded by multiple genes, which display allelic variation and a high degree of homology in mammals. The SAA1/2 genes code for non-glycosylated acute-phase SAA1/2 proteins, that may increase up to 1000-fold during inflammation. The SAA4 gene, well characterized in humans (hSAA4) and mice (mSaa4) codes for a SAA4 protein that is glycosylated only in humans. We here report on a previously uncharacterized SAA4 gene (rSAA4) and its product in Rattus norvegicus, the only mammalian species known not to express acute-phase SAA. The exon/intron organization of rSAA4 is similar to that reported for hSAA4 and mSaa4. By performing 5′- and 3′RACE, we identified a 1830-bases containing rSAA4 mRNA (including a GA-dinucleotide tandem repeat). Highest rSAA4 mRNA expression was detected in rat liver. In McA-RH7777 rat hepatoma cells, rSAA4 transcription was significantly upregulated in response to LPS and IL-6 while IL-1α/β and TNFα were without effect. Luciferase assays with promoter-truncation constructs identified three proximal C/EBP-elements that mediate expression of rSAA4 in McA-RH7777 cells. In line with sequence prediction a 14-kDa non-glycosylated SAA4 protein is abundantly expressed in rat liver. Fluorescence microscopy revealed predominant localization of rSAA4-GFP-tagged fusion protein in the ER.

AB - The serum amyloid A (SAA) family of proteins is encoded by multiple genes, which display allelic variation and a high degree of homology in mammals. The SAA1/2 genes code for non-glycosylated acute-phase SAA1/2 proteins, that may increase up to 1000-fold during inflammation. The SAA4 gene, well characterized in humans (hSAA4) and mice (mSaa4) codes for a SAA4 protein that is glycosylated only in humans. We here report on a previously uncharacterized SAA4 gene (rSAA4) and its product in Rattus norvegicus, the only mammalian species known not to express acute-phase SAA. The exon/intron organization of rSAA4 is similar to that reported for hSAA4 and mSaa4. By performing 5′- and 3′RACE, we identified a 1830-bases containing rSAA4 mRNA (including a GA-dinucleotide tandem repeat). Highest rSAA4 mRNA expression was detected in rat liver. In McA-RH7777 rat hepatoma cells, rSAA4 transcription was significantly upregulated in response to LPS and IL-6 while IL-1α/β and TNFα were without effect. Luciferase assays with promoter-truncation constructs identified three proximal C/EBP-elements that mediate expression of rSAA4 in McA-RH7777 cells. In line with sequence prediction a 14-kDa non-glycosylated SAA4 protein is abundantly expressed in rat liver. Fluorescence microscopy revealed predominant localization of rSAA4-GFP-tagged fusion protein in the ER.

KW - Inflammation

KW - Luciferase assay

KW - Promoter activity

KW - Rat SAA

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U2 - 10.1016/j.bbrc.2014.07.054

DO - 10.1016/j.bbrc.2014.07.054

M3 - Article

SN - 1090-2104

VL - 450

SP - 1643

EP - 1649

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Characterization of rat serum amyloid A4 (SAA4): A novel member of the SAA superfamily

Abstract

ASJC Scopus subject areas

Fields of Expertise

Treatment code (Nähere Zuordnung)

Zugriff auf Dokument

Andere Dateien und Links

Fingerprint

Projekte

FWF - APMAP in adipogenesis - Die Rolle von APMAP in der Adipogenese und im Energiehaushal

Dieses zitieren