Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A chicken homolog of mammalian interleukin-1 beta: cDNA cloning and purification of active recombinant protein
Autore:
Weining, KC; Sick, C; Kaspers, B; Staeheli, P;
Indirizzi:
Univiburg,urg, Dept Virol, Abt Virol, Inst Med Mikrobiol & Hyg, D-79008 Fre Univ Freiburg Freiburg Germany D-79008 Med Mikrobiol & Hyg, D-79008 Fre Univ Munich, Inst Tierphysiol, Munich, Germany Univ Munich Munich Germany iv Munich, Inst Tierphysiol, Munich, Germany
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 3, volume: 258, anno: 1998,
pagine: 994 - 1000
SICI:
0014-2956(199812)258:3<994:ACHOMI>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR ANTAGONIST; PLATELET PROTEIN; BINDING-PROTEIN; IL-1 RECEPTOR; EXPRESSION; SEQUENCE; CELLS; GENE; IDENTIFICATION; PRECURSOR;
Keywords:
chicken; lipopolysaccharide inducibility; interleukin-1 beta; CXC chemokine; cDNA expression cloning;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Staeheli, P Univdereiburg, Dept Virol, Abt Virol, Inst Med Mikrobiol & Hyg, Hermann Her Univ Freiburg Hermann Herder Str 11 Freiburg Germany D-79008
Citazione:
K.C. Weining et al., "A chicken homolog of mammalian interleukin-1 beta: cDNA cloning and purification of active recombinant protein", EUR J BIOCH, 258(3), 1998, pp. 994-1000

Abstract

Upon induction with lipopolysaccharide (LPS) the chicken macrophage cell line HD-11 secretes an activity that stimulates the synthesis of a CXC chemokine in the chicken fibroblast cell line CEC-32. We used a cDNA expression cloning strategy in COS cells to characterize this activity. The isolated cDNA clone codes for a polypeptide of 267 amino acids which lacks a hydrophobic N-terminal domain that could serve as secretory signal. Sequence homology and structural features indicate that this protein is the chicken homolog of mammalian interleukin-1 beta (ChIL-1 beta). Northern blot analysis showed that ChIL-1 beta RNA is quickly induced in blood monocyte-derived macrophages reaching maximal levels within one hour after onset of LPS treatment. To test for biological activity of putative mature ChIL-1 beta, a cDNA fragment comprising amino acids 106 to 267 of the open reading frame was expressed in Escherichia coli so that the resulting polypeptide carried a histidine tag at its N-terminus for easy purification by nickel chelate affinitychromatography. Purified His-ChIL-1 beta potently induced CXC chemokine RNA synthesis in CEC-32 cells. When injected intravenously into adult chickens, it quickly induced a transient increase in serum corticosterone levels.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:31:36