Feedback inhibition of macrophage tumor necrosis factor-α production by tristetraprolin

Science

Volumn 281, Issue 5379, 1998, Pages 1001-1005

  Carballo, Ester ^a   Lai, Wi S ^a   Blackshear, Perry J ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; TUMOR NECROSIS FACTOR ALPHA; ZINC FINGER PROTEIN;

ANIMAL CELL; ARTICLE; IMMUNE RESPONSE; INFLAMMATION; MACROPHAGE; MOUSE; NEGATIVE FEEDBACK; NONHUMAN; PATHOGENESIS; PATHOPHYSIOLOGY; PRIORITY JOURNAL;

3T3 CELLS; ANIMALS; BASE SEQUENCE; BIOLOGICAL TRANSPORT; CELL LINE; CELL NUCLEUS; CHICK EMBRYO; CYTOSOL; DNA-BINDING PROTEINS; FEEDBACK; GENE EXPRESSION REGULATION; HUMANS; IMMEDIATE-EARLY PROTEINS; LIPOPOLYSACCHARIDES; MACROPHAGES; MICE; MICE, KNOCKOUT; PROTEINS; RNA PROBES; RNA, MESSENGER; TRANSFECTION; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR-ALPHA; ZINC FINGERS;

ANIMALIA;

EID: 0032516626     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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43. 2, 0.5 mM PMSF, and 5% glycerol], centrifuged at 1000g for 5 min at 4°C, and then resuspended and sonicated in the same volume of lysis buffer used initially to lyse the cells. The cytosolic fraction (supernatant) was clarified by centrifugation at 45,000g for 30 min at 4°C, using a tabletop ultracentrifuge (Beckman TL-100, rotor TLA.45). This method results in separation of cytosol and nuclear fractions, as assessed by protein immunoblotting with an antibody to SP1 as described (18). Cytosolic extracts matched by trichloroacetic acid - precipitable radioactivity and equivalent volumes of nuclear extracts were incubated with preimmune rabbit serum (1:100 dilution, 1 hour at 4°C) and protein A-Sepharose (1 hour at 4°C), and then incubated overnight at 4°C in the presence of either preimmune serum (1:100) or a 1:100 dilution of a polyclonal rabbit antibody to mouse TTP (18, 19). Immune complexes were recovered by centrifugation after the addition of protein A-Sepharose, washed three times with wash buffer [50 mM tris-HCl (pH 8.3), 150 mM NaCl, 1 mM EDTA, and 0.5% NP-40], resuspended in 100 μl of SDS sample buffer [P. J. Blackshear, Methods Enzymol. 104, 237 (1984)], and subjected to SDS-polyacrylamide gel electrophoresis (PAGE) (9% gel). For autoradiography, gels were fixed and treated with Autofluor (National Diagnostics, Atlanta).
44. We thank A.-B. Shyu for the TNF-α, GM-CSF, and IL-3 β-globin ARE constructs, B. Beutler for the Pro-CAT construct, M. Gilman and D. Stumpo for the fos-CAT construct, D. Germolec and A. Jetten for helpful comments on the manuscript, and E. Kennington for technical assistance.