Mediation of sonic hedgehog-induced expression of COUP-TFII by a protein phosphatase

Science

Volumn 278, Issue 5345, 1997, Pages 1947-1950

  Krishnan, Venkatesh ^a   Pereira, Fred A ^a   Qiu, Yuhong ^a   Chen, Chien Huan ^b   Beachy, Philip A ^b   Tsai, Sophia Y ^a   Tsai, Ming Jer ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE; SONIC HEDGEHOG PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; GENE EXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN BINDING; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION;

ANIMALS; CELL LINE; COUP TRANSCRIPTION FACTOR II; COUP TRANSCRIPTION FACTORS; DNA; DNA-BINDING PROTEINS; ENZYME INHIBITORS; GENE EXPRESSION REGULATION; HEDGEHOG PROTEINS; MICE; OKADAIC ACID; OXAZOLES; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROMOTER REGIONS (GENETICS); PROTEINS; RECEPTORS, STEROID; SIGNAL TRANSDUCTION; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

ANIMALIA; ERINACEIDAE; GALLUS GALLUS;

EID: 0031436999     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5345.1947     Document Type: Article

References (31)

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8. Briefly 20 μg of RNA was hybridized to a 450-nucleotide (Fig. 1A) or 120-nucleotide (Fig. 3B) riboprobe, which corresponds to the 5′ untranslated region of the COUP-TFII gene along with a 670-nucleotide (Fig. 1A) or 102-nucleotide (Fig. 3B) riboprobe in the murine cyclophilin A coding region. Also, a 255-base pair (bp) region of the pBLCAT2 plasmid (Bgl II-Eco RI fragment) or a 123-bp region of the LUC coding (Hinc II-Eco 1091 fragment) region was used to generate an antisense riboprobe and was hybridized with 60 μg of total RNA (Fig. 2) obtained from transfected P19 cells. The RPA II kit from Ambion was used to perform the ribonuclease (RNase) protection assay. The products were subjected to RNase digestion and analyzed on a 6% urea-polyacrylamide gel.
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31. Purified Shh-N was provided by J. A Porter and K. Young, purified protein phosphatases PP1 and PP2A were provided by S. Shenolikar (Duke University), PPIV protein and expression plasmid were provided by T-H. Tan (Baylor College of Medicine). CMV-PPV plasmid was provided by M. Chinkers (Oregon University, Health Science Center). PP1 and PP2A expression plasmids were kindly provided by T. Deng (University of Florida). Human Gli and GliRE-CAT reporters were provided by C-C. Hui (University of Toronto, Canada). The authors also wish to thank N. Fuse for communication of unpublished results. This work is supported by an NIH grant.