scholarly journals Distinct Functions of CCAAT Enhancer-binding Protein Isoforms in the Regulation of Manganese Superoxide Dismutase during Interleukin-1β Stimulation

2008 ◽  
Vol 283 (38) ◽  
pp. 25774-25785 ◽  
Author(s):  
Xiaolei Qiu ◽  
Kimberly J. Aiken ◽  
Ann L. Chokas ◽  
Dawn E. Beachy ◽  
Harry S. Nick
2005 ◽  
Vol 46 (11) ◽  
pp. 2497-2505 ◽  
Author(s):  
Natalia V. Giltiay ◽  
Alexander A. Karakashian ◽  
Alexander P. Alimov ◽  
Sandy Ligthle ◽  
Mariana N. Nikolova-Karakashian

Cytokine ◽  
2000 ◽  
Vol 12 (9) ◽  
pp. 1430-1436 ◽  
Author(s):  
Tengku S Tengku-Muhammad ◽  
Timothy R Hughes ◽  
Harri Ranki ◽  
Anthony Cryer ◽  
Dipak P Ramji

1998 ◽  
Vol 334 (1) ◽  
pp. 205-210 ◽  
Author(s):  
Georgios SABATAKOS ◽  
Gareth E. DAVIES ◽  
Maria GROSSE ◽  
Anthony CRYER ◽  
Dipak P. RAMJI

Transcription factors belonging to the CCAAT-enhancer binding protein (C/EBP) family have been implicated in the activation of gene expression in the mammary gland during lactation. We have therefore investigated the detailed expression profile of the C/EBP family during lactation and involution of the mouse mammary gland. The expression of C/EBPβ and C/EBPδ mRNA was low during lactation, increased dramatically at the beginning of involution and remained constant thereafter. In contrast, C/EBPα mRNA expression was relatively high during the early stages of lactation, declined to low levels during the late stages of lactation and at the start of involution, and increased again during involution. Electrophoretic mobility-shift assays showed a close correlation between the expression of the C/EBP genes and the functional C/EBP DNA-binding activity and, additionally, demonstrated the participation of heterodimers, formed from among the three proteins, in DNA–protein interactions. The DNA-binding activity of the activator protein 1 (AP1) family of transcription factors was also induced during involution. These results therefore point to potentially important regulatory roles for both the C/EBP and the AP1 family during lactation and involution of the mammary gland.


1995 ◽  
Vol 204 (1) ◽  
pp. 66-76 ◽  
Author(s):  
Sylvie Blais ◽  
François Boudreau ◽  
Jean-françois Beaulieu ◽  
Claude Asselin

2001 ◽  
Vol 276 (47) ◽  
pp. 44331-44337 ◽  
Author(s):  
Ionela Gheorghiu ◽  
Claude Deschênes ◽  
Mylène Blais ◽  
François Boudreau ◽  
Nathalie Rivard ◽  
...  

1997 ◽  
Vol 272 (4) ◽  
pp. L714-L719
Author(s):  
D. J. Chung ◽  
L. B. Clerch

A redox-sensitive protein in rat lung binds to the 3'-untranslated region (3'-UTR) of manganese superoxide dismutase (Mn-SOD) mRNA; the activity of this Mn-SOD RNA-binding protein (Mn-SOD-BP) is greater in 12,000-g supernatant fractions (S12) from neonates than in S12 from adults (H. Fazzone, A. Wangner, and L. B. Clerch. J. Clin. Invest. 92: 1278-1281, 1993). To determine the mechanism underlying this developmental difference, lung subcellular fractions were tested for their effect on Mn-SOD-BP activity. Protein in the 130,000-g supernatant (S130) of lung extracts bound the 3'-UTR. However, the developmental difference in binding was not present in S130. The 130,000-g pellet (P130) did not bind the 3'-UTR; rather, it contained an inhibitor of Mn-SOD-BP activity. Addition of P130 to S130 decreased RNA binding in a dose-dependent manner. Furthermore, adult P130 was a more potent inhibitor of RNA-binding activity than neonatal P130. These data indicate that the developmental difference in Mn-SOD-BP activity is due, in part, to an inhibitor in P130. Biochemical characterization revealed that the inhibitor is an RNA that may participate in the posttranscriptional control of Mn-SOD gene expression.


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