Correction: Regulation of Phosphorylation of a Specific Protein in Toad-Bladder Membrane by Antidiuretic Hormone and Cyclic AMP, and Its Possible Relationship to Membrane Permeability Changes

1973 ◽  
Vol 70 (6) ◽  
pp. 1903-1903
2002 ◽  
Vol 25 (11) ◽  
pp. 1539-1549 ◽  
Author(s):  
L. Van Der Weerd ◽  
M. M. A. E. Claessens ◽  
C. Efdé ◽  
H. Van As

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827
Author(s):  
M Chedid ◽  
S B Mizel

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.


1990 ◽  
Vol 10 (12) ◽  
pp. 6264-6272
Author(s):  
E A Park ◽  
W J Roesler ◽  
J Liu ◽  
D J Klemm ◽  
A L Gurney ◽  
...  

Previous studies have identified a region in the promoter of the gene for phosphoenolpyruvate carboxykinase (GTP) (PEPCK) (positions -460 to +73) containing the regulatory elements which respond to cyclic AMP, glucocorticoids, and insulin and confer the tissue- and developmental stage-specific properties to the gene. We report that CCAAT/enhancer-binding protein (C/EBP) binds to the cyclic AMP-responsive element CRE-1 as well as to two regions which have been previously shown to bind proteins enriched in liver nuclei. The DNase I footprint pattern provided by the recombinant C/EBP was identical to that produced by a 43-kDa protein purified from rat liver nuclear extracts, using a CRE oligonucleotide affinity column, which was originally thought to be the CRE-binding protein CREB. Transient contransfection experiments using a C/EBP expression vector demonstrated that C/EBP could trans activate the PEPCK promoter. The trans activation occurred through both the upstream, liver-specific protein-binding domains and the CRE. The CRE-binding protein bound only to CRE-1 and not to the upstream C/EBP-binding sites. The results of this study, along with physiological properties of C/EBP, indicate an important role for this transcription factor in providing the PEPCK gene with several of its regulatory characteristics.


Nature ◽  
1977 ◽  
Vol 270 (5636) ◽  
pp. 391-396 ◽  
Author(s):  
Charles F. Stevens

1978 ◽  
Vol 540 (1) ◽  
pp. 173-182
Author(s):  
E.B.Margareta Ekblad ◽  
Vojtech Ličko
Keyword(s):  

Blood ◽  
1965 ◽  
Vol 26 (3) ◽  
pp. 367-382 ◽  
Author(s):  
JAMES H. JANDL

Abstract The normal survival of red cells requires maintained regulation of cell size and shape. This regulation is to a large extent dependent upon membrane permeability and the active transport of cations. Agents such as C' that affect permeability markedly by creating large holes in the membrane lead to rapid cell death. Most hemolytic disorders thus far studied involve lesser increases in membrane permeability and hemolysis occurs more gradually by the sequence of colloid osmotic swelling, loss of cell surface, and spherocytosis. With very mild permeability changes, as in hereditary spherocytosis, the cell may compensate for an increased leak-rate for cations by increased active transport. This compensation requires increased glycolysis and optimal metabolic conditions, however, and the cell rapidly decompensates during glucose deprivation or metabolic stress. The interaction between reticuloendothelial tissues and red cells provides such a stress for leaky cells and hastens their destruction.


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