Cyclic adenosine 3':5'-monophosphate-binding protein, a biochemical marker of neuroblastoma differentiation.

Mouse neuroblastoma tumors show reduced amounts of cyclic adenosine 3':5'-monophosphate (cAMP) binding protein. However, the levels of cAMP-binding protein were increased by 2-fold when the tumor cells were established in tissue culture, and these levels were comparable to that found in mouse brain. This binding protein is a free cAMP-binding protein that is not associated with protein kinase.

Phosphorylation of endogenous proteins by adenosine 3':5'-monophosphate-dependent protein kinase in mouse neuroblastoma cells.

Increased intracellular adenosine 3':5'-monophosphate (cAMP) levels and activation of cAMP-dependent protein kinases (ATP:protein phosphotransferase, EC 2.7.1.

Dibutyryl cAMP-induced protein changes in differentiating mouse neuroblastoma cells.

Proteins from mouse neuroblastoma cells treated with dibutyryl adenosine-3',5'-monophosphate (B2cAMP) were analyzed by high resolution, two-dimensional gel electrophoresis. Quantitative changes in proteins and charge modifications of proteins apparently induced B2cAMP were detected by isoelectric focusing. Some proteins appeared to be modified and one protein was increased 7- to 8-fold in cells treated with B2cAMP.