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Degradation of extracellular nucleotides and their analogs in HeLa and HUVEC cell cultures.

100%

Gendaszewska-Darmach E. , Maszewska M. , Zakłos M. , Koziołkiewicz M.

Acta Biochimica Polonica

2003

tom 50

nr 4

973-984

The use of nucleotides and their analogs in the pharmacological studies of nucleotide receptors (P2 class) should be preceded by detailed studies on their degradation connected with ecto-enzymes of a given cell type. In the present studies we have analyzed stability of some phosphorothioate and phosphonate analogs of ATP and ADP in the HeLa epitheloid carcinoma and endothelial HUVEC cells cultures. Our studies have revealed that ecto-nucleotide pyrophosphatase (E-NPP) is one of the main enzymes involved in the extracellular degradation of ATP and other nucleotides in the HeLa cells. On the other hand, the ecto-ATPDase is responsible for the hydrolysis of extracellular nucleotides in human endothelial cell cultures, while the E-NPP-like enzymes of the HUVEC cells are not essential to this degradation. The concerted action of the aforementioned ecto-enzymes and nucleotide pyrophosphatase, 5'-nucleotidase and adenosine deaminase present in fetal bovine serum (FBS) supplied to the culture medium, results in partial or complete degradation of the phosphorothioate (ATPγS) and phosphonate analogs of adenosine nucleotides (α,β-methylene-ATP and β,γ-methylene-ATP) in the cell cultures. Only ADPβS appears to be resistant to these enzymes. The influence of some nucleotides and their analogs on the proliferation of the HeLa cells in presence or absence of FBS is also discussed.

Degradation of extracellular nucleotides and their analogs in HeLa and HUVEC cell cultures

75%

Gendaszewska-Darmach E. , Maszewska M. , Zaklos M. , Koziolkiewicz M.

Acta Biochimica Polonica

2003

tom 50

nr 4

The use of nucleotides and their analogs in the pharmacological studies of nucleotide receptors (P2 class) should be preceded by detailed studies on their degradation connected with ecto-enzymes of a given cell type. In the present studies we have analyzed stability of some phosphorothioate and phosphonate analogs of ATP and ADP in the HeLa epitheloid carcinoma and endothelial HUVEC cells cultures. Our studies have revealed that ecto-nucleotide pyrophosphatase (E-NPP) is one of the main enzymes involved in the extracellular degradation of ATP and other nucleotides in the HeLa cells. On the other hand, the ecto-ATPDase is responsible for the hydrolysis of extracellular nucleotides in human endothelial cell cultures, while the E-NPP-like enzymes of the HUVEC cells are not essential to this degradation. The concerted action of the aforementioned ecto-enzymes and nucleotide pyrophosphatase, 5 -nucleo- tidase and adenosine deaminase present in fetal bovine serum (FBS) supplied to the culture medium, results in partial or complete degradation of the phosphorothioate (ATPγS) and phosphonate analogs of adenosine nucleotides (α,β-methylene-ATP and β,γ-methylene-ATP) in the cell cultures. Only ADPβS appears to be resistant to these enzymes. The influence of some nucleotides and their analogs on the proliferation of the HeLa cells in presence or absence of FBS is also discussed.

Alpha-naphthyl and AS-BI-naphthyl esters of nucleotides, specific substrates for cytochemical localization of mammalian pancreatic RNase and 5'-exonuclease and of plant nucleotide pyrophosphatase and cyclic nucleotide phosphodiesterase

63%

Sierakowska H. , Zan-Kowalczewska M. , Bartkiewicz M.

Folia Histochemica et Cytobiologica

1984

tom 22

nr 3-4