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Details for article 1 of 7 found articles
| Title: |
Ecto-diadenosine 5',5'''-P^{1},P^{4}-tetraphosphate (Ap_{4}A)-hydrolase is expressed as an ectoenzyme in a variety of mammalian and human cells and adds ne |
| Author: |
Annette von Drygalski Adaling Ogilvie |
| Appeared in: |
BioFactors |
| Paging: | Volume 11 (2001) nr. 3 pages 179-187 |
| Year: |
2001-04-01 |
| Contents: |
Ap_{4}A and other dinucleotides participate in the regulation of hemostasis and blood pressure control. With the exception of two previously reported surface anchored ectoAp_{4}A-hydrolases on bovine aortic endothelial and chromaffine cells, all Ap_{4}A-hydrolases reported are intracellular or freely soluble. We demonstrated that ectoAp_{4}A-hydrolases are present on a broad variety of cell types of different species: rat mesangial, bovine corneal epithelial, human Hep-G2 and peridontal cells. Ectoenzyme properties were evaluated on rat mesangium cells. Chromatography of purified plasma membranes on Sephacel 300 resulted in enrichment of ectoAp_{4}A-hydrolase and in separation from ectoATPase. In contrast to ATPase, Ap_{4}A-hydrolase was stable at room temperature. EctoAp_{4}A-hydrolase also recognized ATP as substrate, and therefore is not highly specific. The molecular weight was 180 kD. Unlike ectoAMPase ectoAp_{4}A-hydrolase was not attached via a glycosyl-phosphatidylinositol (GPI)-moiety. Concentrations of PI-PLC 10100-fold higher than effective for ectoAMPase cleavage (10100 mU/ml) plus extensively extended incubation times up to eight hours did not result in cleavage of ectoAp_{4}A-hydrolase. The enzyme ectoAp_{4}A-hydrolase might presage a direction for pharmaceutical manipulation in the control of blood pressure and hemostasis. |
| Publisher: |
IOS Press |
| Source file: |
Elektronische Wetenschappelijke Tijdschriften |
Details for article 1 of 7 found articles
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