6 results on '"Schrier, SM"'
Search Results
2. Transport of fragile X mental retardation protein via granules in neurites PC12 cell
- Author
-
Diego Otero, Y, Severijnen, Lies-anne, van Cappellen, Gert, Schrier, SM, Oostra, Ben, Willemsen, Rob, Diego Otero, Y, Severijnen, Lies-anne, van Cappellen, Gert, Schrier, SM, Oostra, Ben, and Willemsen, Rob
- Published
- 2002
3. Apoptosis induced by extracellular ATP in the mouse neuroblastoma cell line N1E-115: studies on involvement of P2 receptors and adenosine.
- Author
-
Schrier SM, Florea BI, Mulder GJ, Nagelkerke JF, and IJzerman AP
- Subjects
- Adenosine Diphosphate pharmacology, Adenosine Kinase antagonists & inhibitors, Adenosine Monophosphate pharmacology, Adenosine Triphosphate metabolism, Animals, Mice, Neuroblastoma pathology, Receptors, Purinergic P2X7, Tumor Cells, Cultured, Adenosine physiology, Adenosine Triphosphate pharmacology, Apoptosis, Receptors, Purinergic P2 physiology
- Abstract
Adenosine triphosphate (ATP) can be released in large amounts from (damaged) cells, leading to locally high concentrations. In this study, we investigated the effect of such high concentrations of ATP on neuroblastoma cells. ATP (>or=30 microM) induced apoptosis in the mouse neuroblastoma cell line N1E-115. Activation of the ATP receptor P2X(7) is one of the routes via which ATP has been shown to induce apoptosis. Although the P2X(7) receptor was present in N1E-115 cells, both at the protein and mRNA level, studies with the P2X(7) receptor agonist benzoyl-benzoyl ATP showed that this receptor was not involved in ATP-induced apoptosis. It has been shown previously that adenosine induces apoptosis in N1E-115 cells after transport inside the cell. In this study, both dipyridamole, a nucleoside transport protein blocker, and uridine, a substrate for this transporter, were able to block ATP-induced apoptosis. This indicated that ATP had to be broken down to adenosine to induce apoptosis. The ecto-nucleotidase inhibitors 6-N,N-diethyl-beta-dibromomethylene-D-adenosine-5'-triphosphate (ARL67156) and alpha,beta-methylene adenosine 5'-diphosphate (AOPCP) commonly used to slow breakdown of ATP did not inhibit ATP breakdown appreciably, while the ATP antagonist PPADS inhibited the breakdown of AMP to adenosine; PPADS was also the only compound capable of inhibiting ATP-induced apoptosis. We conclude that the main route of ATP-induced apoptosis in N1E-115 cells was via breakdown to adenosine.
- Published
- 2002
- Full Text
- View/download PDF
4. Time-dependent changes in factors involved in the apoptotic process in human ovarian cancer cells as a response to cisplatin.
- Author
-
Kolfschoten GM, Hulscher TM, Schrier SM, van Houten VM, Pinedo HM, and Boven E
- Subjects
- Apoptosis physiology, Caspase 3, Caspases biosynthesis, Caspases physiology, Cell Cycle drug effects, Cell Cycle physiology, Cyclin-Dependent Kinase Inhibitor p21, Cyclins biosynthesis, Cyclins physiology, Enzyme Activation, Female, Humans, Inhibitory Concentration 50, Ovarian Neoplasms drug therapy, Ovarian Neoplasms metabolism, Proto-Oncogene Proteins biosynthesis, Proto-Oncogene Proteins physiology, Proto-Oncogene Proteins c-bcl-2 biosynthesis, Proto-Oncogene Proteins c-bcl-2 physiology, Tumor Cells, Cultured, Tumor Suppressor Protein p53 biosynthesis, Tumor Suppressor Protein p53 physiology, bcl-2-Associated X Protein, Antineoplastic Agents pharmacology, Apoptosis drug effects, Cisplatin pharmacology, Ovarian Neoplasms pathology
- Abstract
Objectives: Apoptosis is believed to be a major mechanism of cisplatin-induced cell death. We investigated the kinetics of apoptosis in four human ovarian cancer cell lines treated with cisplatin to obtain insight into the role and the behavior of a variety of factors involved in this process., Methods: The cell lines A2780, H134, and IGROV-1 (all wild-type p53) and OVCAR-3 (mutant p53) were exposed to cisplatin for 1 h and the antiproliferative effects were measured after 96 h. At various time points up to 96 h after the 1-h exposure to the individual 90% growth-inhibiting cisplatin concentrations, FACS analysis and May-Grünwald Giemsa staining were carried out to determine the extent of apoptosis. At the same time points protein expression levels of p53, p21/WAF1, Bax, and Bcl-2 and the activity of caspase-3 were measured. FACS analysis was also carried out to determine changes in cell cycle distribution as a response to cisplatin., Results: The four cell lines differed in sensitivity to cisplatin. A2780 was the most sensitive and IGROV-1 was the least sensitive. In contrast, IGROV-1 cells showed the highest percentage of apoptosis (30-40%), while A2780 had the lowest percentage (6-14%) (r = 0.99). The occurrence of apoptosis was not dependent on functional p53. Of interest, caspase-3 activity was in line with the percentage of apoptosis and preceded DNA fragmentation and the visualization of condensed nuclei. Wild-type p53 cells accumulated in the S phase, while OVCAR-3 arrested in the G2/M phase. The protein expression levels of p53, p21/WAF1, Bax, and Bcl-2 varied in time, but were not related to the apoptotic behavior of the cells. Upregulation of p53 was already evident before activation of caspase-3., Conclusions: Time-dependent changes in the various factors involved in the apoptotic process induced by equitoxic doses of cisplatin vary strongly among the cell lines. Caspase-3 activation plays an important role in cisplatin-induced apoptosis and this precedes morphological changes. The ability of cells to enter apoptosis, however, does not seem to predict sensitivity to cisplatin.
- Published
- 2002
- Full Text
- View/download PDF
5. Evidence of P-glycoprotein mediated apical to basolateral transport of flunisolide in human broncho-tracheal epithelial cells (Calu-3).
- Author
-
Florea BI, van der Sandt IC, Schrier SM, Kooiman K, Deryckere K, de Boer AG, Junginger HE, and Borchard G
- Subjects
- ATP Binding Cassette Transporter, Subfamily B, Member 1 antagonists & inhibitors, ATP Binding Cassette Transporter, Subfamily B, Member 1 metabolism, Animals, Biological Transport drug effects, Bronchi cytology, Bronchi metabolism, Cell Line, Cell Polarity, Cell Survival, Cyclosporins pharmacology, Deoxyglucose pharmacology, Dibenzocycloheptenes pharmacology, Epithelial Cells cytology, Humans, Immunoblotting, Mass Spectrometry, Microscopy, Confocal, Quinolines pharmacology, Sodium Azide pharmacology, Temperature, Time Factors, Trachea cytology, Trachea metabolism, Verapamil pharmacology, ATP Binding Cassette Transporter, Subfamily B, Member 1 physiology, Epithelial Cells metabolism, Fluocinolone Acetonide analogs & derivatives, Fluocinolone Acetonide metabolism
- Abstract
1. Transepithelial transport of flunisolide was studied in reconstituted cell monolayers of Calu-3, LLC-PK1 and the MDR1-P-glycoprotein transfected LLC-MDR1 cells. 2. Flunisolide transport was polarized in the apical (ap) to basolateral (bl) direction in Calu-3 cells and was demonstrated to be ATP-dependent. In LLC-MDR1 cells, flunisolide was transported in the bl to ap direction and showed no polarization in LLC-PK1 cells. 3. Non-specific inhibition of cellular metabolism at low temperature (4 degrees C) or by 2-deoxy-D-glucose (2-d-glu) and sodium azide (NaN(3)) abolished the polarized transport. Polarized flunisolide transport was also inhibited by the specific Pgp inhibitors verapamil, SDZ PSC 833 and LY335979. 4. Under all experimental conditions and in the presence of all used inhibitors, no decrease in the TransEpithelial Electrical Resistance (TEER) values was detected. From all inhibitors used, only the general metabolism inhibitors 2-deoxy-D-glucose and NaN(3), decreased the survival of Calu-3 cells. 5. Western blotting analysis and confocal laser scanning microscopy demonstrated the presence of MDR1-Pgp at mainly the basolateral side of the plasma membrane in Calu-3 cells and at the apical side in LLC-MDR1 cells. Mass spectroscopy studies demonstrated that flunisolide is transported unmetabolized across Calu-3 cells. 6. In conclusion, these results show that the active ap to bl transport of flunisolide across Calu-3 cells is facilitated by MDR1-Pgp located in the basolateral plasma membrane.
- Published
- 2001
- Full Text
- View/download PDF
6. Extracellular adenosine-induced apoptosis in mouse neuroblastoma cells: studies on involvement of adenosine receptors and adenosine uptake.
- Author
-
Schrier SM, van Tilburg EW, van der Meulen H, Ijzerman AP, Mulder GJ, and Nagelkerke JF
- Subjects
- Adenosine metabolism, Adenosine-5'-(N-ethylcarboxamide) pharmacology, Animals, Biological Transport physiology, Carrier Proteins antagonists & inhibitors, Carrier Proteins isolation & purification, Carrier Proteins physiology, Deoxyadenosines pharmacology, Membrane Proteins antagonists & inhibitors, Membrane Proteins isolation & purification, Membrane Proteins physiology, Mice, Neuroblastoma metabolism, Nucleoside Transport Proteins, Purinergic P1 Receptor Agonists, Receptors, Purinergic P1 isolation & purification, Tumor Cells, Cultured, Adenosine pharmacology, Apoptosis, Neuroblastoma pathology, Receptors, Purinergic P1 physiology
- Abstract
The induction of apoptosis by adenosine was studied in the mouse neuroblastoma cell line N1E-115. Apoptosis was characterized by fluorescence and electron microscopy, fluorescence-activated cell sorter (FACS) analysis, and caspase activity assays. A sixteen-hour exposure to 100 microM of adenosine led to chromatin condensation and caspase activation. However, selective agonists for all four adenosine receptors were ineffective. Caspase activation could be blocked partially by an inhibitor of the nucleoside transporter, dipyridamole, and completely by uridine, a competing substrate for adenosine transport. 2'-Deoxycoformycin, an inhibitor of adenosine deaminase, enhanced caspase activation by adenosine but had no effect by itself. Caspase activation could be blocked by 5'-amino-5'-deoxyadenosine, which inhibits the phosphorylation of adenosine by adenosine kinase. These results indicate that adenosine receptors are not involved in adenosine-induced apoptosis in N1E-115 cells, but that uptake of adenosine and its subsequent phosphorylation is required.
- Published
- 2001
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.