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25 results on '"Backstrom, G."'

2. On the Value of LET as a Radiation Quality Descriptor for RBE

Author

Pater, P., Backstrom, G., Enger, S., Villegas, Fernanda Navarro, Ahnesjö, Anders, Seuntjens, J., El Naqa, I., Pater, P., Backstrom, G., Enger, S., Villegas, Fernanda Navarro, Ahnesjö, Anders, Seuntjens, J., and El Naqa, I.

Published
2015

5. Endothelial PDGF-B retention is required for proper investment ofpericytes in the microvessel wall.

Author

Lindblom, P, Gerhardt, H, Liebner, S, Abramsson, A, Enge, M, Hellstrom, M, Backstrom, G, Fredriksson, S, Landegren, U, Nystrom, HC, Bergstrom, G, Dejana, E, Ostman, A, Lindahl, P, Betsholtz, C, Lindblom, P, Gerhardt, H, Liebner, S, Abramsson, A, Enge, M, Hellstrom, M, Backstrom, G, Fredriksson, S, Landegren, U, Nystrom, HC, Bergstrom, G, Dejana, E, Ostman, A, Lindahl, P, and Betsholtz, C

Published
2003

24. Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall.

Author

Lindblom P, Gerhardt H, Liebner S, Abramsson A, Enge M, Hellstrom M, Backstrom G, Fredriksson S, Landegren U, Nystrom HC, Bergstrom G, Dejana E, Ostman A, Lindahl P, and Betsholtz C

Subjects
Alleles, Amino Acid Motifs, Amino Acid Sequence, Animals, Cell Movement, Endothelial Growth Factors metabolism, Glomerulosclerosis, Focal Segmental genetics, Intercellular Signaling Peptides and Proteins metabolism, Kidney physiology, Lymphokines metabolism, Mice, Microscopy, Fluorescence, Models, Genetic, Molecular Sequence Data, Phenotype, Platelet-Derived Growth Factor metabolism, Protein Structure, Tertiary, Proteinuria genetics, Retina metabolism, Retina physiology, Retinal Degeneration genetics, Vascular Endothelial Growth Factor A, Vascular Endothelial Growth Factors, Endothelium, Vascular metabolism, Microcirculation metabolism, Mutation, Pericytes metabolism, Proto-Oncogene Proteins c-sis genetics, Proto-Oncogene Proteins c-sis metabolism
Abstract

Several platelet-derived growth factor (PDGF) and vascular endothelial growth factor (VEGF) family members display C-terminal protein motifs that confer retention of the secreted factors within the pericellular space. To address the role of PDGF-B retention in vivo, we deleted the retention motif by gene targeting in mice. This resulted in defective investment of pericytes in the microvessel wall and delayed formation of the renal glomerulus mesangium. Long-term effects of lack of PDGF-B retention included severe retinal deterioration, glomerulosclerosis, and proteinuria. We conclude that retention of PDGF-B in microvessels is essential for proper recruitment and organization of pericytes and for renal and retinal function in adult mice.

Published
2003
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25. P-glycoprotein efflux pump expression and activity in Calu-3 cells.

Author

Hamilton KO, Backstrom G, Yazdanian MA, and Audus KL

Subjects
ATP Binding Cassette Transporter, Subfamily B, Member 1 antagonists & inhibitors, ATP-Binding Cassette Transporters antagonists & inhibitors, Antineoplastic Agents, Phytogenic pharmacology, Caco-2 Cells drug effects, Caco-2 Cells metabolism, Cell Line drug effects, Cyclosporine pharmacology, Enzyme Inhibitors pharmacology, Humans, Multidrug Resistance-Associated Proteins, Paclitaxel pharmacology, Vinblastine pharmacology, ATP Binding Cassette Transporter, Subfamily B, Member 1 metabolism, ATP-Binding Cassette Transporters metabolism, Cell Line metabolism, Fluorescent Dyes pharmacokinetics, Rhodamine 123 pharmacokinetics
Abstract

The purpose of this work was to determine if the sub-bronchial epithelial cell model, Calu-3, expresses the functionally active P-glycoprotein (Pgp) efflux pump. Calu-3 cells express lower levels of Pgp than both Caco-2 and A549 cells as determined by Western Blot analysis. In Calu-3 cells, accumulation of the Pgp substrates rhodamine 123 (Rh123) and calcein acetoxymethyl ester (calcein-AM) was increased in the presence of the specific Pgp inhibitors cyclosporin A (CsA), vinblastine, and taxol. Significant inhibition of Pgp activity was not observed until after 2 h in both cell lines. The organic anion/multidrug resistance associated protein-1 (MRP1) inhibitors, probenecid and indomethacin, did not affect Rh123 accumulation, whereas an increase in calcein accumulation was observed by both agents. The metabolic inhibitor sodium azide decreased the efflux of Rh123 out of Calu-3 cells to the same degree as CsA, supporting inhibition of an active, efflux pathway. The basolateral-to-apical transport of Rh123 was significantly higher than that in the reverse direction, indicating a secretory pathway of efflux that was inhibited 25-fold by CsA. Basolateral-to-apical transport of Rh123 was inhibited slightly with both MRP1 inhibitors; however, no significant effect of Rh123 net secretion was observed. Mixed inhibitor studies demonstrated that Rh123 efflux was mainly Pgp mediated. These results support an energy-dependent Pgp efflux pump pathway that is sensitive to inhibition with CsA in Calu-3 cells., (Copyright 2001 Wiley-Liss, Inc. and the American Pharmaceutical Association.)

Published
2001
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