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Edward L Schwartz - One of the best experts on this subject based on the ideXlab platform.

  • thymidine phosphorylase and 2 Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αvβ3
    Journal of Biological Chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Abstract Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin α5β1 or αvβ3, whereas VEGF-induced endothelial cell migration was only blocked by the αvβ3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin α5β1 and, in intact cells, increased the co-localization of focal adhesion kinase with α5β1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to α5β1 and αvβ3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of α5β1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

  • Thymidine phosphorylase and 2-Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αVβ3
    The Journal of biological chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin alpha 5 beta 1 or alpha v beta 3, whereas VEGF-induced endothelial cell migration was only blocked by the alpha v beta 3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin alpha 5 beta 1 and, in intact cells, increased the co-localization of focal adhesion kinase with alpha 5 beta 1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to alpha 5 beta 1 and alpha v beta 3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of alpha 5 beta 1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

Kylie A. Hotchkiss - One of the best experts on this subject based on the ideXlab platform.

  • thymidine phosphorylase and 2 Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αvβ3
    Journal of Biological Chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Abstract Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin α5β1 or αvβ3, whereas VEGF-induced endothelial cell migration was only blocked by the αvβ3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin α5β1 and, in intact cells, increased the co-localization of focal adhesion kinase with α5β1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to α5β1 and αvβ3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of α5β1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

  • Thymidine phosphorylase and 2-Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αVβ3
    The Journal of biological chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin alpha 5 beta 1 or alpha v beta 3, whereas VEGF-induced endothelial cell migration was only blocked by the alpha v beta 3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin alpha 5 beta 1 and, in intact cells, increased the co-localization of focal adhesion kinase with alpha 5 beta 1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to alpha 5 beta 1 and alpha v beta 3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of alpha 5 beta 1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

Anthony W. Ashton - One of the best experts on this subject based on the ideXlab platform.

  • thymidine phosphorylase and 2 Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αvβ3
    Journal of Biological Chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Abstract Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin α5β1 or αvβ3, whereas VEGF-induced endothelial cell migration was only blocked by the αvβ3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin α5β1 and, in intact cells, increased the co-localization of focal adhesion kinase with α5β1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to α5β1 and αvβ3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of α5β1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

  • Thymidine phosphorylase and 2-Deoxyribose stimulate human endothelial cell migration by specific activation of the integrins α5β1 and αVβ3
    The Journal of biological chemistry, 2003
    Co-Authors: Kylie A. Hotchkiss, Anthony W. Ashton, Edward L Schwartz
    Abstract:

    Thymidine phosphorylase is an angiogenic factor that is frequently overexpressed in solid tumors, in rheumatoid arthritis, and in response to inflammatory cytokines. Our previous studies showed that cells expressing thymidine phosphorylase stimulated endothelial cell migration in vitro. This was a consequence of the intracellular metabolism of thymidine by thymidine phosphorylase and subsequent extracellular release of 2-Deoxyribose. The mechanisms by which 2-Deoxyribose might mediate thymidine phosphorylase-induced cell migration in vitro, however, are obscure. Here we show that both thymidine phosphorylase and 2-Deoxyribose stimulated the formation of focal adhesions and the tyrosine 397 phosphorylation of focal adhesion kinase in human umbilical vein endothelial cells. Although similar actions occurred upon treatment with the angiogenic factor vascular endothelial growth factor (VEGF), thymidine phosphorylase differed from VEGF in that its effect on endothelial cell migration was blocked by antibodies to either integrin alpha 5 beta 1 or alpha v beta 3, whereas VEGF-induced endothelial cell migration was only blocked by the alpha v beta 3 antibody. Further, thymidine phosphorylase and 2-Deoxyribose, but not VEGF, increased the association of both focal adhesion kinase and the focal adhesion-associated protein vinculin with integrin alpha 5 beta 1 and, in intact cells, increased the co-localization of focal adhesion kinase with alpha 5 beta 1. Thymidine phosphorylase and 2-Deoxyribose-induced focal adhesion kinase phosphorylation was blocked by the antibodies to alpha 5 beta 1 and alpha v beta 3, directly linking the migration and signaling components of thymidine phosphorylase and 2-Deoxyribose action. Cell surface expression of alpha 5 beta 1 was also increased by thymidine phosphorylase and 2-Deoxyribose. These experiments are the first to demonstrate a direct effect of thymidine phosphorylase and 2-Deoxyribose on signaling pathways associated with endothelial cell migration.

Jacob Yashphe - One of the best experts on this subject based on the ideXlab platform.

  • Regulation of the synthesis and activity of thymidine phosphorylase in Lactobacillus casei
    Fems Microbiology Letters, 1991
    Co-Authors: Yosefa Avraham, Nathan Grossowicz, Jacob Yashphe
    Abstract:

    Lactobacillus casei cells grown on excess thymine or on folic acid contained low levels of thymidine phosphorylase. On the other hand, thymine starved cells and also cells of a thymidine-monophosphate-kinase-defective mutant grown on excess thymine, possessed derepressed levels. These results suggest that the synthesis of thymidine phosphorylase is regulated by the end product of the thymidine-triphosphate-biosynthetic pathway. L. casei cells lacked 2-Deoxyribose-1-phosphate-mutase activity and did not grow on 2-Deoxyribose or thymidine as the sole-carbon source. Growth in the presence of thymidine did not result in induction of thymidine-phosphorylase synthesis, probably due to the inability of the cell to convert it to 2-Deoxyribose-5-phosphate, which is known to act as an inducer in E. coli cells. Thymidine triphosphate inhibited non-competitively the activity of thymidine phosphorylase. It was also inhibited by dihydrofolic acid.

Yoshiharu Ishido - One of the best experts on this subject based on the ideXlab platform.

  • Assignments of the Deoxyribose Vibrations: Isotopic Thymidine
    Bulletin of the Chemical Society of Japan, 1994
    Co-Authors: Masamichi Tsuboi, Toyotoshi Ueda, Koichi Ushizawa, Yasuhiro Sasatake, Akira Ono, Masatsune Kainosho, Yoshiharu Ishido
    Abstract:

    Raman spectrum of thymidine-13C5, in which five C atoms of the Deoxyribose moiety are uniformly substituted with 13C atoms, has been examined in the crystalline state with 488.0 nm excitation. Some of the Raman bands were observed at appreciably shifted frequencies from those of the corresponding Raman bands of the natural thymidine, and they were assigned to some vibrations involving Deoxyribose motions.