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evolution
the amino acid sequence of thymidine phosphorylase (TP) is extremely conserved. For instance, human TP shares 39% sequence identity with Escherichia coli TP
evolution
the amino acid sequence of thymidine phosphorylase (TP) is extremely conserved. For instance, human TP shares 39% sequence identity with Escherichia coli TP
evolution
the enzyme is identical to the platelet-derived endothelial cell growth factor (PD-ECGF). Amino acid sequence homology between hepatic thymidine phosphorylase and PD-ECGF
malfunction
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a loss-of-function mutation is involved in mitochondrial neurogastrointestinal encephalomyopathy, an autosomal recessive human disorder associated with multiple deletions of skeletal muscle mitochondrial DNA, overview. Corrleation of tumor development and progression with intratumoral thymidine phsophorylase levels, overview
malfunction
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deficiency of the cytosolic enzyme thymidine phosphorylase causes a multisystem disorder called mitochondrial neurogastrointestinal encephalomyopathy syndrome with symptoms gastrointestinal dysfunction, muscle involvement and neurological deterioration, overview
malfunction
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thymidine phosphorylase promotes angiogenesis. The mechanism of endometrial angiogenesis involves the enzyme and stimulation by ovarian steroids of production of angiogenic regulators by endometrial epithelium and stroma which then act on the endothelium
malfunction
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collagen-, collagen-related peptide-, adenosine diphosphate-and/or thrombin-induced platelet aggregation are significantly attenuated in enzyme deficient platelets. Tymp deficiency also significantly decreases agonist-induced P-select in expression
malfunction
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knocking down enzyme expression enhances the cytotoxicity and cell growth inhibition of tamoxifen
malfunction
EGF receptor inhibition may lead to TP overexpression, which decreases the efficacy of infusional 5-fluorouracil (5FU) regimens, while enhancing that of bolus schedules. Tissue hypoxia secondary to low hemoglobin levels may induce TP overexpression, and subsequently, a relative resistance to infusional 5FU
malfunction
mutation of the TP gene is associated with mitochondrial neurogastrointestinal encephalomyopathy (MNGIE), an autosomal recessive human disease exhibiting multiple deletions of skeletal muscle mitochondrial DNA (peripheral neuropathy, myopathy, leukoencephalopathy, lactic acidosis, gastrointestinal dysmotility, progressive external ophthalmoplegia, and thin body habitus)
malfunction
overexpression of human thymidine phosphorylase (hTP) has been associated with cancer aggressiveness and poor prognosis by triggering proangiogenic and antiapoptotic signaling
malfunction
overexpression of thymidine phosphorylase (TP) causes diseases like psoriasis, chronic inflammatory disease, tumor angiogenesis and rheumatoid arthritis etc. The inhibition of this enzyme is vital to secure life from serious threats
metabolism
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the enzyme is involved in the thymidine salvage pathway and competes with thymidine kinase, overview. Thymidine plays a central role in both proliferation and angiogensis, overview
metabolism
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the enzyme is the key enzyme of the pyrimidine salvage pathway
metabolism
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the enzyme participates in the thymidine salvage pathway maintaining the thymidine pool in the cell
metabolism
the enzyme plays a key role in nucleoside metabolism
metabolism
thymidine phosphorylase is a catabolic enzyme in thymidine metabolism
metabolism
the intracellular catabolism of thymidine mediated via TP produces 2DDR-1P as a metabolic biproduct, which is subsequently converted to 2DDR by the nonenzymatic dephosphorylation. This 2DDR is then secreted from the cells to exhibit the angiogenic effects. Both TP and 2DDR directly stimulate the endothelial cell migration through the activation of focal adhesion kinase (FAK) and the formation of focal adhesions
metabolism
the intracellular catabolism of thymidine mediated via TP produces 2DDR-1P as a metabolic biproduct, which is subsequently converted to 2DDR by the nonenzymatic dephosphorylation. This 2DDR is then secreted from the cells to exhibit the angiogenic effects. Both TP and 2DDR directly stimulate the endothelial cell migration through the activation of focal adhesion kinase (FAK) and the formation of focal adhesions. TP and 2DDR roles in tumour development, overview
metabolism
thymidine phosphorylase (TP) is the key enzyme of the pyrimidine salvage pathway, which speedup the conversion of thymidine and 2'-deoxyuridine to their respective bases and 2-deoxy-D-ribose 1-phosphate
physiological function
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2-deoxy-D-ribose, a downstream mediator of thymidine phosphorylase, regulates tumor angiogenesis and progression, mechanism, overview
physiological function
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heterogeneous nuclear ribonucleoprotein K and thymidine phosphorylase prevent hypoxia-induced apoptosis in nasopharyngeal carcinoma cells, overview
physiological function
the enzyme is the sole endothelial mitogenic and angiogenic factor, it plays a role in the stimulation of chemotaxis and thymidine incorporation into endothelial cells in vitro and angiogenesis in vivo
physiological function
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the enzyme plays an important role in the female reproductive cycle, and is also involved in a wide variety of chronic inflammatory diseases. Dual role of thymidine phosphorylase in cancer development and chemotherapy, acts as thymidine salvage enzyme and as platelet-derived endothelial cell growth factor inducing endothelial cell migration in vitro and angiogenesis in vivo, overview. The enzyme promotes tumor growth and metastasis by preventing apoptosis and inducing angiogenesis. The enzyme is also indispensable for the activation of the extensively used 5-fluorouracil prodrug capecitabine. Role of thymidine phosphorylase in angiogenesis, mediators are matrix metalloproteinases, interleukin-8, P-selectin, and vascular epithelial growth factor, detailed overview
physiological function
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the enzyme promotes the survival and neurite outgrowth of cortical neurons
physiological function
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thymidine phosphorylase is a key regulator of the angiogenic potential of colony-forming units and endothelial progenitor cell cultures, overview. The enzyme is a survival factor, it protects against apoptosis, stimulates endothelial cell migration and enhances wound healing in vitro and angiogenesis in vivo, overview
physiological function
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thymidine phosphorylase inhibits vascular smooth muscle cell proliferation via upregulation of STAT3. Overexpression of thymidine phosphorylase increases STAT3 phosphorylation and expression in vascular smooth muscle cells via Lyn. STAT3 protein but not STAT3 phosphorylation is necessary for thymidine phosphorylase inhibited vascular smooth muscle cell proliferation
physiological function
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transient decrease of mRNA and protein expression by 87.1% and 72.5%, respectively, using siRNAleads to significant decrease in migration of KKU-M139 cells, and suppresses migration and tube formation of human umbilical vein endothelial cells. siRNA also reduces the ability of thymidine phosphorylase to resist hypoxia-induced apoptosis, while suppression of thymidine phosphorylase reduces the sensitivity of KKU-M139 cells to 5-fluorouracil
physiological function
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the enzyme participates in platelet signaling and promotes thrombosis by platelet activation
physiological function
thymidine phosphorlyase is a key enzyme in the pyrimidine salvage pathway and involved in thymidine homeostasis in cells
physiological function
thymidine phosphorylase is not essential for Mycoplasma pneumoniae survival
physiological function
thymidine phosphorylase (TP) catalyzes the reversible phosphorolysis of thymidine, deoxyuridine, and their analogues to their respective nucleobases and 2-deoxy-alpha-D-ribose-1-phosphate. TP is a key enzyme in the pyrimidine salvage pathways. Activity of the enzyme is crucial in angiogenesis, cancer chemotherapy, radiotherapy, and tumor imaging
physiological function
thymidine phosphorylase (TP) is a nucleoside-metabolizing enzyme that plays a key role in 5-fluorouracil (5FU) pharmacokinetics, as well as in the inflammatory response, neoangiogenesis and apoptosis. TP expression is regulated by hypoxia, inflammatory cytokines and antitumoral agents
physiological function
thymidine phosphorylase (TP), an enzyme involved in pyrimidine salvage pathway, is identical to platelet-derived endothelial cell growth factor (PD-ECGF) and gliostatin. The enzyme function in cancer development. TP activity is also shown to augment the levels of hypoxia-inducible factor (HIF)-1alpha during in vitro hypoxia in RT112 cells. Eventually, TP acts in concert with HIF-1a to induce VEGF secretion. Additionally, TP and VEGF are coexpressed in various human cancers and display a cooperative role in neovascularization. TP dramatically reduces the apoptotic index in various cancer cells. TP inactivates and eventually reduces the bioavailability of 5-trifluorothymidine (TFT), a clinically used anticancer drug
physiological function
thymidine phosphorylase (TP), an enzyme involved in pyrimidine salvage pathway, is identical to platelet-derived endothelial cell growth factor (PD-ECGF) and gliostatin. TP activity is also shown to augment the levels of hypoxia-inducible factor (HIF)-1alpha during in vitro hypoxia in RT112 cells. Eventually, TP acts in concert with HIF-1a to induce VEGF secretion. Additionally, TP and VEGF are coexpressed in various human cancers and display a cooperative role in neovascularization. TP dramatically reduces the apoptotic index in various cancer cells
physiological function
thymidine phosphorylase is an important enzyme of the pyrimidine salvage pathways. It catalyzes the reversible phosphorolysis of thymidine, deoxyuridine, but not deoxycytidine, and their analogues, to their respective nucleobases and 2-deoxy-alpha-D-ribose-1-phosphate. The biological significance of TP has several aspects. It has a role in maintaining the integrity of the blood vessels, and its activity is an essential step in the regulation of intra- or extracellular thymidine concentration and homeostasis in mammalian cells. The enzyme is identical to the platelet-derived endothelial cell growth factor (PD-ECGF) which is involved in the process of angiogenesis, neoplastic tissue growth, and metastases. Thymidine phosphorylase is involved regulation of intra- or extracellular thymidine concentration and angiogenesis
physiological function
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thymidine phosphorylase is not essential for Mycoplasma pneumoniae survival
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additional information
elevated enzyme levels are associated with tumor angiogenesis, metastasis and poor prognosis
additional information
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elevated enzyme levels are associated with tumor angiogenesis, metastasis and poor prognosis
additional information
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the cytoplasmic level of heterogeneous nuclear ribonucleoprotein K is significantly correlated with the elevated expression of thymidine phosphorylase, and high levels of both proteins are predictive of a poor prognosis in nasopharyngeal carcinoma
additional information
the important residues of enzyme TP responsible for activity are Ser117, Ser217, His116, Lys221, Arg202, Tyr199, Thr118, Arg146, Leu148, Thr151, Gly152, and Ile214, computational structure-function analysis