BibSonomyburst/user/kanefendt/ActivationBibSonomy RSS feed for /user/kanefendt/Activation2012-02-16T16:56:13+01:00http://www.bibsonomy.org/bibtex/27006f0426f910dc9e19ab2973b68d79a/kanefendtkanefendt2010-02-05T11:28:39+01:00Activation Animals Binding Biological Coenzymes Conformation Cross-Talk Enzyme Humans Kinase Kinases Ligands Models Protein Protein-Tyrosine Receptor Research Signal Transduction Tyrosine metabolism pharmacology <span class="authorEditorList"><a href="/author/Hubbard">S. R. Hubbard</a>, and <a href="/author/Miller">W. T. Miller</a> </span><em>Curr.Opin.Cell Biol.</em> <em>19(2):117-123</em> (<em>2007</em>)Fri Feb 05 11:28:39 CET 2010Curr.Opin.Cell Biol.2117-123Receptor tyrosine kinases: mechanisms of activation and signaling192007Activation Animals Binding Biological Coenzymes Conformation Cross-Talk Enzyme Humans Kinase Kinases Ligands Models Protein Protein-Tyrosine Receptor Research Signal Transduction Tyrosine metabolism pharmacology Receptor tyrosine kinases (RTKs) are essential components of signal transduction pathways that mediate cell-to-cell communication. These single-pass transmembrane receptors, which bind polypeptide ligands - mainly growth factors - play key roles in processes such as cellular growth, differentiation, metabolism and motility. Recent progress has been achieved towards an understanding of the precise (and varied) mechanisms by which RTKs are activated by ligand binding and by which signals are propagated from the activated receptors to downstream targets in the cellhttp://www.bibsonomy.org/bibtex/2cf69ff499544b537a6b75c62f9c9f808/kanefendtkanefendt2010-02-05T11:28:39+01:00A Activation Aged Aggregation Angiopoietin-1 Aspirin Biological Blood Case-Control Count Cyclooxygenase Endothelial England Factor Female Follow-Up Growth Humans Hypertension Immunoassay Inhibitors Longitudinal Male Markers Middle Outcome P-Selectin Platelet Platelets Pressure Research Studies Thrombosis Treatment Vascular blood drug effects metabolism methods pharmacology physiopathology therapeutic therapy use <span class="authorEditorList"><a href="/author/Nadar">S. Nadar</a>, <a href="/author/Blann">A. D. Blann</a>, and <a href="/author/Lip">G. Y. Lip</a> </span><em>Am.J.Hypertens.</em> <em>19(9):970-977</em> (<em>2006</em>)Fri Feb 05 11:28:39 CET 2010Am.J.Hypertens.9970-977Effects of aspirin on intra-platelet vascular endothelial growth factor, angiopoietin-1, and p-selectin levels in hypertensive patients192006A Activation Aged Aggregation Angiopoietin-1 Aspirin Biological Blood Case-Control Count Cyclooxygenase Endothelial England Factor Female Follow-Up Growth Humans Hypertension Immunoassay Inhibitors Longitudinal Male Markers Middle Outcome P-Selectin Platelet Platelets Pressure Research Studies Thrombosis Treatment Vascular blood drug effects metabolism methods pharmacology physiopathology therapeutic therapy use BACKGROUND: Although aspirin is useful in reducing platelet activation and cardiovascular events, its effects on platelet levels of angiogenic factors, such as vascular endothelial growth factor (VEGF) and angiopoietin-1 (Ang-1), and markers of platelet activation in hypertension are unknown. The aim of this study was to study the effects of aspirin on the platelet morphology, plasma and platelet levels of VEGF (sVEGF and pVEGF respectively), Ang-1 (sAng-1 and pAng-1 respectively), and P-selectin (sPsel and pPsel respectively) in patients with well controlled hypertension. METHODS: A total of 35 aspirin-naive, hypertensive patients (29 male and six female; mean age 64 years) were compared with 30 (23 male, seven female, mean age 59 years) normotensive control subjects. Blood was collected for plasma VEGF, P-selectin, and Ang-1 (enzyme-linked immunoassay), intra-platelet levels of VEGF, Ang-1, and P-selectin, and platelet volume and mass. Research indices in hypertensive patients were shttp://www.bibsonomy.org/bibtex/2fdc813c8de774f99db38d80c7745dbef/kanefendtkanefendt2010-02-05T11:28:39+01:005 Activation Alleles Animals C Cell Chemistry Chromosomes Data Dominant Endothelial Enzyme Factor Factors Female Fusion Genes Growth Half-Life Human Humans Infant Kinase Kinases Laboratories Line Lymphedema Male Mice Missense Models Molecular Mutation Newborn Pair Pedigree Phosphorylation Protein Protein-Tyrosine Proteins Receptor Receptor-3 Receptors Recombinant Research Sequence Signal Stability Structure Surface Transcriptional Transduction Tyrosine Vascular congenital drug effects genetics metabolism pharmacology protein secondary <span class="authorEditorList"><a href="/author/Karkkainen">M. J. Karkkainen</a>, <a href="/author/Ferrell">R. E. Ferrell</a>, <a href="/author/Lawrence">E. C. Lawrence</a>, <a href="/author/Kimak">M. A. Kimak</a>, <a href="/author/Levinson">K. L. Levinson</a>, <a href="/author/McTigue">M. A. McTigue</a>, <a href="/author/Alitalo">K. Alitalo</a>, and <a href="/author/Finegold">D. N. Finegold</a> </span><em>Nat.Genet.</em> <em>25(2):153-159</em> (<em>2000</em>)Fri Feb 05 11:28:39 CET 2010Nat.Genet.2153-159Missense mutations interfere with VEGFR-3 signalling in primary lymphoedema2520005 Activation Alleles Animals C Cell Chemistry Chromosomes Data Dominant Endothelial Enzyme Factor Factors Female Fusion Genes Growth Half-Life Human Humans Infant Kinase Kinases Laboratories Line Lymphedema Male Mice Missense Models Molecular Mutation Newborn Pair Pedigree Phosphorylation Protein Protein-Tyrosine Proteins Receptor Receptor-3 Receptors Recombinant Research Sequence Signal Stability Structure Surface Transcriptional Transduction Tyrosine Vascular congenital drug effects genetics metabolism pharmacology protein secondary Primary lymphoedema is a rare, autosomal dominant disorder that leads to a disabling and disfiguring swelling of the extremities and, when untreated, tends to worsen with time. Here we link primary human lymphoedema to the FLT4 locus, encoding vascular endothelial growth factor receptor-3 (VEGFR-3), in several families. All disease-associated alleles analysed had missense mutations and encoded proteins with an inactive tyrosine kinase, preventing downstream gene activation. Our study establishes that VEGFR-3 is important for normal lymphatic vascular function and that mutations interfering with VEGFR-3 signal transduction are a cause of primary lymphoedemahttp://www.bibsonomy.org/bibtex/241b22e9a7cae94814792ffa4f105b207/kanefendtkanefendt2010-02-05T11:28:39+01:00&amp; A Activation Antineoplastic Blood Breast Burden Chemotherapy Colony-Stimulating Combined Cyclophosphamide Doxorubicin Endothelial Factor Factors Female Granulocyte-Macrophage Growth Healing Humans Lymphokines Medical Neoplasms Oncology Platelet Platelets Protocols Reference Research Tumor Values Vascular Wound administration adverse blood dosage drug effects physiology therapeutic therapy use <span class="authorEditorList"><a href="/author/Verheul">H. M. Verheul</a>, <a href="/author/Hoekman">K. Hoekman</a>, <a href="/author/de">Bakker S. Luykx de</a>, <a href="/author/Eekman">C. A. Eekman</a>, <a href="/author/Folman">C. C. Folman</a>, <a href="/author/Broxterman">H. J. Broxterman</a>, and <a href="/author/Pinedo">H. M. Pinedo</a> </span><em>Clin.Cancer Res.</em> <em>3(12 Pt 1):2187-2190</em> (<em>1997</em>)Fri Feb 05 11:28:39 CET 2010Clin.Cancer Res.12 Pt 12187-2190Platelet: transporter of vascular endothelial growth factor31997& A Activation Antineoplastic Blood Breast Burden Chemotherapy Colony-Stimulating Combined Cyclophosphamide Doxorubicin Endothelial Factor Factors Female Granulocyte-Macrophage Growth Healing Humans Lymphokines Medical Neoplasms Oncology Platelet Platelets Protocols Reference Research Tumor Values Vascular Wound administration adverse blood dosage drug effects physiology therapeutic therapy use In animal models, growth of tumors and their metastases is dependent on factors that stimulate vessel formation (angiogenesis). Most clinical studies confirm the importance of angiogenesis for cancer growth in patients. Recent studies on circulating angiogenic factors in patients have focused on serum vascular endothelial growth factor (VEGF) levels in a variety of cancer types. We measured serum VEGF concentrations and blood counts in 27 breast cancer patients during each of 6 cycles of chemotherapy with doxorubicin and cyclophosphamide supported by granulocyte macrophage colony-stimulating factor. Serum VEGF concentrations highly correlated with platelet counts during chemotherapy (r = 0.8; P < 0.01). In particular, during the first treatment cycle, after an initial episode of thrombocytopenia, a strong platelet rebound coincided closely with a serum VEGF peak (r = 0.9; P < 0.01). In addition, plasma VEGF concentrations from 15 other cancer patients and 30 healthy volunteers were 5- http://www.bibsonomy.org/bibtex/2dcd4cc2ed8e0bb113931393fabbf2889/kanefendtkanefendt2010-02-05T11:28:39+01:003 Acid Activation Acute Amino Cell DNA-Binding Data Enzyme Factor Human Humans Indoles Kinase Kinases Leukemia Milk Mitogen-Activated Molecular Mutation Myeloid Neoplastic Phenotype Phosphorylation Protein Protein-Tyrosine Proteins Proto-Oncogene Receptor Research STAT3 STAT5 Sequence Trans-Activators Transcription Transformation Tyrosine cells fms-Like metabolism pathology pharmacology physiology protein response therapy <span class="authorEditorList"><a href="/author/Spiekermann">K. Spiekermann</a>, <a href="/author/Bagrintseva">K. Bagrintseva</a>, <a href="/author/Schwab">R. Schwab</a>, <a href="/author/Schmieja">K. Schmieja</a>, and <a href="/author/Hiddemann">W. Hiddemann</a> </span><em>Clin.Cancer Res.</em> <em>9(6):2140-2150</em> (<em>2003</em>)Fri Feb 05 11:28:39 CET 2010Clin.Cancer Res.62140-2150Overexpression and constitutive activation of FLT3 induces STAT5 activation in primary acute myeloid leukemia blast cells920033 Acid Activation Acute Amino Cell DNA-Binding Data Enzyme Factor Human Humans Indoles Kinase Kinases Leukemia Milk Mitogen-Activated Molecular Mutation Myeloid Neoplastic Phenotype Phosphorylation Protein Protein-Tyrosine Proteins Proto-Oncogene Receptor Research STAT3 STAT5 Sequence Trans-Activators Transcription Transformation Tyrosine cells fms-Like metabolism pathology pharmacology physiology protein response therapy PURPOSE: Activating length mutations in the juxtamembrane domain (FLT3-LM) and mutations in the tyrosine kinase domain (FLT3-TKD) of FLT3 represent the most frequent genetic alterations in acute myeloid leukemia (AML). However, the functional role of active FLT3 mutants in primary AML blast cells is not well characterized. EXPERIMENTAL DESIGN: We analyzed the transforming potential and the signaling of FLT3-ITD mutants in Ba/F3 cells and in primary AML blasts. RESULTS: FLT3-ITD mutants induce an autophosphorylation of the receptor, interleukin 3-independent growth in Ba/F3 cells, and a strong STAT5 and mitogen-activated protein kinase (MAPK) activation. In contrast to the FLT3-ITD mutants, the ligand-stimulated FLT3-WT receptor was unable to transduce a fully proliferative response in Ba/F3 and monocytic OCI-AML5 cells. The ligand-stimulated FLT3-WT receptor activated AKT and MAPK, but not STAT5. In primary blast cells from 60 patients with AML, FLT3 was expressed in 91.9% of patients