Heparanase
From Basic Research to Clinical Applications
Samenvatting
Written by internationally recognized leaders in Heparanase biology, the book’s eight chapters offer an opportunity for scientists, clinicians and advanced students in cell biology, tumor biology and oncology to obtain a comprehensive understanding of Heparanase’s multifaceted activities in cancer, inflammation, diabetes and other diseases, as well as its related clinical applications.
Proteases and their involvement in cancer progression have been well addressed and documented; however, the emerging premise presented within this book is that Heparanase is a master regulator of aggressive cancer phenotypes and crosstalk with the tumor microenvironment. This endoglycosidase contributes to tumor-mediated remodeling of the extracellular matrix and cell surfaces, augmenting the bioavailability of pro-tumorigenic and pro-inflammatory growth factors and cytokines that are bound to Heparan sulfate. Compelling evidence ties Heparanase with all steps of tumor progression including tumor initiation, growth, angiogenesis, metastasis, and chemoresistance, supporting the notion that Heparanase is an important contributor to the poor outcome of cancer patients and a validated target for therapy. Unlike Heparanase, heparanase-2, a close homolog of Heparanase, lacks enzymatic activity, inhibits Heparanase, and regulates selected genes that promote normal differentiation and tumor suppression. Written by internationally recognized leaders in Heparanase biology, this volume presents a comprehensive understanding of Heparanase’s multifaceted activities in cancer, inflammation, diabetes and other diseases, as well as its related clinical applications to scientists, clinicians and advanced students in cell biology, tumor biology and oncology.
Specificaties
Inhoudsopgave
<p>1. Mast cell/platelet heparanase/Heparan sulfate biosynthesis and turnover</p>
<p>2. Gene cloning/overview<br></p>
<p>3. Gene cloning/melanoma metastasis</p>
<p>4. Gene cloning/cancer/immune system</p>
<p>5. Heparin/HS modifying enzymes</p>
<p> </p>
<p>Crystal structure/substrate specificity/gene regulation </p>
<p>6. Crystal structure</p>
<p>7. Molecular dynamics, KKDC peptide</p>
<p>8. Biochemistry/active site</p>
<p>9. Substrate specificity</p>
<p>10.Gene regulation, promoter/Egr1/methylation</p>
<p>11. SNPs - polymorphism</p>
<p>12. Splice variants</p>
<p> </p>
<p>Cell & tumor biology (general functions & mode of action)</p>
<p>13 Exosomes/heparan sulfate/heparanase</p>
<p>14. Exosomes/drug resistance</p>
<p>15. Nuclear heparanase/transcriptional activity</p>
<p> 16. Non-enzymatic functions/signal transduction/cellular trafficking/autophagy</p>
<p>17. Heparan sulfate/stem cells/inflammation</p>
<p>18. Danger signals/HS/platelet heparanase</p>
<p>19. Heparanase/integrins/melanoma</p>
<p> </p>
<p>Immune cells/immuno-modulation</p>
<p>20. Heparin, heparanase & selectins in cancer metastasis and inflammation</p>
<p>21Trans-endithelial migration, lymphocytes/neutrophils/t-cells</p>
<p>22 Macrophages/ dendritic cells/autoimmunity</p>
23. Macrophages, Heparanase and the tumor microenvironment, neutralizing antibodies<p></p>
<p>24. NK cells</p>
<p> </p>
<p>Cancer (heparanase in specic types of cancer)</p>
<p>25. Myeloma/inhibition/drug resistance</p>
<p>26. Breast cancer/pancreatic cancer/Cancer & Inflammation</p>
<p>27 Brain metastasis/mir-1258</p>
<p>28. Gastric cancer/immunization</p>
<p>29. Head & Neck</p>
<p>30. Glioma</p>
31.Sarcoma<p></p>
<p> </p>
<p>Inhibitors/clinical trials/cancer</p>
<p>32. Chemistry/synthesis of heparanase inhibitors PI-88, PG</p>
<p>33. PG series; biology. Tumor models & clinical trial</p>
<p>34 Chemically modified heparins/ Heparin mimetics</p>
<p>35. Roneparstat/small molecules/clinical trials</p>
<p> </p>
<p>Other indications/diseases</p>
<p>36.IBD/inflammation & cancer/diabetes/obesity</p>
<p>37 immune diabetes</p>
<p>38. Inflammation, Sepsis/Amyloidosis</p>
<p>39. Kidney dysfunction</p>
<p>40. Fibrosis</p>
<p>41. Viral infection</p>
<p>42. Cariomyocytes/ Endothelial cell-cardiomyocyte crosstalk in diabetic cardiomyopathy </p>
<p>43. Eye research</p>
<p>44. Atherosclerosis, nuclear localization</p>
<p>45. Coagulation/tissue factor</p>
<p> </p>
<p>Heparanase-2 (Hpa2)</p>
<p>46. Hpa2 gene cloning</p>
<p>47. UFS - urofacial syndrome; peripheral neuropathy</p>
<p>48. Hpa2: tumor suppressor</p>