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  • 1
    Online Resource
    Online Resource
    Heparanase : From Basic Research to Clinical Applications (2020)
    Cham :Springer International Publishing :
    Details
    Keywords: Cancer. ; Oncology. ; Medicine Research. ; Biology Research. ; Cancer Biology. ; Oncology. ; Biomedical Research.
    Description / Table of Contents: Section 1: Historical Background -- Chapter 1: Mast cell/platelet heparanase/Heparan sulfate biosynthesis and turnover -- Chapter 2: gene cloning/overview -- Chapter 3: gene cloning/melanoma metastasis -- Chapter 4: gene cloning/cancer/immune system -- Chapter 5: heparin/HS modifying enzymes -- Section 2: Crystal Structure/substrate specificity/gene regulation -- Chapter 6: crystal structure -- Chapter 7: molecular dynamics, KKDC peptide -- Chapter 8: Biochemistry/active site -- Chapter 9: substrate specificity -- Chapter 10: gene regulation, promoter/Egr1/methylation -- Chapter 11: SNPs -- polymorphism -- Chapter 12: Splice variants -- Section 3: Cell & tumor biology (general functions & mode of action) -- Chapter 13: Exosomes/heparan sulfate/heparanse -- Chapter 14: Exosomes/drug resistance -- Chapter 15: Nuclear heparanse/transcriptional activity -- Chapter 16: Non-Enzymatic functions/Signal transduction/cellular trafficking/autophagy -- Chapter 17: Heparan sulfate/stem cells/inflammation -- Chapter 18: Danger signals/HS/platelet heparanse -- Chapter 19: Heparanse/Intergrins/Melanoma -- Section 3: Immune Cells/Immnuno-Modulation -- Chapter 20: Heparain. Heparanse and Selectins in Cancer Metastasis and Inflamation --- Chapter 21: Trans-Endithelial Migration, Lymphocytes, Neutrophils/T-cells --Chapter 22: Macrophages, dendritic cells, autoimmunity -- Chapter 23: Macrophages, Heparanse and the tumor microenvironment, neutralizing antibodies -- Chapter 24: NK Cells -- Section 4: Cancer (heparanse in specific types of cancer) -- Chapter 25: Myeloma, inhbition, drug resistance -- Chapter 26: Breast Cancer/Pancreatic Cancer/Cancer and Inflammation -- Chapter 27: Brain Metastasis/MIR-1258 -- Chapter 28: Gastric cancer/immunization -- Chapter 29: Head and Neck Cancer -- Chapter 30: Glioma -- Chapter 31: Sarcoma -- Section 5: Inhibitors/clinical trails/cancer -- Chapter 32: Chemistry/synthesis of heparanse inhibitors PI-88, PG -- Chapter 33: PG series/biology/Tumor models and clinical trial -- Chapter 34:Chemically modified heparins/Heparin mimetics -- Chapter 35: Medicinal Chemistry (Ronesparstat/small molecules/clinical trials) - Section 6: Other indications/diseases -- Chapter 36: IBD/inflammation and cancer/diabetes/obesity -- Chapter 37: Immune Diabetes -- Chapter 38 Inflammation, Sepsis/Amyloidosis -- Chapter 39: Kidney dysfunction -- Chapter 40: Fibrosis -- Chapter 41: Viral infection -- Chapter 42: Cariomyocytes/Endothelial cell-cardiomyocyte crosstakl in diabetic cariomyopathy -- Chapter 43: Eye research -- Chapter 44: atheroscelerosis, nuclear localization -- Chapter 45: Yona Nadir (coagulation/tissue factor) -- Section 7: Heparanse-2 (Hpa2) -- Chapter 46: Hpa2 gene cloning -- Chapter 47: UFS -- urofacial syndrome/peripheral neuropathy -- Chapter 48: Hpa2: tumor suppressor.
    Abstract: 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.
    Type of Medium: Online Resource
    Pages: XVIII, 885 p. 168 illus., 107 illus. in color. , online resource.
    Edition: 1st ed. 2020.
    ISBN: 9783030345211
    Series Statement: Advances in Experimental Medicine and Biology, 1221
    URL: https://doi.org/10.1007/978-3-030-34521-1
    DOI: 10.1007/978-3-030-34521-1
    DDC: 571.978
    Language: English
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  • 2
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    Heparan sulfate proteoglycans in invasion and metastasis (2001)
    Elsevier
    Details
    Publication Date: 2001-04-01
    Print ISSN: 1084-9521
    Electronic ISSN: 1096-3634
    Topics: Biology , Medicine
    Published by Elsevier
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  • 3
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    Opposing Functions of Heparanase-1 and Heparanase-2 in Cancer Progression (2018)
    Cell Press
    Details
    Publication Date: 2018-01-01
    Print ISSN: 0968-0004
    Electronic ISSN: 1362-4326
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Cell Press
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  • 4
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    Heparanase promotes the spontaneous metastasis of myeloma cells to bone (2005)
    American Society of Hematology
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    Publication Date: 2005-02-01
    Description: Although widespread skeletal dissemination is a critical step in the progression of myeloma, little is known regarding mechanisms that control metastasis of this cancer. Heparanase-1 (heparanase), an enzyme that cleaves heparan sulfate chains, is expressed at high levels in some patients with myeloma and promotes metastasis of some tumor types (eg, breast, lymphoma). Using a severe combined immunodeficient (SCID) mouse model, we demonstrate that enhanced expression of heparanase by myeloma cells dramatically up-regulates their spontaneous metastasis to bone. This occurs from primary tumors growing subcutaneously and also from primary tumors established in bone. Interestingly, tumors formed by subcutaneous injection of cells metastasize not only to bone, but also to other sites including spleen, liver, and lung. In contrast, tumors formed by injection of cells directly into bone exhibit a restricted pattern of metastasis that includes dissemination of tumor to other bones but not to extramedullary sites. In addition, expression of heparanase by myeloma cells (1) accelerates the initial growth of the primary tumor, (2) increases whole-body tumor burden as compared with controls, and (3) enhances both the number and size of microvessels within the primary tumor. These studies describe a novel experimental animal model for examining the spontaneous metastasis of bone-homing tumors and indicate that heparanase is a critical determinant of myeloma dissemination and growth in vivo.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 5
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    Soluble syndecan-1 promotes growth of myeloma tumors in vivo (2002)
    American Society of Hematology
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    Publication Date: 2002-07-15
    Description: Syndecan-1 (CD138) is a transmembrane heparan sulfate–bearing proteoglycan expressed by most myeloma plasma cells that regulates adhesion, migration, and growth factor activity. In patients with myeloma, shed syndecan-1 accumulates in the bone marrow, and high levels of syndecan-1 in the serum are an indicator of poor prognosis. To test the effect of soluble syndecan-1 on tumor cell growth and dissemination, ARH-77 B-lymphoid cells were engineered to produce a soluble form of syndecan-1. Controls included vector only (neo)–transfected cells and cells transfected with full-length syndecan-1 complementary DNA that codes for the cell surface form of syndecan-1. Assays reveal that all 3 transfectants have similar growth rates in vitro, but cells expressing soluble syndecan-1 are hyperinvasive in collagen gels relative to controls. When injected into the marrow of human bones that were implanted in severe combined immunodeficient mice, tumors formed by cells expressing soluble syndecan-1 grow faster than tumors formed by neo-transfected cells or by cells expressing cell surface syndecan-1. In addition, cells bearing cell surface syndecan-1 exhibit a diminished capacity to establish tumors within the mice as compared with both neo- and soluble syndecan-1–transfected cells. Tumor cell dissemination to a contralateral human bone is detected significantly more often in the tumors producing soluble syndecan-1 than in controls. Thus, high levels of soluble syndecan-1 present in patients with myeloma may contribute directly to the growth and dissemination of the malignant cells and thus to poor prognosis.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 6
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    The epidermal growth factor–like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans (2003)
    American Society of Hematology
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    Publication Date: 2003-10-15
    Description: Using multivalent protein probes, an evolutionarily conserved endogenous ligand for EMR2, a human myeloid cell–restricted EGF-TM7 receptor, was identified on the surface of a number of adherent cell lines. In addition, in situ staining of the ligand has revealed specific in vivo patterns consistent with a connective tissue distribution. The interaction is conserved across species and mediated exclusively by the largest EMR2 isoform containing 5 epidermal growth factor (EGF)–like modules. Antibody-blocking studies subsequently revealed that the fourth EGF-like module constitutes the major ligand-binding site. The largest isoform of CD97, a related EGF-TM7 molecule containing an identical EGF-like module, also binds to the putative EMR2 ligand. Through the use of mutant Chinese hamster ovary (CHO) cell lines defective in glycosaminoglycans (GAGs) biosynthesis as well as the enzymatic removal of specific cell surface GAGs, the molecular identity of the EMR2 ligand was identified as chondroitin sulfate (CS). Thus, exogenous CS GAGs blocked the EMR2-ligand interaction in a dose-dependent manner. EMR2-CS interaction is Ca2+- and sulphation-dependent and results in cell attachment. This is the first report of a GAG ligand for the TM7 receptors extending the already vast repertoire of stimuli of the GPCR superfamily.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 7
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    Sperm protein 17 is expressed on normal and malignant lymphocytes and promotes heparan sulfate–mediated cell-cell adhesion (2001)
    American Society of Hematology
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    Publication Date: 2001-10-01
    Description: Sperm protein 17 (Sp17) is a highly conserved mammalian protein present on acrosome-reacted sperm that is thought to promote fertilization by binding sulfated carbohydrates of the oocyte zona pellucida. Although Sp17 was originally described as a testis-specific antigen, emerging evidence indicates that it may be more ubiquitously expressed than was previously thought. With the use of a specific antiserum, Sp17 was found to be present on the surface of malignant lymphoid cells, including B- and T-lymphoid cell lines, and on the surface of primary cells isolated from 2 patients having B-lymphoid tumors. Surprisingly, circulating B lymphocytes isolated from healthy volunteers also expressed Sp17, while circulating T lymphocytes exhibited only very weak expression. The role of Sp17 in promoting lymphoid cell adhesion was addressed with the use of recombinant Sp17 (rSp17). The rSp17 binds to the surface of myeloma cells but not to cells pretreated with heparitinase, an enzyme that removes heparan sulfate from the cell surface. Moreover, rSp17 promotes extensive aggregation of cells that express the syndecan-1 heparan sulfate proteoglycan, but in contrast, cells lacking syndecan-1 expression fail to aggregate in the presence of rSp17. These findings suggest that Sp17 promotes heparan sulfate–mediated cell aggregation and thereby plays a role in regulating adhesion and migration of normal and malignant lymphocytes.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 8
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    A Heparin-Based Inhibitor of Heparanase Blocks Myeloma Growth In Vivo by Targeting the Tumor Microenvironment. (2007)
    American Society of Hematology
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    Publication Date: 2007-11-16
    Description: Heparanase is an enzyme that cleaves heparan sulfate chains of proteoglycans and promotes the growth and metastasis of many types of human tumors. Our previous work demonstrates that enzymatically active heparanase is present in the bone marrow of myeloma patients and is associated with a poor prognosis, substantially enhances tumor growth and spontaneous metastasis to bone in an animal model of myeloma, and increases the synthesis and shedding of syndecan-1 by myeloma cells, this in turn contributes to myeloma progression by elevating levels of syndecan-1 in the tumor microenvironment. Thus, we hypothesized that inhibitors of heparanase activity would have a dramatic impact on the growth of myeloma tumors. To test this we used a chemically modified form of heparin that is 100% N-acetylated and 25% glycol-split (designated 100NA,RO-H). This form heparin is a potent inhibitor of heparanase enzyme activity but lacks anticoagulant activity thus enabling use of relatively high doses of the drug in vivo. Delivery of the 100NA,RO-H to animals bearing established myeloma tumors dramatically blocked tumor growth and progression in a dose-dependent manner(P
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    Published by American Society of Hematology
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  • 9
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    Syndecan-1 is targeted to the uropods of polarized myeloma cells where it promotes adhesion and sequesters heparin-binding proteins (2000)
    American Society of Hematology
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    Publication Date: 2000-10-01
    Description: Syndecan-1 (CD138) is a heparan sulfate-bearing proteoglycan present on the surface of myeloma cells where it mediates myeloma cell-cell and cell-extracellular matrix adhesion. In this study, we examined myeloma cell lines for cell membrane localization of syndecan-1. On some cells we note a striking localization of syndecan-1 to a single small membrane protrusion, with the remainder of the cell surface being mostly negative for syndecan-1. Examination of cell morphology reveals that a proportion of cells from myeloma cell lines, as well as primary myeloma cells, are polarized, with a uropod on one end and lamellipodia on the other end. On these polarized cells, syndecan-1 is specifically targeted to the uropod, but in contrast, on nonpolarized cells syndecan-1 is evenly distributed over the entire cell surface. In addition to syndecan-1, several other cell surface molecules localize specifically to the uropod, including CD44 and CD54. Functional assays reveal that myeloma cell lines with a high proportion of polarized cells have a much higher migratory potential than cell lines with few polarized cells. Moreover, the uropod is the cell pole preferentially involved in aggregation of myeloma cells and in adhesion of myeloma cells to osteoblast-like cells. When polarized myeloma cells are incubated with heparin-binding proteins, like hepatocyte growth factor or osteoprotegerin, they concentrate in the uropod. These data indicate that syndecan-1 is targeted to the uropod of polarized myeloma cells and that this targeting plays a role in promoting cell-cell adhesion and may also regulate the biological activity of heparin-binding cytokines.
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    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 10
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    Syndecan-1 Is a Multifunctional Regulator of Myeloma Pathobiology: Control of Tumor Cell Survival, Growth, and Bone Cell Differentiation (1998)
    American Society of Hematology
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    Publication Date: 1998-04-15
    Description: Multiple myeloma is characterized by an accumulation of malignant plasma cells in the bone marrow coupled with an altered balance of osteoclasts and osteoblasts, leading to lytic bone disease. Although some of the cytokines driving this process have been characterized, little is known about the negative regulators. We show that syndecan-1 (CD 138), a heparan sulfate proteoglycan, expressed on and actively shed from the surface of most myeloma cells, induces apoptosis and inhibits the growth of myeloma tumor cells and also mediates decreased osteoclast and increased osteoblast differentiation. The addition of intact purified syndecan-1 ectodomain (1 to 6 nmol/L) to myeloma cell lines in culture leads to induction of apoptosis and dose-dependent growth inhibition, with concurrent downregulation of cyclin D1. The addition of purified syndecan-1 in picomolar concentrations to bone marrow cells in culture leads to a dose-dependent decrease in osteoclastogenesis and a smaller increase in osteoblastogenesis. In contrast to the effect on myeloma cells, the effect of syndecan-1 on osteoclastogenesis only requires the syndecan-1 heparan sulfate chains and not the intact ectodomain, suggesting that syndecan's effect on myeloma and bone cells occurs through different mechanisms. When injected in severe combined immune deficient (scid) mice, control-transfected myeloma cells (ARH-77 cells) expressing little syndecan-1 readily form tumors, leading to hind limb paralysis and lytic bone disease. However, after the injection of syndecan-1–transfected ARH-77 cells, the development of disease-related morbidity and lytic bone disease is significantly inhibited. Taken together, our data demonstrate, both in vitro and in vivo, that syndecan-1 has a significant beneficial effect on the behavior of both myeloma and bone cells and therefore may represent one of the central molecules in the regulation of myeloma pathobiology.
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    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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