Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells - Wikidata - wikimedia - TriplyDB

Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells

Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells

http://www.wikidata.org/entity/Q36321055

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Heparanase deglycanation of syndecan-1 is required for binding of the epithelial-restricted prosecretory mitogen lacritin.The transcription factor SOX18 regulates the expression of matrix metalloproteinase 7 and guidance molecules in human endothelial cells Syndecan-1 in Cancer: Implications for Cell Signaling, Differentiation, and Prognostication Molecular and clinical profiles of syndecan-1 in solid and hematological cancer for prognosis and precision medicine Syndecans play dual roles as cell adhesion receptors and docking receptors Insights into the key roles of proteoglycans in breast cancer biology and translational medicine Heparan sulfate signaling in cancer Mechanisms of heparanase inhibitors in cancer therapy.The mutual impact of syndecan-1 and its glycosaminoglycan chains--a multivariable puzzle.Inflammation and Epithelial-Mesenchymal Transition in Pancreatic Ductal Adenocarcinoma: Fighting Against Multiple Opponents Elevated glypican-1 expression is associated with an unfavorable prognosis in pancreatic ductal adenocarcinoma.Membrane type 1 matrix metalloproteinase-mediated stromal syndecan-1 shedding stimulates breast carcinoma cell proliferation.Diagnostic and prognostic value of soluble syndecan-1 in pleural malignancies.Matrix metalloproteinase-7 (matrilysin) controls neutrophil egress by generating chemokine gradients.Soluble syndecan-1 (sCD138) as a prognostic factor independent of mutation status in patients with chronic lymphocytic leukemia WSS25 inhibits growth of xenografted hepatocellular cancer cells in nude mice by disrupting angiogenesis via blocking bone morphogenetic protein (BMP)/Smad/Id1 signaling Heparan sulfate proteoglycans and human breast cancer epithelial cell tumorigenicity.Shed Syndecan-1 is involved in chemotherapy resistance via the EGFR pathway in colorectal cancer Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes.Heparan sulfate proteoglycans.Targeting tumor cell motility to prevent metastasis.Stage and tissue-specific prognostic impact of miR-182 in NSCLC.Heparin impairs angiogenesis through inhibition of microRNA-10b.Omega-3 fatty acids induce apoptosis in human breast cancer cells and mouse mammary tissue through syndecan-1 inhibition of the MEK-Erk pathway A KrasG12D-driven genetic mouse model of pancreatic cancer requires glypican-1 for efficient proliferation and angiogenesis Breast and ovarian cancers: a survey and possible roles for the cell surface heparan sulfate proteoglycans.Relevance of serum levels of interleukin-6 and syndecan-1 in patients with hepatocellular carcinoma Heparan sulfate chains of syndecan-1 regulate ectodomain shedding.Pancreatic cancer-associated stroma production Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells.Toll-like receptor 7 regulates pancreatic carcinogenesis in mice and humans.Interaction of human papillomavirus type 16 particles with heparan sulfate and syndecan-1 molecules in the keratinocyte extracellular matrix plays an active role in infection.Extracellular superoxide dismutase in pulmonary fibrosis Syndecan-1 is an in vivo suppressor of Gram-positive toxic shock Proteoglycans in cancer biology, tumour microenvironment and angiogenesis.Heparanase stimulation of protease expression implicates it as a master regulator of the aggressive tumor phenotype in myeloma Overexpression of glypican-1 implicates poor prognosis and their chemoresistance in oesophageal squamous cell carcinoma.Heparan sulfate and heparanase as modulators of breast cancer progression Expression of genes encoding for proteins involved in heparan sulphate and chondroitin sulphate chain synthesis and modification in normal and malignant plasma cells Glypican-1 controls brain size through regulation of fibroblast growth factor signaling in early neurogenesis.

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P2860

Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells

http://www.wikidata.org/entity/Q36321055

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Growth factor-induced shedding ...... enic responses of cancer cells

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Growth factor-induced shedding ...... enic responses of cancer cells

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Growth factor-induced shedding ...... enic responses of cancer cells

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Growth factor-induced shedding ...... enic responses of cancer cells

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Growth factor-induced shedding ...... enic responses of cancer cells

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Arthur D Lander

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José Antonio Sánchez-Duran

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Kan Ding

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Martha Lopez-Burks

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Murray Korc

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P2860

Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome

The cell-surface heparan sulfate proteoglycan glypican-1 regulates growth factor action in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer

Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells

Soluble syndecan-1 promotes growth of myeloma tumors in vivo

Pancreatic cancer: the potential clinical relevance of alterations in growth factors and their receptors

Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation

Specificities of heparan sulphate proteoglycans in developmental processes

Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)

Glypican-3 modulates BMP- and FGF-mediated effects during renal branching morphogenesis

Intestinal tumorigenesis is suppressed in mice lacking the metalloproteinase matrilysin

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