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The FEBS Journal

Cover image for Vol. 280 Issue 10

Special Issue: Proteoglycans: signaling, targeting and therapeutics

May 2013

Volume 280, Issue 10

Pages i–iii, 2119–2534

  1. Front Cover

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
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      Front Cover (page i)

      Version of Record online: 9 MAY 2013 | DOI: 10.1111/j.1742-4658.2013.08778.x

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      Proteoglycans: signaling, targeting and therapeutics. Top left hand: KS structural motif (A. Weyers et al. pp 2285–2293); Top right hand: HSPGs in multiple myeloma pathogenesis (R.M. Reijmers et al. pp 2180–2193); Centre: Serglycin in myeloma cell properties (A. Skliris et al. pp 2342–2352); Background: Neoproteoglycans in tissue engineering (A. Weyers & R.J. Linhardt pp 2511–2522).

  2. Editorial Information

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
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      Editorial Information (pages ii–iii)

      Version of Record online: 9 MAY 2013 | DOI: 10.1111/j.1742-4658.2013.08778_1.x

  3. Special Issue

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Special Issue: Proteoglycans: signaling, targeting and therapeutics : Introduction (page 2119)

      Nikos K. Karamanos and Robert J. Linhardt

      Version of Record online: 18 APR 2013 | DOI: 10.1111/febs.12262

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      This special issue of FEBS Journal contains 31 review and primary research articles reflecting the advancements covered at the 2012 Proteoglycans Gordon Research Conference and novel aspects from experts in the field. It is mainly focused on current status of the extracellular and cell surface proteoglycans’ regulatory roles in cell signaling, molecular targeting, engineering attempts and potential therapeutic approaches.

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      The regulatory roles of small leucine-rich proteoglycans in extracellular matrix assembly (pages 2120–2137)

      Shoujun Chen and David E. Birk

      Version of Record online: 14 FEB 2013 | DOI: 10.1111/febs.12136

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      Small leucine-rich proteoglycans (SLRPs) have protein cores and hypervariable glycosylation with multivalent binding abilities. During development, differential interactions of SLRPs with other molecules results in tissue-specific spatial and temporal distributions. This review focuses on their structural and instructive roles in regulating matrix assembly, cell-matrix interactions, and their abnormal expression and/or structures that result in dysfunctional extracellular matrices and pathophysiology.

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      Dichotomy of decorin activity on the insulin-like growth factor-I system (pages 2138–2149)

      Andrea Morrione, Thomas Neill and Renato V. Iozzo

      Version of Record online: 15 FEB 2013 | DOI: 10.1111/febs.12149

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      In this mini-review we discuss the emerging dichotomy that decorin exhibits on the IGF-IR system in either normal or malignant cells. Under physiological conditions, IGF-IR phosphorylation and downstream signaling ensue upon decorin engagement. However, in pathological states such as transformed cells, decorin exerts suppression of IRS-1, MAPK, and PI3K pathways as key effectors of IGF-IR-dependent tumorigenesis without affecting receptor stability.

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      Decorin interferes with platelet-derived growth factor receptor signaling in experimental hepatocarcinogenesis (pages 2150–2164)

      Kornélia Baghy, Zsolt Horváth, Eszter Regős, Katalin Kiss, Zsuzsa Schaff, Renato V. Iozzo and Ilona Kovalszky

      Version of Record online: 25 MAR 2013 | DOI: 10.1111/febs.12215

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      Decorin acts as a tumor repressor in a variety of cancers by blocking the action of receptor tyrosine kinases. Genetic ablation of decorin led to enhanced tumor formation in the liver. These findings correlated with decreased levels of p21Waf1/Cip1 and concurrent activation of PDGFRα. The blocking action of decorin on PDGFRα is established via binding and sequestering the ligand PDGF.

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      Biological interplay between proteoglycans and their innate immune receptors in inflammation (pages 2165–2179)

      Helena Frey, Nina Schroeder, Tina Manon-Jensen, Renato V. Iozzo and Liliana Schaefer

      Version of Record online: 21 FEB 2013 | DOI: 10.1111/febs.12145

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      Proteoglycans maintain and regulate the architecture of extracellular matrices, but also constitute ligands of numerous receptors that regulate growth, motility, and immune responses. In this review, we critically assess the signaling events induced by the proteoglycans biglycan, decorin, lumican, and versican as well as the glycosaminoglycan hyaluronan during inflammation.

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      Heparan sulfate proteoglycans in the control of B cell development and the pathogenesis of multiple myeloma (pages 2180–2193)

      Rogier M. Reijmers, Marcel Spaargaren and Steven T. Pals

      Version of Record online: 4 MAR 2013 | DOI: 10.1111/febs.12180

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      Heparan sulfate proteoglycans (HSPGs) are macromolecules that display modified HS domains providing docking sites for growth factors and chemokines. The development of normal B lymphocytes and the progression of B-lineage malignancies depend on many of such factors. Here, we discuss the latest research on the role of HSPGs in these processes and the opportunities for therapy in multiple myeloma by targeting HS.

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      Vascular endothelial-cadherin stimulates syndecan-1-coupled insulin-like growth factor-1 receptor and cross-talk between αVβ3 integrin and vascular endothelial growth factor receptor 2 at the onset of endothelial cell dissemination during angiogenesis (pages 2194–2206)

      Alan C. Rapraeger, Brian J. Ell, Madhuchhanda Roy, Xuehui Li, Orrianne R. Morrison, Grant M. Thomas and DeannaLee M. Beauvais

      Version of Record online: 11 FEB 2013 | DOI: 10.1111/febs.12134

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      The αVβ3 integrin is captured with the insulin-like growth factor-1 receptor (IGF1R) by the matrix receptor syndecan-1 (Sdc1). This core receptor complex is required for angiogenesis stimulated by VEGF and VE-cadherin. Disruption of the Sdc1-coupled complex by synstatin prevents activation of VEGFR2 by VEGF or by homophillic VE-cadherin engagement and prevents the initial phase of endothelial cell dissemination during angiogenesis.

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      Synstatin: a selective inhibitor of the syndecan-1-coupled IGF1R–αvβ3 integrin complex in tumorigenesis and angiogenesis (pages 2207–2215)

      Alan C. Rapraeger

      Version of Record online: 24 FEB 2013 | DOI: 10.1111/febs.12160

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      An extracellular docking site in the matrix receptor syndecan-1 (Sdc1) captures the αVβ3 and αVβ5 integrins along with the insulin-like growth factor 1 receptor (IGF1R), clustering and activating the receptors at sites of matrix adhesion in tumor cells and activated endothelial cells. This minireview describes this mechanism and its disruption by synstatin, a peptide mimetic of the syndecan docking site.

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      Syndecan-1 modulates β-integrin-dependent and interleukin-6-dependent functions in breast cancer cell adhesion, migration, and resistance to irradiation (pages 2216–2227)

      Hebatallah Hassan, Burkhard Greve, Mauro S. G. Pavao, Ludwig Kiesel, Sherif A. Ibrahim and Martin Götte

      Version of Record online: 31 JAN 2013 | DOI: 10.1111/febs.12111

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      The cell surface heparan sulfate proteoglycan syndecan-1 modulates breast cancer cell adhesion to fibronectin in an integrin-dependent manner, while increased cell motility in syndecan-1-deficient cells depends on both integrins and IL-6. Increased activation of FAK in the absence of Sdc-1 is associated with increased resistance to irradiation. IL-6-dependent modulation of FAK and NF- кB are inhibited by syndecan-1 depletion.

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      Innate immune signaling induces expression and shedding of the heparan sulfate proteoglycan syndecan-4 in cardiac fibroblasts and myocytes, affecting inflammation in the pressure-overloaded heart (pages 2228–2247)

      Mari E. Strand, Kate M. Herum, Zaheer A. Rana, Biljana Skrbic, Erik T. Askevold, Christen P. Dahl, Maria Vistnes, Almira Hasic, Heidi Kvaløy, Ivar Sjaastad, Cathrine R. Carlson, Theis Tønnessen, Lars Gullestad, Geir Christensen and Ida G. Lunde

      Version of Record online: 24 FEB 2013 | DOI: 10.1111/febs.12161

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      Pressure overload, an important stimulus for the highly morbid disease, heart failure, induces cardiac levels of the transmembrane heparan sulphate proteoglycan, syndecan-4. We here show that expression and shedding of the extracellular domain of syndecan-4 is regulated by innate immunity mediators in the two major cell types of the myocardium, cardiac myocytes and fibroblasts, affecting inflammation in the pressure-overloaded heart.

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      Evaluation of the coordinated actions of estrogen receptors with epidermal growth factor receptor and insulin-like growth factor receptor in the expression of cell surface heparan sulfate proteoglycans and cell motility in breast cancer cells (pages 2248–2259)

      Anastasios I. Tsonis, Nikolaos Afratis, Chrisostomi Gialeli, Maria-Ioanna Ellina, Zoi Piperigkou, Spyridon S. Skandalis, Achilleas D. Theocharis, George N. Tzanakakis and Nikos K. Karamanos

      Version of Record online: 27 FEB 2013 | DOI: 10.1111/febs.12162

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      Heparan sulfate proteoglycans have significant role in cell adhesion and migration. Exceptional importance in these functions has the E2/ERs axis coordinated by the action of EGFR and IGFR signaling cascade. Different ER status in breast cancer cells indicated the predominance either of EGFR or IGFR pathway in SDC-2, SDC-4 and GPC-1 gene expression.

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      Analysis of the fibroblast growth factor receptor (FGFR) signalling network with heparin as coreceptor: evidence for the expansion of the core FGFR signalling network (pages 2260–2270)

      Ruoyan Xu, Timothy R. Rudd, Ashley J Hughes, Giuliano Siligardi, David G. Fernig and Edwin A. Yates

      Version of Record online: 13 MAR 2013 | DOI: 10.1111/febs.12201

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      Analysis of the signalling abilities of combinations of fibroblast growth factor (FGF) subfamilies 1–9 with FGF receptors and heparin co-receptor, revealed a core network of four FGF receptors. An ancient three membered network was evident, which evolved to four members at the divergence of FGF-21, -4 and -9 from the FGF-8 subfamily, increasing four-fold the available signaling options.

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      Endorepellin laminin-like globular 1/2 domains bind Ig3–5 of vascular endothelial growth factor (VEGF) receptor 2 and block pro-angiogenic signaling by VEGFA in endothelial cells (pages 2271–2284)

      Chris D. Willis, Chiara Poluzzi, Maurizio Mongiat and Renato V. Iozzo

      Version of Record online: 28 FEB 2013 | DOI: 10.1111/febs.12164

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      We investigated the mechanism of endorepellin dual receptor antagonism and block of angiogenesis. Endorepellin LG1/2 domains bind VEGFR2 and cause receptor downregulation and inhibition of VEGFA transcription. LG3 binds to α2β1 integrin and causes SHP-1 activation, dephosphorylation of VEGFR2 at Tyr1175, and collapse of the actin cytoskeleton. Additionally, endorepellin evokes dual receptor internalization and degradation via caveosomes.

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      Isolation of bovine corneal keratan sulfate and its growth factor and morphogen binding (pages 2285–2293)

      Amanda Weyers, Bo Yang, Kemal Solakyildirim, Vienna Yee, Lingyun Li, Fuming Zhang and Robert J. Linhardt

      Version of Record online: 28 FEB 2013 | DOI: 10.1111/febs.12165

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      Keratan sulfate prepared in multi-milligram quantities from bovine cornea was structurally characterized by nuclear magnetic resonance spectroscopy and mass spectrometry and the binding of fibroblast growth factors and morphogens was studied using surface plasmon resonance.

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      The heparanase/syndecan-1 axis in cancer: mechanisms and therapies (pages 2294–2306)

      Vishnu C. Ramani, Anurag Purushothaman, Mark D. Stewart, Camilla A. Thompson, Israel Vlodavsky, Jessie L-S. Au and Ralph D. Sanderson

      Version of Record online: 4 MAR 2013 | DOI: 10.1111/febs.12168

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      Levels of the heparan sulfate proteoglycan syndecan-1 and the heparan sulfate degrading enzyme heparanase are elevated in many cancers. Together these two molecules form a powerful axis that promotes an aggressive tumor phenotype. This review focuses on the mechanism of action of the heparanase/syndecan-1 axis and emerging therapeutic strategies to target this axis.

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      Heparanase in inflammation and inflammation-associated cancer (pages 2307–2319)

      Amichay Meirovitz, Rachel Goldberg, Adi Binder, Ariel M. Rubinstein, Esther Hermano and Michael Elkin

      Version of Record online: 4 MAR 2013 | DOI: 10.1111/febs.12184

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      Heparanase, the sole mammalian endoglycosidase capable of cleaving heparan sulfate, is mechanistically involved in both malignancy and inflammation. Specific effects of heparanase in cancer development, particularly when inflammation is a causal factor, merit further systematic analysis and searching for the effective heparanase-inhibiting strategies, toward future translation to the clinical setting.

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      Mapping of matrix metalloproteinase cleavage sites on syndecan-1 and syndecan-4 ectodomains (pages 2320–2331)

      Tina Manon-Jensen, Hinke A. B. Multhaupt and John R. Couchman

      Version of Record online: 4 MAR 2013 | DOI: 10.1111/febs.12174

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      Syndecans are transmembrane signalling proteoglycans whose glycosaminoglycan chains and core proteins regulate cell behaviour. Syndecan ectodomains are shed from cell surfaces by several classes of enzymes, notably metalloproteinases, but the sites and significance of cleavage remain poorly known. We have mapped multiple cleavage sites for several tumour-associated metalloproteinases in syndecan-1 and -4 ectodomains and identify sub-domains of high proteinase sensitivity.

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      Functional interactions between matrix metalloproteinases and glycosaminoglycans (pages 2332–2341)

      Autumn Tocchi and William C. Parks

      Version of Record online: 8 MAR 2013 | DOI: 10.1111/febs.12198

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      Although matrix metalloproteinases (MMP) can cleave many proteins in vitro, in vivo individual MMPs act on just a few substrates. The limited functions of MMPs imply that mechanisms evolved to specify proteinase/substrate interactions. We discuss that glycosaminoglycans function as allosteric effectors directing MMPs to specific substrates and how understanding these interactions can provide a means to block deleterious MMP-mediated processes.

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      Cell-surface serglycin promotes adhesion of myeloma cells to collagen type I and affects the expression of matrix metalloproteinases (pages 2342–2352)

      Antonis Skliris, Vassiliki T. Labropoulou, Dionysios J. Papachristou, Alexios Aletras, Nikos K. Karamanos and Achilleas D. Theocharis

      Version of Record online: 1 MAR 2013 | DOI: 10.1111/febs.12179

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      Serglycin is a major proteoglycan synthesized by myeloma cells that interacts with collagen type I (Col I). Serglycin is localized on the cell surface in some myeloma cells and promotes their adhesion to Col I. The interaction of myeloma cells with Col I through cell-surface associated serglycin affects the expression of MMP-9 and MMP-2, which are highly expressed by myeloma cells in vivo.

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      Decorin induces rapid secretion of thrombospondin-1 in basal breast carcinoma cells via inhibition of Ras homolog gene family, member A/Rho-associated coiled-coil containing protein kinase 1 (pages 2353–2368)

      Thomas Neill, Holly R. Jones, Zoe Crane-Smith, Rick T. Owens, Liliana Schaefer and Renato V. Iozzo

      Version of Record online: 15 FEB 2013 | DOI: 10.1111/febs.12148

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      Upon engaging EGFR, decorin induces transient receptor activation leading to RhoA degradation via the 26S proteasome. This precludes RhoA from stimulating the inhibitory properties of ROCK1 on thrombospondin-1 (TSP-1). Thus, in the presence of decorin, ROCK1 no longer suppresses TSP-1 secretion; hence, there is enhanced movement of TSP-1-containing vesicles to the cell surface for its secretion and consequent angiogenesis inhibition.

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      Lumican effects in the control of tumour progression and their links with metalloproteinases and integrins (pages 2369–2381)

      Stéphane Brézillon, Katarzyna Pietraszek, François-Xavier Maquart and Yanusz Wegrowski

      Version of Record online: 18 MAR 2013 | DOI: 10.1111/febs.12210

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      Lumican is present in extracellular matrices in more or less glycanated forms. Apart from its role in the control of fibrillogenesis it also reacts with cell receptors or ligands to modulate the phenomena dealing with growth, migration, apoptosis or inflammation. This review summarizes recent data concerning lumican control of tumour progression and more particularly its interactions with metalloproteinases and integrins.

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      Lumican is increased in experimental and clinical heart failure, and its production by cardiac fibroblasts is induced by mechanical and proinflammatory stimuli (pages 2382–2398)

      Kristin V. T. Engebretsen, Ida G. Lunde, Mari E. Strand, Anne Waehre, Ivar Sjaastad, Henriette S. Marstein, Biljana Skrbic, Christen P. Dahl, Erik T. Askevold, Geir Christensen, Johannes L. Bjørnstad and Theis Tønnessen

      Version of Record online: 2 APR 2013 | DOI: 10.1111/febs.12235

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      Lumican was increased in the failing heart of mice and men. In vitro cyclic mechanical stretch and inflammation induced lumican expression and protein secretion from cardiac fibroblasts. Moreover, increased lumican in cardiac fibroblasts induced expression of molecules important for cardiac remodeling and fibrosis, suggesting a role for lumican in heart failure development.

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      Proteoglycans and their roles in brain cancer (pages 2399–2417)

      Anna Wade, Aaron E. Robinson, Jane R. Engler, Claudia Petritsch, C. David James and Joanna J. Phillips

      Version of Record online: 6 FEB 2013 | DOI: 10.1111/febs.12109

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      Glioblastoma (GBM) is characterized by abnormal activation of receptor tyrosine kinase signaling pathways and a poor prognosis. In cancer, extracellular proteoglycans help regulate oncogenic signaling and tumor cell invasion via extracellular interactions with ligands, receptors, and extracellular matrix components, and intracellular interactions with enzymes and structural proteins. We propose that proteoglycan alterations promote GBM progression and represent promising therapeutic targets.

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      New insights into the pathobiology of Down syndrome – hyaluronan synthase-2 overexpression is regulated by collagen VI α2 chain (pages 2418–2430)

      Evgenia Karousou, Xanthi Stachtea, Paola Moretto, Manuela Viola, Davide Vigetti, Maria Luisa D'Angelo, Luigi Raio, Fabio Ghezzi, Francesco Pallotti, Giancarlo De Luca, Nikos K. Karamanos and Alberto Passi

      Version of Record online: 28 MAR 2013 | DOI: 10.1111/febs.12220

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      The umbilical cord of Down Syndrome-affected fetuses is characterized by an increased content of hyaluronan and collagen type VI. The over expression of COL6A2 gene, located on chromosome 21, is probably the result of the gene dosage effect and is closely related to the increased expression of hyaluronan synthase-2 (HAS2) and consequently the augmented hyaluronan amount.

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      Biological functions of iduronic acid in chondroitin/dermatan sulfate (pages 2431–2446)

      Martin A. Thelin, Barbara Bartolini, Jakob Axelsson, Renata Gustafsson, Emil Tykesson, Edgar Pera, Åke Oldberg, Marco Maccarana and Anders Malmstrom

      Version of Record online: 28 MAR 2013 | DOI: 10.1111/febs.12214

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      The presence of iduronic acid in chondroitin/dermatan sulfate is important for multiple cellular properties such as migration, proliferation, differentiation, angiogenesis and regulation of cytokine/growth factor activities. Dermatan sulfate epimerase 1 and 2 and 4-O-sulfotransferase 1 are the dermatan biosynthetic enzymes whose roles in normal and pathophysiological situations are described in the review.

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      Comparative glycomics of leukocyte glycosaminoglycans (pages 2447–2461)

      Chun Shao, Xiaofeng Shi, Mitchell White, Yu Huang, Kevan Hartshorn and Joseph Zaia

      Version of Record online: 2 APR 2013 | DOI: 10.1111/febs.12231

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      We report cell type specific heparan sulfate (HS) and chondroitin sulfate (CS) expression in healthy human leukocyte populations. In addition, HS chains with level of sulfation similar to heparin were observed in leukocyte populations, especially in T cells. This information will be of great value for subsequent inquiry into disease states.

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      Glycosaminoglycans are functional ligands for receptor for advanced glycation end-products in tumors (pages 2462–2470)

      Shuji Mizumoto and Kazuyuki Sugahara

      Version of Record online: 24 FEB 2013 | DOI: 10.1111/febs.12156

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      Glycosaminoglycans attached to proteoglycans at the surface of tumor cells play key roles in malignant transformation and metastasis. Receptor for advanced glycation end-products (RAGE) expressed in lung was identified as a functional receptor for glycosaminoglycans expressed at the tumor cell surface. Hence, RAGE and glycosaminoglycans are potential targets of drug discovery for pulmonary metastasis.

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      Glypican-3: a marker and a therapeutic target in hepatocellular carcinoma (pages 2471–2476)

      Jorge Filmus and Mariana Capurro

      Version of Record online: 31 JAN 2013 | DOI: 10.1111/febs.12126

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      Glypican-3 (GPC3) is expressed by most hepatocellular carcinomas (HCCs), but it is not detected in normal liver or benign liver disease. Consequently, immunostaining of liver biopsies for GPC3 is currently being used by clinical pathologists to confirm HCC diagnosis. Two therapeutic approaches for HCC that target GPC3 are currently being tested in phase II clinical trials.

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      Imatinib as a key inhibitor of the platelet-derived growth factor receptor mediated expression of cell surface heparan sulfate proteoglycans and functional properties of breast cancer cells (pages 2477–2489)

      Christina J. Malavaki, Andreas E. Roussidis, Chrisostomi Gialeli, Dimitris Kletsas, Theodore Tsegenidis, Achileas D. Theocharis, George N. Tzanakakis and Nikos K. Karamanos

      Version of Record online: 27 FEB 2013 | DOI: 10.1111/febs.12163

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      PDGF/PDGF-R-mediated signaling axis is highly associated with cancer progression. The regulatory role of PDGF-R in breast cancer is highlighted as imatinib, a specific PDGF-tyrosine kinase inhibitor, exerts an inhibitory effect on cancer cell proliferation, invasion and migration as well as HS-proteoglycans expression. Imatinib may be of a potential therapeutic usefulness in breast cancer regimes.

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      Recombinant production of proteoglycans and their bioactive domains (pages 2490–2510)

      Megan S. Lord and John M. Whitelock

      Version of Record online: 18 MAR 2013 | DOI: 10.1111/febs.12197

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      Proteoglycans (PGs) are ubiquitous dynamic molecules composed of a protein core to which glycosaminoglycans have been covalently coupled. They have roles in many biological and pathological processes. This review of the literature describes the recombinant expression of PGs present in the extracellular, cell surface and intracellular environments with an emphasis on how their structures relate to their biological function.

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      Neoproteoglycans in tissue engineering (pages 2511–2522)

      Amanda Weyers and Robert J. Linhardt

      Version of Record online: 7 MAR 2013 | DOI: 10.1111/febs.12187

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      Neoproteoglycans are synthetic glycoconjugates prepared by covalently attaching a glycosaminoglycan chain to a core composed of a nanomaterial, protein, or polymer. The covalent attachment can be made to the reducing end (natural configuration), non-reducing end, or center of the chain. Neoproteoglycans might have applications in tissue engineering applications.

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      Neutralizing the anticoagulant activity of ultra-low-molecular-weight heparins using N-acetylglucosamine 6-sulfatase (pages 2523–2532)

      Xianxuan Zhou, Lingyun Li, Robert J. Linhardt and Jian Liu

      Version of Record online: 6 MAR 2013 | DOI: 10.1111/febs.12169

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      Ultra-low molecular weight heparin (ULMWH) is a clinically used anticoagulant drug. Here, we demonstrate that N-acetylglucosamine 6-sulfatase can eliminate the anti-Xa activity of ULMWH construct 1(ULMWH1) and fondaparinux by hydrolyzing the 6-O-sulfo groups at the non-reducing end of the compounds. This discovery offers a method to neutralize the anticoagulant activity of ULMWHs.

  4. Author index

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Author index (page 2533)

      Version of Record online: 9 MAY 2013 | DOI: 10.1111/j.1742-4658.2013.08777.x

  5. Table of Contents

    1. Top of page
    2. Front Cover
    3. Editorial Information
    4. Special Issue
    5. Author index
    6. Table of Contents
    1. You have free access to this content
      Table of Contents (page 2534)

      Version of Record online: 9 MAY 2013 | DOI: 10.1111/febs.12306

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