Syndecan 2

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 8061 Experts worldwide ranked by ideXlab platform

Inn-oc Han - One of the best experts on this subject based on the ideXlab platform.

  • A Unique Phenylalanine in the Transmembrane Domain Strengthens Homodimerization of the Syndecan-2 Transmembrane Domain and Functionally Regulates Syndecan-2
    The Journal of biological chemistry, 2015
    Co-Authors: Mi Jung Kwon, Youngsil Choi, Ji Hye Yun, Weontae Lee, Inn-oc Han
    Abstract:

    Abstract The Syndecans are a type of cell surface adhesion receptor that initiates intracellular signaling events through receptor clustering mediated by their highly conserved transmembrane domains (TMDs). However, the exact function of the Syndecan TMD is not yet fully understood. Here, we investigated the specific regulatory role of the Syndecan-2 TMD. We found that Syndecan-2 mutants in which the TMD had been replaced with that of Syndecan-4 were defective in Syndecan-2-mediated functions, suggesting that the TMD of Syndecan-2 plays one or more specific roles. Interestingly, Syndecan-2 has a stronger tendency to form sodium dodecyl sulfate (SDS)-resistant homodimers than Syndecan-4. Our structural studies showed that a unique phenylalanine residue (Phe167) enables an additional molecular interaction between the TMDs of the Syndecan-2 homodimer. The presence of Phe167 was correlated with a higher tendency toward oligomerization, and its replacement with isoleucine significantly reduced the SDS-resistant dimer formation and cellular functions of Syndecan-2 (e.g., cell migration). Conversely, replacement of isoleucine with phenylalanine at this position in the Syndecan-4 TMD rescued the defects observed in a mutant Syndecan-2 harboring the Syndecan-4 TMD. Taken together, these data suggest that Phe167 in the TMD of Syndecan-2 endows the protein with specific functions. Our work offers new insights into the signaling mediated by the TMD of Syndecan family members.

  • Syndecan 2 regulates melanin synthesis via protein kinase c βii mediated tyrosinase activation
    Pigment Cell & Melanoma Research, 2014
    Co-Authors: Hyejung Jung, Heesung Chung, Inn-oc Han, Sung Eun Chang, Sora Choi, Duk-hee Kang
    Abstract:

    Summary Syndecan-2, a transmembrane heparan sulfate proteoglycan that is highly expressed in melanoma cells, regulates melanoma cell functions (e.g. migration). Since melanoma is a malignant tumor of melanocytes, which largely function to synthesize melanin, we investigated the possible involvement of Syndecan-2 in melanogenesis. Syndecan-2 expression was increased in human skin melanoma tissues compared with normal skin. In both mouse and human melanoma cells, siRNA-mediated knockdown of Syndecan-2 was associated with reduced melanin synthesis, whereas overexpression of Syndecan-2 increased melanin synthesis. Similar effects were also detected in human primary epidermal melanocytes. Syndecan-2 expression did not affect the expression of tyrosinase, a key enzyme in melanin synthesis, but instead enhanced the enzymatic activity of tyrosinase by increasing the membrane and melanosome localization of its regulator, protein kinase CβII. Furthermore, UVB caused increased Syndecan-2 expression, and this up-regulation of Syndecan-2 was required for UVB-induced melanin synthesis. Taken together, these data suggest that Syndecan-2 regulates melanin synthesis and could be a potential therapeutic target for treating melanin-associated diseases.

  • Syndecan‐2 regulates melanin synthesis via protein kinase C βII‐mediated tyrosinase activation
    Pigment cell & melanoma research, 2014
    Co-Authors: Hyejung Jung, Heesung Chung, Inn-oc Han, Sung Eun Chang, Sora Choi, Duk-hee Kang
    Abstract:

    Summary Syndecan-2, a transmembrane heparan sulfate proteoglycan that is highly expressed in melanoma cells, regulates melanoma cell functions (e.g. migration). Since melanoma is a malignant tumor of melanocytes, which largely function to synthesize melanin, we investigated the possible involvement of Syndecan-2 in melanogenesis. Syndecan-2 expression was increased in human skin melanoma tissues compared with normal skin. In both mouse and human melanoma cells, siRNA-mediated knockdown of Syndecan-2 was associated with reduced melanin synthesis, whereas overexpression of Syndecan-2 increased melanin synthesis. Similar effects were also detected in human primary epidermal melanocytes. Syndecan-2 expression did not affect the expression of tyrosinase, a key enzyme in melanin synthesis, but instead enhanced the enzymatic activity of tyrosinase by increasing the membrane and melanosome localization of its regulator, protein kinase CβII. Furthermore, UVB caused increased Syndecan-2 expression, and this up-regulation of Syndecan-2 was required for UVB-induced melanin synthesis. Taken together, these data suggest that Syndecan-2 regulates melanin synthesis and could be a potential therapeutic target for treating melanin-associated diseases.

  • The extracellular domain of Syndecan-2 regulates the interaction of HCT116 human colon carcinoma cells with fibronectin
    Biochemical and biophysical research communications, 2013
    Co-Authors: Mi Jung Kwon, Youngsil Choi, Inn-oc Han, Yeonhee Kim, Sohyun Kim, Sungsu Park, Duk-hee Kang
    Abstract:

    The cell surface heparan sulfate proteoglycan, Syndecan-2, is known to play an important role in the tumorigenic activity of colon cancer cells, but the function of its extracellular domain is not yet clear. Cell spreading assays showed that HCT116 human colon cancer cells attached and spread better on fibronectin compared to the other tested extracellular matrixes (ECMs). Notably, Syndecan-2 overexpression enhanced the spreading of HCT116 cells on fibronectin, and the opposite effects were observed when Syndecan-2 expression was reduced. In addition, an oligomerization-defective Syndecan-2 mutant failed to increase cell–ECM interactions and adhesion-related Syndecan-2 functions, including migration. Furthermore, analyses using a microfabricated post array detector system revealed that Syndecan-2, but not the oligomerization-defective mutant, enhanced the interaction affinity of HCT116 cells on fibronectin. Taken together, these results suggest that the extracellular domain of Syndecan-2 regulates the interaction of HCT116 human colon carcinoma cells with fibronectin.

  • The matrix metalloproteinase-7 regulates the extracellular shedding of Syndecan-2 from colon cancer cells.
    Biochemical and biophysical research communications, 2011
    Co-Authors: Sojoong Choi, Jin Yung Kim, Jun Hyoung Park, Seung Teak Lee, Inn-oc Han
    Abstract:

    The cell surface heparan sulfate proteoglycan Syndecan-2 regulates the activation of matrix metalloproteinase-7 (MMP-7) as a docking receptor. Here, we demonstrate the role of MMP-7 on Syndecan-2 shedding in colon cancer cells. Western blot analysis showed that shed Syndecan-2 was found in the culture media from various colon cancer cells. Overexpression of MMP-7 enhanced Syndecan-2 shedding, whereas the opposite was true when MMP-7 levels were knocked-down using small inhibitory RNAs. Consistently, HT29 cells treated with MMP-7, but neither MMP-2 nor MMP-9, showed increased shed Syndecan-2 in a time- and concentration-dependent manner. Furthermore, MALDI-TOF MS analysis and N-terminal amino acid sequencing revealed that MMP-7 cleaved both recombinant Syndecan-2 and an endogenously glycosylated Syndecan-2 ectodomain in the N-terminus at Leu(149) residue in vitro. Taken together, the data suggest that MMP-7 directly mediates shedding of Syndecan-2 from colon cancer cells.

Senén Vilaró - One of the best experts on this subject based on the ideXlab platform.

  • Syndecan-2 downregulation impairs angiogenesis in human microvascular endothelial cells.
    Experimental cell research, 2008
    Co-Authors: Oriol Noguer, Senén Vilaró, Joan Villena, Jordi Lorita, Manuel Reina
    Abstract:

    The formation of new blood vessels, or angiogenesis, is a necessary process during development but also for tumour growth and other pathologies. It is promoted by different growth factors that stimulate endothelial cells to proliferate, migrate, and generate new tubular structures. Syndecans, transmembrane heparan sulphate proteoglycans, bind such growth factors through their glycosaminoglycan chains and could transduce the signal to the cytoskeleton, thus regulating cell behaviour. We demonstrated that Syndecan-2, the major Syndecan expressed by human microvascular endothelial cells, is regulated by growth factors and extracellular matrix proteins, in both bidimensional and tridimensional culture conditions. The role of Syndecan-2 in "in vitro" tumour angiogenesis was also examined by inhibiting its core protein expression with antisense phosphorothioate oligonucleotides. Downregulation of Syndecan-2 reduces spreading and adhesion of endothelial cells, enhances their migration, but also impairs the formation of capillary-like structures. These results suggest that Syndecan-2 has an important function in some of the necessary steps that make up the angiogenic process. We therefore propose a pivotal role of this heparan sulphate proteoglycan in the formation of new blood vessels.

  • Syndecan-2 expression increases serum-withdrawal-induced apoptosis, mediated by re-distribution of Fas into lipid rafts, in stably transfected Swiss 3T3 cells.
    Apoptosis : an international journal on programmed cell death, 2006
    Co-Authors: Joan Villena, Francesc Granés, Manuel Reina, Oriol Noguer, Jèssica Mainez, Héctor Contreras, Isabel Fabregat, Senén Vilaró
    Abstract:

    To examine the function of Syndecan-2, one of the most abundant heparan sulfate proteoglycans in fibroblasts, we obtained stably transfected Swiss 3T3 clones. We examined the effects of stable Syndecan-2 overexpression on programmed cell death, finding that Syndecan-2 transfected cells were more sensitive to apoptosis induced by serum-withdrawal than control cells. In addition, overexpression of Syndecan-2 correlates with increased membrane levels of the Fas/CD95 receptor, suggesting that the increased serum-withdrawal apoptosis observed in Swiss 3T3 cells might be Fas receptor-dependent. Differences in Fas membrane levels between both control and Syndecan-2 transfected cells result from a redistribution of the Fas receptor. Our data clearly demonstrate that increased Fas levels are primarily related to lipid rafts and that this increase is a key factor in Fas/CD95-mediated apoptosis. Moreover, disruption of lipid rafts with methyl-beta-cyclodextrin or filipin significantly reduced apoptosis in response to serum withdrawal. The differences in Fas/CD95 membrane distribution could explain why Syndecan-2 transfected cells have a higher susceptibility to serum-withdrawal-induced apoptosis.

  • Identification of a novel Ezrin-binding site in Syndecan-2 cytoplasmic domain.
    FEBS letters, 2003
    Co-Authors: Francesc Granés, Manuel Reina, Christine Berndt, Christian Roy, Paul Mangeat, Senén Vilaró
    Abstract:

    ERM (Ezrin/Radixin/Moesin) proteins are crosslinkers between plasma membrane proteins and the actin cytoskeleton, thereby involved in the formation of cell adhesion sites. Earlier work showed that Ezrin links Syndecan-2 to the actin cytoskeleton. Here we provide evidence that the Ezrin N-terminal domain binds to the Syndecan-2 cytoplasmic domain with an estimated K(D) of 0.71 microM and without the requirement of other proteins. We also studied the regions in the Syndecan-2 cytoplasmic domain implicated in the binding to Ezrin. By truncating the Syndecan-2 cytoplasmic domain and by oligopeptide competition assays we show that the Ezrin-binding sequence is not located in the positively charged juxtamembrane region (RMRKK), but in the neighboring sequence DEGSYD. We therefore conclude that the consensus sequence for Ezrin binding is unique among membrane proteins, suggesting a distinct regulation.

  • Syndecan-2 expression enhances adhesion and proliferation of stably transfected Swiss 3T3 cells
    Cell biology international, 2003
    Co-Authors: Joan Villena, Francesc Granés, Manuel Reina, Christine Berndt, Senén Vilaró
    Abstract:

    Abstract Syndecans (heparan sulfate proteoglycans) participate in cell–cell and cell–matrix adhesion and are co- and low-affinity receptors for growth factors and enzymes, respectively. We examined the influence of stable Syndecan-2 expression in Swiss 3T3 cells on cell-adhesion and proliferation. Higher Syndecan-2 expression changed cell morphology and increased spreading and adhesion in these cells and proliferation induced by FCS and FGF-2. This emphasizes the role of Syndecan-2 in the integration of signals from soluble and insoluble factors.

  • Syndecan-2 expression in colorectal cancer-derived HT-29 M6 epithelial cells induces a migratory phenotype.
    Biochemical and biophysical research communications, 2001
    Co-Authors: H.r. Contreras, Francesc Granés, Ricardo P. Casaroli-marano, Manuel Reina, Nativitat Rocamora, Myriam Fabre, A García De Herreros, Senén Vilaró
    Abstract:

    Members of the heparan sulfate proteoglycan family, the Syndecans have emerged as integrators of extracellular signals, such as ECM components or growth factors, that activate cytoplasmic signaling cascades and regulate cytoskeletal functions. Specifically, Syndecan-2 has been implicated in various cellular processes, from differentiation to migration, including its participation in cell-cell and cell-matrix adhesion. Here, we focused on the involvement of Syndecan-2 in epithelial versus mesenchymal differentiation. Colorectal cancer-derived HT-29 M6 epithelial cells were stably transfected with full-length Syndecan-2 cDNA, and the effect on cell morphology, adhesion, and mobility was evaluated. Characteristic features of migratory cells such as loss of intercellular contacts, flatter shape and multiple membrane projections were observed in Syndecan-2 transfectants. Western blot analysis of the major component of epithelial adherens junctions, E-cadherin, revealed decreased expression levels. Furthermore, Syndecan-2 induced stronger adhesion to collagen type I, specifically inhibited by heparin. This was correlated with an increased ability for migration, as demonstrated by wound healing experiments and transwell assays, without affecting their growth rate. These results indicate that Syndecan-2 expression in mucus-secreting HT-29 M6 cells induces differentiation toward a migratory mesenchymal-like phenotype.

Anne Woods - One of the best experts on this subject based on the ideXlab platform.

  • Syndecan 2 regulates transforming growth factor β signaling
    Journal of Biological Chemistry, 2004
    Co-Authors: Ligong Chen, Carmen M. Klass, Anne Woods
    Abstract:

    Transforming growth factor-β (TGF-β) has multiple functions including increasing extracellular matrix deposition in fibrosis. It functions through a complex family of cell surface receptors that mediate downstream signaling. We report here that a transmembrane heparan sulfate proteoglycan, Syndecan-2 (S2), can regulate TGF-β signaling. S2 protein increased in the renal interstitium in diabetes and regulated TGF-β-mediated increased matrix deposition in vitro. Transfection of renal papillary fibroblasts with S2 or a S2 construct that has a truncated cytoplasmic domain (S2ΔS) promoted TGF-β binding and S2 core protein ectodomain directly bound TGF-β. Transfection with S2 increased the amounts of type I and type II TGF-β receptors (TβRI and TβRII), whereas S2ΔS was much less effective. In contrast, S2ΔS dramatically increased the level of type III TGF-β receptor (TβRIII), betaglycan, whereas S2 resulted in a decrease. Syndecan-2 specifically co-immunoprecipitated with betaglycan but not with TβRI or TβRII. This is a novel mechanism of control of TGF-β action that may be important in fibrosis.

  • Syndecan-2 Regulates Transforming Growth Factor-β Signaling *
    The Journal of biological chemistry, 2004
    Co-Authors: Ligong Chen, Carmen M. Klass, Anne Woods
    Abstract:

    Transforming growth factor-β (TGF-β) has multiple functions including increasing extracellular matrix deposition in fibrosis. It functions through a complex family of cell surface receptors that mediate downstream signaling. We report here that a transmembrane heparan sulfate proteoglycan, Syndecan-2 (S2), can regulate TGF-β signaling. S2 protein increased in the renal interstitium in diabetes and regulated TGF-β-mediated increased matrix deposition in vitro. Transfection of renal papillary fibroblasts with S2 or a S2 construct that has a truncated cytoplasmic domain (S2ΔS) promoted TGF-β binding and S2 core protein ectodomain directly bound TGF-β. Transfection with S2 increased the amounts of type I and type II TGF-β receptors (TβRI and TβRII), whereas S2ΔS was much less effective. In contrast, S2ΔS dramatically increased the level of type III TGF-β receptor (TβRIII), betaglycan, whereas S2 resulted in a decrease. Syndecan-2 specifically co-immunoprecipitated with betaglycan but not with TβRI or TβRII. This is a novel mechanism of control of TGF-β action that may be important in fibrosis.

  • Decreased Syndecan-2 expression correlates with trichostatin-A induced-morphological changes and reduced tumorigenic activity in colon carcinoma cells
    Oncogene, 2003
    Co-Authors: Yeonhee Kim, Haein Park, Ho Jeong Kwon, Inn-oc Han, Yangmi Lim, Anne Woods
    Abstract:

    The inhibition of histone deacetylase activity is known to induce morphological changes of transformed cells. In this study, we investigated the effect of the specific HDAC inhibitor, trichostatin A (TSA), on colon carcinoma cell lines. Treatment of human colorectal carcinoma cells, KM1214 and KM12SM, with TSA induced distinct morphological changes. Both cell lines, which normally piled up in layers without clear boundary, became more flattened, and formed monolayers with evident boundaries between cells, with concomitant increased actin filament organization. Cell–cell interaction was not affected much, based on expression level, membrane localization, and interaction of E-cadherin with β -catenin. In contrast, Syndecan-2 expression was dramatically reduced and it was correlated with the morphological changes of colon carcinoma cells. Consistently, downregulation of Syndecan-2 expression by antisense cDNA clearly mimicked the morphological changes in KM12SM and reduced anchorage-independent growth of colon cancer cells. All these results indicate that reduced Syndecan-2 expression correlates with TSA-induced morphological changes and reduced tumorigenic activity in colon carcinoma cells.

  • Decreased Syndecan-2 expression correlates with trichostatin-A induced-morphological changes and reduced tumorigenic activity in colon carcinoma cells.
    Oncogene, 2003
    Co-Authors: Yeonhee Kim, Haein Park, Ho Jeong Kwon, Inn-oc Han, Yangmi Lim, Anne Woods
    Abstract:

    The inhibition of histone deacetylase activity is known to induce morphological changes of transformed cells. In this study, we investigated the effect of the specific HDAC inhibitor, trichostatin A (TSA), on colon carcinoma cell lines. Treatment of human colorectal carcinoma cells, KM1214 and KM12SM, with TSA induced distinct morphological changes. Both cell lines, which normally piled up in layers without clear boundary, became more flattened, and formed monolayers with evident boundaries between cells, with concomitant increased actin filament organization. Cell-cell interaction was not affected much, based on expression level, membrane localization, and interaction of E-cadherin with beta-catenin. In contrast, Syndecan-2 expression was dramatically reduced and it was correlated with the morphological changes of colon carcinoma cells. Consistently, downregulation of Syndecan-2 expression by antisense cDNA clearly mimicked the morphological changes in KM12SM and reduced anchorage-independent growth of colon cancer cells. All these results indicate that reduced Syndecan-2 expression correlates with TSA-induced morphological changes and reduced tumorigenic activity in colon carcinoma cells.

  • Molecular characterization of chicken Syndecan-2 proteoglycan
    Biochemical Journal, 2002
    Co-Authors: Ligong Chen, John R Couchman, Jacqueline Smith, Anne Woods
    Abstract:

    A partial Syndecan-2 sequence (147 bp) was obtained from chicken embryonic fibroblast poly(A)+ RNA by reverse transcription-PCR. This partial sequence was used to produce a 5'-end-labelled probe. A chicken liver cDNA library was screened with this probe, and overlapping clones were obtained encompassing the entire cDNA of 3 kb. The open reading frame encodes a protein of 201 amino acids. The cytoplasmic domain is identical with that of mammalian Syndecan-2, and highly similar to those of Xenopus laevis and zebrafish Syndecan-2. The transmembrane domain is identical with that of mammalian and zebrafish Syndecan-2, and highly similar to that of Xenopus laevis Syndecan-2. The ectodomain is 45-62% identical with that of zebrafish, Xenopus laevis and mammalian Syndecan-2. Two coding single nucleotide polymorphisms were observed. In vitro transcription and translation yielded a product of 30 kDa. Western blotting of chicken embryonic fibroblast cell lysates with species-specific monoclonal antibody mAb 8.1 showed that chicken Syndecan-2 is substituted with heparan sulphate, and that the major form of chicken Syndecan-2 isolated from chicken fibroblasts is consistent with the formation of SDS-resistant dimers, which is common for Syndecans. A 5'-end-labelled probe hybridized to two mRNA species in chicken embryonic fibroblasts, while Northern analysis with poly(A)+ RNAs from different tissues of chicken embryos showed wide and distinct distributions of chicken Syndecan-2 during embryonic development. This pattern was different from that reported for Syndecan-4, but consistent with the roles of Syndecan-2 in neural maturation and in mesenchymal-matrix interactions.

Manuel Reina - One of the best experts on this subject based on the ideXlab platform.

  • The PDZ-binding domain of Syndecan-2 inhibits LFA-1 high-affinity conformation
    Cellular signalling, 2014
    Co-Authors: Xavier Rovira-clavé, Manuel Reina, Maria Angulo-ibáñez, Enric Espel
    Abstract:

    Syndecans are cell membrane proteoglycans that can modulate the activity and dynamics of some growth factor receptors and integrins. Here, we show the down-regulation of integrin lymphocyte function-associated antigen-1 (LFA-1) and inhibition of adhesion of Jurkat T cells transfected with Syndecan-2. The PDZ-binding domain in the cytoplasmic region of Syndecan-2 was necessary to block the LFA-1 high-affinity conformation, and to reduce cellular adhesion. A second cytoplasmic motif comprising tyrosines 179 and 191, and serines 187 and 188 contributed also to reduce LFA-1 function and cellular adhesion. Inhibition of the LFA-1 high-affinity conformation by Syndecan-2 was independent of the expression of the talin head domain and RhoA, Rac1 and Cdc42 GTPases. These results demonstrate the importance of PDZ-binding domain of Syndecan-2 for controlling LFA-1 affinity and cell adhesion.

  • Syndecan 2 can promote clearance of t cell receptor cd3 from the cell surface
    Immunology, 2012
    Co-Authors: Xavier Roviraclave, Enric Espel, Oriol Noguer, Maria Anguloibanez, Manuel Reina
    Abstract:

    T cells express the heparan sulphate proteoglycans Syndecan-2 and Syndecan-4. Syndecan-4 plays a T-cell inhibitory role; however, the function of Syndecan-2 is unknown. In an attempt to examine this function, Syndecan-2 was expressed constitutively in Jurkat T cells. Interestingly, the expression of Syndecan-2 decreased the surface levels of T-cell receptor (TCR)/CD3 complex, concomitant with intracellular retention of CD3e and partial degradation of the TCR-ζ chain. Immunofluorescence microscopy revealed that intracellular CD3e co-located with Rab-4 endosomes. However, the intracellular pool of CD3e did not recycle to the cell surface. The lower TCR/CD3 surface levels caused by Syndecan-2 led to reduced TCR/CD3 responsiveness. We show that the cytosolic PDZ-binding domain of Syndecan-2 is not necessary to elicit TCR/CD3 down-regulation. These results identify a previously unrecognized means of controlling surface TCR/CD3 expression by Syndecan-2.

  • Syndecan-2 can promote clearance of T-cell receptor/CD3 from the cell surface.
    Immunology, 2012
    Co-Authors: Xavier Rovira-clavé, Maria Angulo-ibáñez, Oriol Noguer, Enric Espel, Manuel Reina
    Abstract:

    T cells express the heparan sulphate proteoglycans Syndecan-2 and Syndecan-4. Syndecan-4 plays a T-cell inhibitory role; however, the function of Syndecan-2 is unknown. In an attempt to examine this function, Syndecan-2 was expressed constitutively in Jurkat T cells. Interestingly, the expression of Syndecan-2 decreased the surface levels of T-cell receptor (TCR)/CD3 complex, concomitant with intracellular retention of CD3e and partial degradation of the TCR-ζ chain. Immunofluorescence microscopy revealed that intracellular CD3e co-located with Rab-4 endosomes. However, the intracellular pool of CD3e did not recycle to the cell surface. The lower TCR/CD3 surface levels caused by Syndecan-2 led to reduced TCR/CD3 responsiveness. We show that the cytosolic PDZ-binding domain of Syndecan-2 is not necessary to elicit TCR/CD3 down-regulation. These results identify a previously unrecognized means of controlling surface TCR/CD3 expression by Syndecan-2.

  • Corrigendum to “Syndecan-2 and -4 expressed on activated primary human CD4+ lymphocytes can regulate T cell activation” [Mol. Immunol. 45 (10) (2008) 2905–2919]
    Molecular Immunology, 2012
    Co-Authors: Trini Teixé, Manuel Reina, Patricia Nieto-blanco, Ramon Vilella, Pablo Engel, Enric Espel
    Abstract:

    The author regrets that in the above published paper the following error occurred:In Fig. 3 of the paper cited above, trace amounts of protein A in the affinity chromatography-purified anti-Syndecan-2 mAb 186C(protein Awhichleachedfromtheaffinityresin),whosepresencewentunnoticed,interferedwiththeanti-CD3 mAb(mouseIgG2a)usedto stimulate the T cells. Based on the original results we suggested that Syndecan-2 could have an inhibitory effect on T cells. However, re-evaluation ofsimilarexperimentswithproteinA-freeanti-Syndecan-2mAb186CindicatesthatthemAbdoesnotinhibitT-cellproliferationor IL-2 mRNA synthesis.

  • Is Syndecan-2 a key angiogenic element?
    TheScientificWorldJournal, 2009
    Co-Authors: Oriol Noguer, Manuel Reina
    Abstract:

    Angiogenesis has been extensively related with the development of many different diseases, from tumor progression to cardiovascular disorders. In our last article, we demonstrated that Syndecan-2, the most abundant heparan sulfate proteoglycan expressed by human microvascular endothelial cells, is regulated by proangiogenic factors and plays an important role in most of the cellular events that take place in neovascularization processes. Here, we also reported its involvement in the reorganization of the cytoskeleton and propose a key role for this proteoglycan as an adaptor protein, able to work in cooperation with the integrins in the formation of new blood vessels.

Duk-hee Kang - One of the best experts on this subject based on the ideXlab platform.

  • Syndecan 2 regulates melanin synthesis via protein kinase c βii mediated tyrosinase activation
    Pigment Cell & Melanoma Research, 2014
    Co-Authors: Hyejung Jung, Heesung Chung, Inn-oc Han, Sung Eun Chang, Sora Choi, Duk-hee Kang
    Abstract:

    Summary Syndecan-2, a transmembrane heparan sulfate proteoglycan that is highly expressed in melanoma cells, regulates melanoma cell functions (e.g. migration). Since melanoma is a malignant tumor of melanocytes, which largely function to synthesize melanin, we investigated the possible involvement of Syndecan-2 in melanogenesis. Syndecan-2 expression was increased in human skin melanoma tissues compared with normal skin. In both mouse and human melanoma cells, siRNA-mediated knockdown of Syndecan-2 was associated with reduced melanin synthesis, whereas overexpression of Syndecan-2 increased melanin synthesis. Similar effects were also detected in human primary epidermal melanocytes. Syndecan-2 expression did not affect the expression of tyrosinase, a key enzyme in melanin synthesis, but instead enhanced the enzymatic activity of tyrosinase by increasing the membrane and melanosome localization of its regulator, protein kinase CβII. Furthermore, UVB caused increased Syndecan-2 expression, and this up-regulation of Syndecan-2 was required for UVB-induced melanin synthesis. Taken together, these data suggest that Syndecan-2 regulates melanin synthesis and could be a potential therapeutic target for treating melanin-associated diseases.

  • Interleukin-1α promotes extracellular shedding of Syndecan-2 via induction of matrix metalloproteinase-7 expression.
    Biochemical and biophysical research communications, 2014
    Co-Authors: Mi Jung Kwon, Youngsil Choi, Eunkyoung Hong, Duk-hee Kang
    Abstract:

    The cell surface heparan sulfate proteoglycan, Syndecan-2, is known to play an important role in the tumorigenic activity of colon cancer cells. In addition, the extracellular domain of Syndecan-2 is cleaved by matrix metalloproteinase-7 (MMP-7) in various colon cancer cells, but factors involved in regulating this process remain unknown. Here, we demonstrate a role for interleukin-1α (IL-1α) in Syndecan-2 shedding in colon cancer cells. Treatment of low metastatic (HT-29) and highly metastatic (HCT-116) colon cancer cells with various soluble growth factors and cytokines revealed that IL-1α specifically increased extracellular shedding of Syndecan-2 in a concentration- and time-dependent manner. IL-1α did not affect the expression of Syndecan-2, but did significantly reduce its cell surface levels. Notably, IL-1α increased the mRNA expression and subsequent secreted levels of MMP-7 protein and enhanced the phosphorylation of p38 and ERK mitogen-activated protein kinases. Furthermore, increased Syndecan-2 shedding was dependent on the mitogen-activated protein kinase-mediated MMP-7 expression. Taken together, these data suggest that IL-1α regulates extracellular domain shedding of Syndecan-2 through regulation of the MAP kinase-mediated MMP-7 expression in colon cancer cells.

  • Syndecan‐2 regulates melanin synthesis via protein kinase C βII‐mediated tyrosinase activation
    Pigment cell & melanoma research, 2014
    Co-Authors: Hyejung Jung, Heesung Chung, Inn-oc Han, Sung Eun Chang, Sora Choi, Duk-hee Kang
    Abstract:

    Summary Syndecan-2, a transmembrane heparan sulfate proteoglycan that is highly expressed in melanoma cells, regulates melanoma cell functions (e.g. migration). Since melanoma is a malignant tumor of melanocytes, which largely function to synthesize melanin, we investigated the possible involvement of Syndecan-2 in melanogenesis. Syndecan-2 expression was increased in human skin melanoma tissues compared with normal skin. In both mouse and human melanoma cells, siRNA-mediated knockdown of Syndecan-2 was associated with reduced melanin synthesis, whereas overexpression of Syndecan-2 increased melanin synthesis. Similar effects were also detected in human primary epidermal melanocytes. Syndecan-2 expression did not affect the expression of tyrosinase, a key enzyme in melanin synthesis, but instead enhanced the enzymatic activity of tyrosinase by increasing the membrane and melanosome localization of its regulator, protein kinase CβII. Furthermore, UVB caused increased Syndecan-2 expression, and this up-regulation of Syndecan-2 was required for UVB-induced melanin synthesis. Taken together, these data suggest that Syndecan-2 regulates melanin synthesis and could be a potential therapeutic target for treating melanin-associated diseases.

  • The extracellular domain of Syndecan-2 regulates the interaction of HCT116 human colon carcinoma cells with fibronectin
    Biochemical and biophysical research communications, 2013
    Co-Authors: Mi Jung Kwon, Youngsil Choi, Inn-oc Han, Yeonhee Kim, Sohyun Kim, Sungsu Park, Duk-hee Kang
    Abstract:

    The cell surface heparan sulfate proteoglycan, Syndecan-2, is known to play an important role in the tumorigenic activity of colon cancer cells, but the function of its extracellular domain is not yet clear. Cell spreading assays showed that HCT116 human colon cancer cells attached and spread better on fibronectin compared to the other tested extracellular matrixes (ECMs). Notably, Syndecan-2 overexpression enhanced the spreading of HCT116 cells on fibronectin, and the opposite effects were observed when Syndecan-2 expression was reduced. In addition, an oligomerization-defective Syndecan-2 mutant failed to increase cell–ECM interactions and adhesion-related Syndecan-2 functions, including migration. Furthermore, analyses using a microfabricated post array detector system revealed that Syndecan-2, but not the oligomerization-defective mutant, enhanced the interaction affinity of HCT116 cells on fibronectin. Taken together, these results suggest that the extracellular domain of Syndecan-2 regulates the interaction of HCT116 human colon carcinoma cells with fibronectin.

Related terms

Syndecan 2 - 15 days free trial to Access Experts & Abstracts