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CD63 glycosylation

Mingjia Yu, Shanjun Yang, Hongxia Sun, Qiang Xia
As one of the surface membrane proteins of tetraspanin family, CD63 plays a crucial role in cellular trafficking and endocytosis, which also is associated with activation of a wide variety of immune cells. Here, the homolog of CD63 was characterized from one marine mollusk, Paphia undulata, which is designated as Pu-CD63. The complete cDNA of Pu-CD63 is 1,738 bp in length with an open reading frame (ORF) of 849 bp, encoding a 282 amino acid protein with four putative hydrophobic transmembrane helixes. Bioinformatic analysis revealed that Pu-CD63 contains one putative YXXØ consensus motif of "110-YVII-113" and one N-glycosylation site "155-NGT-157" within the large extracellular loop (LEL) region, supporting its conserved function in plasma membrane and endosomal/lysosomal trafficking...
2016: Journal of Immunology Research
Siriwan Wansook, Supansa Pata, Watchara Kasinrerk, Panida Khunkaewla
BACKGROUND: Monoclonal antibodies (mAbs) have become essential tools in life science research and in medicine, because of their extreme specificity. Several mAbs against leukocyte surface molecules have been generated in our laboratory. From these, mAb COS3A was selected for biochemical and functional analysis. OBJECTIVE: To analyze the properties and function of the mAb COS3A. METHOD: Cellular distribution was analyzed by immunofluorescence staining and flow cytometry...
December 2016: Asian Pacific Journal of Allergy and Immunology
Zhu Han, Mingyu Lv, Ying Shi, Jinghua Yu, Junqi Niu, Xiao-Fang Yu, Wenyan Zhang
BST-2/tetherin blocks the release of various enveloped viruses including HIV-1 with a "physical tethering" model. The detailed contribution of N-linked glycosylation to this model is controversial. Here, we confirmed that mutation of glycosylation sites exerted an effect of post-translational mis-trafficking, leading to an accumulation of BST-2 at intracellular CD63-positive vesicles. BST-2 with this phenotype potently inhibited the release of multivesicular body-targeted HIV-1 and hepatitis B virus, without affecting the co-localization of BST-2 with EEA1 and LAMP1...
February 29, 2016: Viruses
Joana Gomes, Patrícia Gomes-Alves, Sofia B Carvalho, Cristina Peixoto, Paula M Alves, Peter Altevogt, Julia Costa
Cells release vesicles to the extracellular environment with characteristic nucleic acid, protein, lipid, and glycan composition. Here we have isolated and characterized extracellular vesicles (EVs) and total cell membranes (MBs) from ovarian carcinoma OVMz cells. EVs were enriched in specific markers, including Tsg101, CD63, CD9, annexin-I, and MBs contained markers of cellular membrane compartments, including calnexin, GRASP65, GS28, LAMP-1, and L1CAM. The glycoprotein galectin-3 binding protein (LGALS3BP) was strongly enriched in EVs and it contained sialylated complex N-glycans...
2015: Biomolecules
Yaxuan Liang, William S Eng, David R Colquhoun, Rhoel R Dinglasan, David R Graham, Lara K Mahal
Exosomes, also known as microvesicles (EMVs), are nano-sized membranous particles secreted from nearly all mammalian cell types. These nanoparticles play critical roles in many physiological processes including cell-cell signaling, immune activation, and suppression and are associated with disease states such as tumor progression. The biological functions of EMVs are highly dependent on their protein composition, which can dictate pathogenicity. Although some mechanisms have been proposed for the regulation of EMV protein trafficking, little attention has been paid to N-linked glycosylation as a potential sorting signal...
November 21, 2014: Journal of Biological Chemistry
Swati Gupta, Ilya Reviakine
BACKGROUND: The diversity of platelet functions implies multiple activation states arising in response to different stimuli. Distinguishing between these states has been challenging. METHODS: We used fluorescently labelled carbohydrate binding proteins lectins to investigate agonist-induced changes in platelet surface glycosylation. RESULTS: Each of the seven agonists we used caused a unique set of changes in platelet surface glycosylation, eliciting a unique functional state...
December 2014: Biochimica et Biophysica Acta
Naoomi Tominaga, Keitaro Hagiwara, Nobuyoshi Kosaka, Kimi Honma, Hitoshi Nakagama, Takahiro Ochiya
BACKGROUND: The tetraspanin CD63 is a highly N-glycosylated protein that is known to regulate cancer malignancy. However, the contribution of glycosylation of CD63 to cancer malignancy remains unclear. Previously, we reported that ribophorin II (RPN2), which is part of an N-oligosaccharyle transferase complex, is responsible for drug resistance in breast cancer cells. In this study, we demonstrate that cancer malignancy associated with the glycosylation of CD63 is regulated by RPN2. RESULTS: Inhibition of RPN2 expression led to a reduction in CD63 glycosylation...
2014: Molecular Cancer
H M Schröder, S C Hoffmann, M Hecker, T Korff, T Ludwig
The membrane-type 1 matrix metalloproteinase (MT1-MMP) drives fundamental physiological and pathophysiological processes. Among other substrates, MT1-MMP cleaves components of the extracellular matrix and activates other matrix-cleaving proteases such as MMP-2. Trafficking is a highly effective means to modulate MT1-MMP cell surface expression, and hence regulate its function. Here, we describe the complex interaction of MT1-MMP with tetraspanins, their effects on MT1-MMP intracellular trafficking and proteolytic function...
June 2013: International Journal of Biochemistry & Cell Biology
Adrian Waite, Maria Cristina De Rosa, Andrea Brancaccio, Derek J Blake
Missense mutations in the SGCE gene encoding ε-sarcoglycan account for approximately 15% of SGCE-positive cases of myoclonus-dystonia syndrome (MDS) in humans. In this study, we show that while the majority of MDS-associated missense mutants modeled with a murine ε-sarcoglycan cDNA are substrates for endoplasmic reticulum-associated degradation, one mutant, M68T (analogous to human c.275T>C, p.M92T), located in the Ig-like domain of ε-sarcoglycan, results in a gain-of-glycosylation mutation producing a protein that is targeted to the plasma membrane, albeit at reduced levels compared to wild-type ε-sarcoglycan...
November 2011: Human Mutation
Thorsten Schäfer, P Starkl, C Allard, R M Wolf, T Schweighoffer
BACKGROUND: Mast cells are secretory immune cells whose degranulation can provoke acute allergic reactions. It is presently unclear, however, whether an individual mast cell can repeatedly degranulate or turns dysfunctional after a single antigen stimulus. This work thus aims to better define the mast cell life cycle, with particular focus on new target structures for therapeutic or diagnostic approaches in allergy. METHODS: Monoclonal antibodies were raised against degranulated cord blood-derived human mast cells...
October 2010: Allergy
Ashutosh K Pathak, Birgit A Helm
Allergen-mediated cross-linking of the high-affinity receptor for IgE on mast cells triggers the release of diverse preformed and de novo synthesized immunoregulatory mediators that further the allergic response. A proteomic screen applied to the detection of proteins secreted by the model rat mast cell line, RBL-2H3 (rat basophilic leukaemia, subline 2H3.1), led to the identification of the cholesterol-binding glycoprotein, NPC2/RE1 (Niemann-Pick Type C2/epididymal secretory protein 1). Glycosylated NPC2 is secreted early in response to an IgE-mediated stimulus and co-localizes with the lysosomal membrane marker, CD63...
April 2010: Cell Biology International
Takeshi Yoshida, Hirotaka Ebina, Yoshio Koyanagi
Efficient downregulation of CXCR4 cell surface expression by introduction of the CD63 gene has previously been reported by us. In the present study, it was found that CD63 and its mutant efficiently interact with CXCR4 in live cells and that CD63-induced downregulation and interaction are significantly abrogated by the N-linked glycosylation inhibitor, TM. Furthermore, the downregulation and interaction were clearly attenuated by alternation of all three N-linked glycosylation sites in CD63. Either CD63 or CD63DeltaN formed a complex with CXCR4 at the Golgi apparatus and the late endosomes, while CD63 GD mutants lost the ability to form a complex with CXCR4 exclusively at the Golgi apparatus...
November 2009: Microbiology and Immunology
Thomas Gawlowski, Bernd Stratmann, Ruth Ruetter, Christina E Buenting, Barbara Menart, Jürgen Weiss, Helen Vlassara, Theodor Koschinsky, Diethelm Tschoepe
BACKGROUND: Diabetes mellitus is characterized by hyperglycemia that plays an important role in the pathogenesis of diabetic complications including cardiovascular diseases. Moreover, hyperglycemia induces increased generation of advanced glycation end products (AGEs). The activation of platelets is associated with the development of cardiovascular diseases. AIM OF THE STUDY: The question whether AGEs acutely induce platelet activation as a response to exogenous stimulus is addressed...
December 2009: European Journal of Nutrition
Gouri Baldwin, Vera Novitskaya, Rafal Sadej, Ewa Pochec, Anna Litynska, Christoph Hartmann, Janelle Williams, Leonie Ashman, Johannes A Eble, Fedor Berditchevski
The tetraspanin CD151 forms a stoichiometric complex with integrin alpha3beta1 and regulates its endocytosis. We observed that down-regulation of CD151 in various epithelial cell lines changed glycosylation of alpha3beta1. In contrast, glycosylation of other transmembrane proteins, including those associated with CD151 (e.g. alpha6beta1, CD82, CD63, and emmprin/CD147) was not affected. The detailed analysis has shown that depletion of CD151 resulted in the reduction of Fucalpha1-2Gal and bisecting GlcNAc-beta(1-->4) linkage on N-glycans of the alpha3 integrin subunit...
December 19, 2008: Journal of Biological Chemistry
Marcelo G Binker, Laura I Cosen-Binker, Mauricio R Terebiznik, Gustavo V Mallo, Shannon E McCaw, Eeva-Liisa Eskelinen, Marion Willenborg, John H Brumell, Paul Saftig, Sergio Grinstein, Scott D Gray-Owen
Mature, microbicidal phagosomes are rich in the lysosome-associated membrane proteins, LAMP-1 and LAMP-2, two highly glycosylated proteins presumed to form a protective barrier lining the phagosomal membrane. Pathogenic Neisseria secrete a protease that selectively cleaves LAMP-1, suggesting a critical role for LAMP proteins in the microbicidal competence of phagosomes. To determine the requirement for LAMP proteins in bacterial phagocytosis, we employed embryonic fibroblasts isolated from knockout mice lacking lamp-1, lamp-2 or both genes, as well as small interfering RNA (siRNA)-mediated knockdown of LAMP expression in a human epithelial cell line...
September 2007: Cellular Microbiology
Nahoko Ogata, Shosaku Nomura, Akira Shouzu, Masahito Imaizumi, Miwa Arichi, Miyo Matsumura
Diabetic retinopathy is associated with microvascular damage and capillary occlusions which are common features of the microangiopathy in diabetes. Monocyte-derived microparticles (MDMPs) are released from activated monocytes and enhance the procoagulant activity, and also activate adhesion reactions. These are key events in the development of capillary occlusion. The MDMPs level in the blood, and platelet activation markers (platelet-derived microparticles (PDMPs), CD62P and CD63) were measured by flow cytometry in 72 diabetic patients...
September 2006: Diabetes Research and Clinical Practice
Nahoko Ogata, Masahito Imaizumi, Shosaku Nomura, Akira Shozu, Miwa Arichi, Masato Matsuoka, Miyo Matsumura
Diabetic retinopathy is caused by capillary occlusions. Platelet-derived microparticles (PMPs) stimulate the coagulation cascade and increase leukocyte and endothelial cell adhesions, both of which are key events in the development of diabetic retinopathy. However, the correlation between the levels of PMPs and diabetic retinopathy has not been precisely determined. The PMPs levels and the expression of platelet CD62P and CD63 were measured in 92 diabetic patients. The level of PMPs was significantly correlated with the expression of CD62P (r = 0...
June 2005: Diabetes Research and Clinical Practice
Wei Chen, Jian Tang, Pamela Stanley
Factors that regulate alpha(1,3)fucosyltransferase activity are important to identify because FUT genes are up-regulated during inflammation, cancer progression, and tumor metastasis. FUT gene activation increases the expression of cell surface oncofetal antigens such as Lewis X, sialyl-Le X and VIM-2. The LEC11B gain-of-function glycosylation mutant displays these antigens and binds E-selectin because it expresses the Fut6B gene that is shown here to lie immediately downstream of the Fut6A gene. A retroviral strategy for expression cloning factors that suppress alpha(1,3)fucosylation in LEC11B cells was developed, and several cDNAs that reverted the LEC11B glycosylation phenotype were isolated...
March 2005: Glycobiology
Alicia Llorente, María C de Marco, Miguel A Alonso
MAL, BENE and MAL2 are raft-associated integral membrane proteins of the MAL family of proteins involved in membrane trafficking processes. We show here that the human prostate carcinoma PC-3 cell line expresses the transcripts for the three proteins simultaneously. MAL, BENE and MAL2 co-fractionated with caveolin-1 in the raft fraction of PC-3 cells, and immunofluorescence analysis showed colocalization of these proteins with caveolin-1 in a multivesicular intracellular compartment. Markers of the Golgi apparatus, early and recycling endosomes and lipid droplets were excluded from this compartment...
October 15, 2004: Journal of Cell Science
Zhouxun Chen, Tarek Mustafa, Bogusz Trojanowicz, Michael Brauckhoff, Oliver Gimm, Cornelia Schmutzler, Josef Köhrle, Hans-Jürgen Holzhausen, Astrid Kehlen, Thomas Klonisch, Rainer Finke, Henning Dralle, Cuong Hoang-Vu
CD82 (KAI1) and CD63 (ME491) are highly glycosylated proteins which belong to the transmembrane 4 superfamily (TM4SF). CD82 has been implicated as a possible prostate cancer metastasis suppressor gene, whereas CD63 is involved in the progression of human melanoma cancer. Down-regulation of both CD82 and CD63 expression has been associated with the metastatic potential of several solid tumors. Currently, information is lacking on the role of CD82 and CD63 during thyroid carcinogenesis. The aim of this study was to determine whether the expression of CD82 and CD63 is a useful prognostic indicator in patients with thyroid carcinoma...
October 2004: International Journal of Molecular Medicine
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