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  • 1
    Keywords: PEPTIDE ; human ; DISEASE ; SITE ; SITES ; PROTEIN ; SAMPLE ; SAMPLES ; SERA ; INDUCTION ; BINDING ; treatment ; ACID ; IDENTIFICATION ; SUBUNIT ; DIFFERENCE ; MOBILITY ; GAS ; ACUTE LYMPHOBLASTIC-LEUKEMIA ; IONIZATION ; ACETYLATED SIALIC ACIDS ; sialic acid ; VISCERAL LEISHMANIASIS ; C-REACTIVE PROTEIN ; acute-phase protein ; BINDING CHARACTERISTICS ; CATLA-CATLA ; CHROMATOGRAPHY ; ELECTROPHORESIS ; FRAGMENTS ; GLUCOSE ; glycosylation ; INDIVIDUALS ; LABEO-ROHITA ; LECTIN ; lectin binding ; LIQUID-CHROMATOGRAPHY ; MAJOR CARP ; matrix-assisted laser-desorption ionization analysis (MALDI analysis) ; molecular modelling ; protein-protein interaction ; PROTEIN-PROTEIN INTERACTIONS ; SIALIC-ACID ; SUBUNITS
    Abstract: As an acute-phase protein, human C-reactive protein (CRP) is clinically important. CRPs were purified from several samples in six different pathological conditions, where their levels ranged from 22 to 342 mug/ml. Small, but significant, variations in electrophoretic mobilities on native PAGE suggested differences in molecular mass, charge and/or shape. Following separation by 9 SDS/PAGE, the), showed single subunits with some differences in their molecular masses ranging between 27 and 30.5 kDa, but for a particular disease, the mobility was the same for CRPs purified from multiple individuals or pooled sera. Isoelectric focusing (IEF) also indicated that the purified CRPs differed from each other. Glycosylation was demonstrated in these purified CRPs by Digoxigenin kits, neuraminidase treatment and binding with lectins. The presence of N-linked sugar moiety was confirmed by N-glycosidase F digestion. The presence of sialic acid, glucose, galactose and mannose has been demonstrated by gas liquid chromatography, mass spectroscopic and fluorimetric analysis. Matrix-assisted laser-desorption ionization analysis of the tryptic digests of three CRPs showed systematic absence of two peptide fragments, one at the N-terminus and the other near the C-terminus. Model-building suggested that the loss of these fragments exposed two potential glycosylation sites on a cleft floor keeping the protein-protein interactions in pentraxins and calcium-dependent phosphorylcholine-binding qualitatively unaffected. Thus we have convincingly demonstrated that human CRP is glycosylated in some pathological conditions
    Type of Publication: Journal article published
    PubMed ID: 12693993
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  • 2
    Keywords: CELLS ; tumor ; TUMOR-CELLS ; carcinoma ; Germany ; RELEASE ; MECHANISM ; CLEAVAGE ; PRECURSOR PROTEIN ; L1 ; ADHESION MOLECULE ; ovarian carcinoma ; CD44 ; RE ; VESICLES ; OVARIAN CARCINOMAS ; CELLULAR CHOLESTEROL ; exosome ; METALLOPROTEINASE ; ectodomain shedding ; CALCIUM INFLUX ; ALPHA-CONVERTING-ENZYME ; ADAM (a disintegrin and metalloproteinase) ; DEPENDENT MECHANISM
    Abstract: Ectodomain shedding is a proteolytic mechanism by which transmembrane molecules are converted into a soluble form. Cleavage is mediated by metalloproteases and proceeds in a constitutive or inducible fashion. Although believed to be a cell-surface event, there is increasing evidence that cleavage can take place in intracellular compartments. However, it is unknown how cleaved soluble molecules get access to the extracellular space. By analysing L1 (CD171) and CD44 in ovarian carcinoma cells, we show in the present paper that the cleavage induced by ionomycin, APMA (4-aminophenylmercuric acetate) or MCD (methyl-beta-cyclodextrin) is initiated in an endosomal compartment that is subsequently released in the form of exosomes. Calcium influx augmented the release of exosomes containing functionally active forms of ADAM10 (a disintegrin and metalloprotease 10) and ADAM 17 [TACE (tumour necrosis factor alpha-converting enzyme)] as well as CD44 and L1 cytoplasmic cleavage fragments. Cleavage could also proceed in released exosomes, but only depletion of ADAM 10 by small interfering RNA blocked cleavage under constitutive and induced conditions. In contrast, cleavage of L1 in response to PMA occurred at the cell surface and was mediated by ADAM17. We conclude that different ADAMs are involved in distinct cellular compartments and that ADAM10 is responsible for shedding in vesicles. Our findings open up the possibility that exosomes serve as a platform for ectodomain shedding and as a vehicle for the cellular export of soluble molecules
    Type of Publication: Journal article published
    PubMed ID: 16229685
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  • 3
    Keywords: CELLS ; EXPRESSION ; GROWTH ; CELL ; Germany ; MODEL ; MODELS ; CLASSIFICATION ; liver ; CLONING ; GENE ; PROTEIN ; LIGAND ; animals ; TISSUES ; SKIN ; BIOLOGY ; MOLECULAR-BIOLOGY ; SEQUENCE ; antibodies ; immunohistochemistry ; PATTERNS ; PROMOTER ; REGION ; EMBRYO ; EVOLUTION ; LIGANDS ; LECTIN ; AMINO-ACID-SEQUENCE ; AFFINITY-CHROMATOGRAPHY ; molecular biology ; molecular ; RECOMBINANT ; ADULT ; PATTERN ; HOMOLOGY ; PROMOTER REGION ; animal ; Phylogeny ; ENGLAND ; 14 KDA ; DEVELOPMENTALLY REGULATED LECTIN ; GALACTOSIDE-BINDING LECTIN ; MAMMALIAN LECTINS ; nephron ; prototype chicken galectin
    Abstract: Prototype galectins are versatile modulators of cell adhesion and growth via their reactivity to certain carbohydrate and protein ligands. These functions and the galectins' marked developmental regulation explain their attractiveness as models to dissect divergent evolution after gene duplication. Only two members have so far been assumed to constitute this group in chicken, namely the embryonic muscle/liver form {C-16 or CLL-I [16 kDa; chicken lactose lectin, later named CG-16 (chicken galectin-16)]} and the embryonic skin/intestine form (CLL-II or C-14; later named CG-14). In the present study, we report on the cloning and expression of a third prototype CG. It has deceptively similar electrophoretic mobility compared with recombinant C-14, the protein first isolated from embryonic skin, and turned out to be identical with the intestinal protein. Hydrodynamic properties unusual for a homodimeric galectin and characteristic traits in the proximal promoter region set it apart from the two already known CGs. Their structural vicinity to galectin-1 prompts their classification as CG-1A (CG-16)/CG-1B (CG-14), whereas sequence similarity to mammalian galectin-2 gives reason to refer to the intestinal protein as CG-2. The expression profiling by immunohistochemistry with specific antibodies discerned nonoverlapping expression patterns for the three CGs in several organs of adult animals. Overall, the results reveal a network of three prototype galectins in chicken
    Type of Publication: Journal article published
    PubMed ID: 17887955
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  • 4
    Keywords: CELLS ; GROWTH ; INHIBITOR ; INVASION ; carcinoma ; CELL ; Germany ; human ; INHIBITION ; MODEL ; GENE ; GENE-EXPRESSION ; ACCUMULATION ; LINES ; MICE ; RELEASE ; TIME ; MECHANISM ; DOMAIN ; BINDING ; BIOLOGY ; CELL-LINES ; MOLECULE ; CLEAVAGE ; PROGRESSION ; CARCINOMA CELLS ; METASTASIS ; COLORECTAL-CANCER ; NUDE-MICE ; CELL-LINE ; CARCINOMA-CELLS ; LOCALIZATION ; CELL-ADHESION ; INTRACELLULAR DOMAIN ; MIGRATION ; L1 ; LIPID RAFTS ; TRANSLOCATION ; L1 adhesion molecule ; OVEREXPRESSION ; cell lines ; AMYLOID PRECURSOR PROTEIN ; DOMAINS ; molecular biology ; regulation ; NUCLEAR TRANSLOCATION ; cell adhesion ; raft ; signalling ; MOTILITY ; PROMOTES ; L1CAM ; lipid ; nuclear localization ; ADAM10 ; DISINTEGRIN ; 3 ; a disintegrin and metalloprotease 10 (ADAM10) ; GAMMA-SECRETASE ; L1 cell-adhesion molecule (L1-CAM) ; presenilin (PS)/gamma-secretase activity
    Abstract: L1-CAM (L1 cell-adhesion molecule), or more simply L1, plays an important role ill the progression of human carcinoma. Overexpression promotes tumour-cell invasion and motility, growth in nude mice and tumour metastasis. It is feasible that L1-dependent signalling contributes to these effects, However, little is known about its mechanism in tumour cells. We reported previously that L1 is cleaved by ADAM (a disintegrin and metalloprotease) and that the cytoplasmic part is essential for L1 function. Here we analysed more closely the role of proteolytic cleavage in L1-mediated nuclear signalling. Using OVMz carcinoma cells and L1-transfected cells as a model, we found that ADAM 10-mediated cleavage of L1 proceeds in lipid raft and non-raft domains. The cleavage product, L1-32, is further processed by PS (presenilin)/gamma-secretase to release L1-ICD, an L1 intracellular domain of 28 kDa. Overexpression of dominant-negative PSI or use of a specific gamma-secretase inhibitor leads to all accumulation of L1-32. Fluorescence and biochemical analysis revealed a nuclear localization for L1-ICD. Moreover, inhibition of ADAM10 and/or gamma-secretase blocks nuclear translocation of L1-ICD and L1-dependent gene regulation. Overexpression of recombinant L1-ICD mediates gene regulation in a similar manner to full-length L1. Our results establish for the first time that regulated proteolytic processing by ADAM10 and PS/gamma-secretase is essential for the nuclear signalling of L1 in human carcinoma cell lines
    Type of Publication: Journal article published
    PubMed ID: 19260824
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  • 5
    Keywords: CELLS ; CELL ; Germany ; IN-VIVO ; ENZYMES ; GENE-EXPRESSION ; GENOME ; PROTEIN ; PROTEINS ; DNA ; MOUSE ; ASSAY ; Drosophila ; MAMMALIAN-CELLS ; TRACT ; DE-NOVO ; HISTONE DEACETYLASE ; OVEREXPRESSION ; CYTOSINE METHYLATION ; CYTOSINE-5 METHYLTRANSFERASES ; DE-NOVO METHYLATION ; EMBRYONIC STEM-CELLS ; MAMMALIAN DEVELOPMENT ; IMMUNODEFICIENCY SYNDROME ; METHYLTRANSFERASE ; DNA methyltransferase,Dnmt1,Dnmt2,Dnmt3a,Dnmt3b,Drosophila ; ENZYMATIC-PROPERTIES ; NON-CPG METHYLATION
    Abstract: DNA methyltransferases (Dnmts) mediate the epigenetic modification of eukaryotic genomes. Mammalian DNA methylation patterns are established and maintained by co-operative interactions among the Dnmt proteins Dnmt1, Dnmt3a and Dnmt3b. Owing to their simultaneous presence in mammalian cells, the activities of individual Dnmt have not yet been determined. This includes a fourth putative Dnmt, namely Dnmt2, which has failed to reveal any activity in previous assays. We have now established transgenic Drosophila strains that allow for individual overexpression of all known mouse Dnmts. Quantitative analysis of genomic cytosine methylation levels demonstrated a robust Dural activity for the de novo methyltransferases Dnmt3a and Dnmt3b. In addition, we also detected a weak but significant activity for Dnmt2. Subsequent methylation tract analysis by genomic bisulphite sequencing revealed that Dnmt3 enzymes preferentially methylated CpG dinucleotides in a processive manner, whereas Dnmt2 methylated isolated cytosine residues in a non-CpG dinucleotide context. Our results allow a direct comparison of the activities of mammalian Dnmts and suggest a significant functional specialization of these enzymes
    Type of Publication: Journal article published
    PubMed ID: 14636159
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  • 6
    Keywords: CANCER CELLS ; CELLS ; tumor ; carcinoma ; Germany ; NETWORKS ; PROTEIN ; COMPLEX ; COMPLEXES ; MARKER ; RAT ; tumour ; ASSOCIATION ; MOLECULE ; ALPHA ; antibodies ; antibody ; PROGRESSION ; CARCINOMA CELLS ; MEMBRANE ; METASTASIS ; CARCINOMA-CELLS ; BETA ; SUPERFAMILY ; INTEGRIN ; CARCINOMAS ; LIPID RAFTS ; MASSES ; molecular ; EP-CAM ; interaction ; ORGANIZER ; CORE ; carcinoma cell ; beta 1 integrin ; CD151 ; CD9 ; D6.1A ; MAJOR CD9 ; prostaglandin F2 alpha receptor-regulatory protein (FPRP) ; raft ; RECEPTOR REGULATORY PROTEIN ; tetraspanin-enriched microdomain (TEM) ; TM4SF PROTEINS
    Abstract: Tetraspanins function as molecular organizers of multi-protein complexes by assembling primary complexes of a relatively low mass into extensive networks involved in cellular signalling. In this paper, we summarize our studies performed on the tetraspanin D6.1A/CO-029/TM4SF3 expressed by rat carcinoma cells. Primary complexes of D6.1A are almost indistinguishable from complexes isolated with anti-CD9 antibody. Indeed, both tetra-spanins directly associate with each other and with a third tetraspanin, CD81. Moreover, FPRP (prostaglandin F2 alpha receptor-regulatory protein)/EWI-F/CD9P-1), an Ig superfamily member that has been described to interact with CD9 and CD81, is also a prominent element in D6.1A complexes. Primary complexes isolated with D6.1A-specific antibody are clearly different from complexes containing the tetraspanin CD151. CD151 is found to interact only with D6.1A if milder conditions, i.e. lysis with LubrolWX instead of Brij96, are applied to disrupt cellular membranes. CD151 probably mediates the interaction of D6.1A primary complexes with alpha 3 beta 1 integrin. In addition, two other molecules were identified to be part of D6.1A complexes at this higher level of association: type II phosphatidylinositol 4-kinase and EpCAM, an epithelial marker protein overexpressed by many carcinomas. The characterization of the D6.1A core complex and additional more indirect interactions will help to elucidate the role in tumour progression and metastasis attributed to D6.1A
    Type of Publication: Journal article published
    PubMed ID: 15725074
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  • 7
    Keywords: APOPTOSIS ; CANCER ; CELLS ; EXPRESSION ; GROWTH ; proliferation ; SURVIVAL ; carcinoma ; CELL ; KINASE ; DEATH ; PROTEIN ; DRUG ; METABOLISM ; LINES ; ACTIVATION ; AP-1 ; CARCINOGENESIS ; BINDING ; CELL-LINES ; treatment ; CELL-LINE ; p53
    Abstract: Carcinogenesis is a dynamic and stepwise process, which is accompanied by a variety of somatic and epigenetic alterations in response to a changing microenvironment. Hypoxic conditions will select for cells, which have adjusted their metabolic profile and maintain proliferation by successfully competing for scarce nutritional and oxygen resources. In the present report we have studied the effects of energy depletion in the context of HPV-induced pathogenesis. We show that cervical carcinoma cell lines are susceptible to undergo either growth arrest or cell death under conditions of metabolic stress induced by 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR), a known activator of the AMP-activated protein kinase (AMPK). Our results revealed that AICAR treatment led to a reduced binding affinity of the transcription factor AP-1 and in turn to a selective suppression of HPV transcription. Moreover, the outcome of AICAR on proliferation and survival was dependent on p53 activation and the presence of LKB1, the major upstream kinases of AMPK. Using non-malignant LKB1 expressing somatic cell hybrids, which lose expression after tumourigenic segregation as well as siRNA LKB1 knock-down approaches, we could further demonstrate that expression of LKB1 protects cells from cytotoxicity induced by agents which modulate the ATP:AMP ratio. Since simulation of low energy status can selectively eradicate LKB1 negative cervical carcinoma cells, AICAR may represent a novel drug in the treatment of cervical cancer
    Type of Publication: Journal article published
    PubMed ID: 17212587
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  • 8
    Keywords: APOPTOSIS ; ENDOTHELIAL-CELLS ; EXPRESSION ; INHIBITOR ; CELL ; human ; MODEL ; QUANTIFICATION ; SYSTEM ; DISTINCT ; RNA ; DIFFERENTIATION ; BIOLOGY ; fibroblasts ; MOLECULAR-BIOLOGY ; ACID ; ACIDS ; MODULATION ; CALCIUM ; OXIDATIVE STRESS ; FLUORESCENCE ; SUPEROXIDE ; ARACHIDONIC-ACID ; OXYGEN ; reactive oxygen species ; INHIBITORS ; molecular biology ; molecular ; fibroblast ; INTERFERENCE ; NAD(P)H OXIDASE ; SUPEROXIDE-PRODUCTION ; SUPEROXIDE-DISMUTASE ; REACTIVE OXYGEN ; LEVEL ; ROS ; DOCOSAHEXAENOIC ACID ; enzymatic ; OXIDASE ; polyunsaturated fatty acid ; superoxide dismutase ; CARDIAC FIBROBLASTS ; haem oxygenase ; NADPH oxidase (NOX) ; NADPH OXIDASE ACTIVATION
    Abstract: The strong ROS (reactive oxygen species) production, part of an antioxidant response of human fibroblasts triggered by DHA (docosahexaenoic acid; C22:6.n-3), served as a model for deciphering the relative contribution of NOX (NADPH oxidase) to ROS production, as the role of this enzymatic system remains controversial. Using hydroxyethidium fluorescence for fibroblast ROS production, RT (reverse transcriptase)-PCR for NOX 4 mRNA quantification and mRNA silencing, we show that ROS production evolves in parallel with the catalytic activity of NOX and is suppressed by siNOX 4 (small interference oligonucleotide RNA directed against NOX 4) silencing. Apocynin and plumbagin, specific inhibitors of NOX, prevent ROS production in this cellular model and confirm the role of NOX 4 for this production. Furthermore, we show that, in cell lysates, NOX 4 activity can be modulated by PUFAs (polyunsaturated fatty acids) at the micromolar level in the presence of calcium: NOX 4 activity is increased by arachidonic acid (C20:4.n-6) (similar to 175 % of the control), and conjugated linoleic acid (C-18:2 [9Z, 11 E]) is a potent inhibitor (50 % of the control). Unexpectedly, intracellular superoxide dismutase does not participate in the modulation of this ROS production and the opposite effects of some PUFAs, described in our experiments, could suggest another way of regulating NOX activity
    Type of Publication: Journal article published
    PubMed ID: 17472580
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  • 9
    Keywords: CANCER ; CELLS ; EXPRESSION ; IN-VITRO ; INHIBITOR ; proliferation ; AGENTS ; carcinoma ; CELL ; Germany ; IN-VIVO ; MODEL ; MODELS ; VITRO ; VIVO ; screening ; ENZYMES ; GENE ; GENE-EXPRESSION ; GENES ; METABOLISM ; DIFFERENTIATION ; INDUCTION ; BIOLOGY ; MOLECULAR-BIOLOGY ; IDENTIFICATION ; gene expression ; TRANSCRIPTIONAL ACTIVITY ; ASSAY ; CARCINOMA CELLS ; NUMBER ; EFFICIENT ; acetylation ; CARCINOMA-CELLS ; ONCOGENE ; PHENOTYPE ; RECRUITMENT ; specificity ; HISTONE DEACETYLASE ; histone deacetylase inhibitor ; REPRESSION ; neuroblastoma ; INHIBITORS ; AGENT ; molecular biology ; molecular ; INCREASE ; LEVEL ; ENZYME ; HISTONE DEACETYLASE INHIBITORS ; HISTONE ACETYLATION ; H4 ; ENGLAND ; amidohydrolase ; STRAIN ; SMALL-MOLECULE ; ACTINOMYCIN-D ; amidohydrolase (HDAH) ; chromone ; histone deacetylase-like ; KETONE INHIBITORS ; LEUKEMIA-CELL LINE ; medium-throughput screening ; p-benzoquinone ; pyran-4-one ; SOPHOROSE LIPIDS ; trifluoromethylketone
    Abstract: HDACs (histone deacetylases) are considered to be among the most important enzymes that regulate gene expression in eukaryotic cells. In general, increased levels of histone acetylation are associated with increased transcriptional activity, whereas decreased levels are linked to repression of gene,expression. HDACs associate with a number of cellular oncogenes and tumour-suppressor genes, leading to an aberrant recruitment of HDAC activity, which results in changes of gene expression, impaired differentiation and excessive proliferation of tumour cells. Therefore HDAC inhibitors are efficient anti-proliferative agents in both in vitro and in vivo pre-clinical models of cancer, making them promising anticancer therapeutics. In the present paper, we present the results of a medium-throughput screening programme aiming at the identification of novel HDAC inhibitors using HDAH (HDAC-like amidohydrolase) from Bordetella or Alcaligenes strain FB188 as a model enzyme. Within a library of 3719 compounds, several new classes of HDAC inhibitor were identified. Among these hit compounds, there were also potent inhibitors of eukaryotic HDACs, as demonstrated by an increase in histone H4 acetylation, accompanied by a decrease in tumour cell metabolism in both SHEP neuroblastoma and T24 bladder carcinoma cells. In conclusion, screening of a compound library using FB188 HDAH as model enzyme identified several promising new lead structures for further development
    Type of Publication: Journal article published
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  • 10
    Keywords: RECEPTOR ; CELLS ; proliferation ; CELL ; IN-VIVO ; KINASE ; VIVO ; TOOL ; PROTEIN ; DIFFERENTIATION ; MOLECULES ; TRANSDUCTION ; ACTIVATION ; LIGAND ; DOMAIN ; BINDING ; DOWN-REGULATION ; GROWTH-FACTOR RECEPTOR ; PHOSPHORYLATION ; signal transduction ; SIGNAL ; MOLECULE ; FORM ; MUTANT ; hormone ; resistance ; DECREASE ; SIGNAL-TRANSDUCTION ; SURFACE ; DIMERIZATION ; ENDOPLASMIC-RETICULUM ; ERYTHROPOIETIN RECEPTOR ; TYROSINE PHOSPHORYLATION ; ER ; POTENT ; COMPARTMENTS ; MOTIF ; CELL-SURFACE EXPRESSION ; Janus kinase 2 ; PROTEIN-TYROSINE-PHOSPHATASE ; PTP1B ; PTP1B (protein tyrosine phosphatase 1B) 'substrate-trapping' mutant ; TYROSINE-PHOSPHORYLATION
    Abstract: Erythropoietin (EPO) is the principal hormone regulating the proliferation of erythroid precursors and their differentiation into erythrocytes. Binding of ligand to the cell-surface EPO-R (EPO receptor) induces dimerization and JAK2 (Janus kinase 2)-mediated tyrosine phosphorylation of the receptor. Less than 1% of the EPO-Rs are displayed on the cell Surface; most of the receptor molecules are retained in intracellular compartments, including the ER (endoplasmic reticulum). Using pervanadate (PV) as a potent tool to inhibit cellular PTPs (protein tyrosine phosphatases), we demonstrated previously the accumulation of mature (endoglycosidase H-resistant) tyrosine-phosphorylated EPO-R [Cohen, Altaratz, Zick, Klingmuller and Neumann (1997) Biochem. J. 327, 391-397]. In the present study, we investigated the participation of the ER-associated PTP1B in the dephosphorylation of intracellular EPO-R. We demonstrate tyrosine phosphorylation of EPO-R in BOSC-23T cells co-expressing EPO-R and the 'substrate- trapping' mutant form of PTP1B, PTP1B D181A (referred to as PTP1BD). In vivo interaction between EPO-R and PTP1B suggested that PTP1B dephosphorylates the EPO-R intracellularly. Endoglycosidase H resistance of tyrosine-phosphorylated EPO-R in cells expressing PTP1BD suggested that mature EPO-R is dephosphorylated by PTP1B. Stimulation with EPO of cells co-expressing EPO-R and either PTP1BD or PTP1B resulted in an increase or decrease respectively in phosphotyrosine EPO-R. We thus suggest that PTP1B dephosphorylates EPO-stimulated EPO-R and participates in the downregulation cascade of EPO-mediated signal transduction
    Type of Publication: Journal article published
    PubMed ID: 14527337
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