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  • Vascular adhesion protein-1 mediates adhesion and transmigration of lymphocytes on human hepatic endothelial cells. 12097405

    Vascular adhesion protein-1 (VAP-1) is an amine oxidase and adhesion receptor that is expressed by endothelium in the human liver. The hepatic sinusoids are perfused by blood at low flow rates, and sinusoidal endothelium lacks selectin expression and has low levels of CD31, suggesting that VAP-1 may play a specific role in lymphocyte recruitment to the liver. In support of this we now report the constitutive expression of VAP-1 on human hepatic sinusoidal endothelial cells (HSEC) in vitro and demonstrate that VAP-1 supports adhesion and transmigration of lymphocytes across these cells under physiological shear stress. These are the first studies to report the function of VAP-1 on primary human endothelial cells. Under static conditions lymphocyte adhesion to unstimulated HSEC was dependent on VAP-1 and ICAM-2, whereas adhesion to TNF-alpha-stimulated HSEC was dependent on ICAM-1, VCAM-1, and VAP-1. Under conditions of flow, blocking VAP-1 reduced lymphocyte adhesion to TNF-alpha-treated HSEC by 50% and significantly reduced the proportion of adherent lymphocytes that transmigrated across cytokine or LPS-activated endothelium. In addition, inhibition of the amine oxidase activity of VAP-1 reduced both adhesion and transmigration of lymphocytes to a level similar to that seen with VAP-1 Ab. Thus, VAP-1 can support transendothelial migration as well as adhesion, and both functions are dependent on its enzymatic activity. In the absence of selectins and CD31, VAP-1 may play a specific role in lymphocyte recruitment via hepatic sinusoidal endothelium. Moreover, since VAP-1 is induced on nonhepatic endothelium in response to inflammation, its ability to support lymphocyte transendothelial migration may be an important systemic function of VAP-1.
    Tipo de documento:
    Referencia
    Referencia del producto:
    MAB2154
    Nombre del producto:
    Anti-P-Selectin Antibody, clone P8G6

  • Functional consequences of homo- but not hetero-oligomerization between transporters for the biogenic amine neurotransmitters. 12787070

    Before this study, the human norepinephrine transporter (hNET) was the only member of the biogenic amine neurotransmitter transporter family that had not been demonstrated to be a functional homo-oligomer. Here, using two forms of the transporter, I155C and hNET-myc, with distinct antigenicity and inhibitor sensitivity, we demonstrated that hNET exists as a homo-oligomer. hNET I155C is a functional mutant and is sensitive to inactivation by the sulfhydryl reagent [2-(trimethylammonium)ethyl]methanethiosulfonate, while hNET-myc is resistant to inactivation by this reagent. Coimmunoprecipitation of these two forms demonstrated that a physical interaction exists between norepinephrine transporter monomers. Further characterization of this physical interaction has revealed that the activity of norepinephrine transporters depends on interactions between monomers. Because norepinephrine transporters and serotonin transporters are the only two members of the neurotransmitter transporter family endogenously expressed in the cell membrane of the same cells, placental syncytiotrophoblasts, we tested the ability of norepinephrine transporters and serotonin transporters to associate and function in a hetero-oligomeric form. Similarly, coexpression of hNET-myc with serotonin transporter-FLAG showed a physical interaction in coimmunoprecipitation assays. However, coexpression of serotonin and norepinephrine transporters did not sensitize norepinephrine transporter activity to inhibition by citalopram, a selective serotonin transport inhibitor. Thus, the norepinephrine transporter-serotonin transporter physical association did not produce functional consequences. Based on this, we propose that the transporters for biogenic amine neurotransmitters interact functionally in homo- but not hetero-oligomeric forms.
    Tipo de documento:
    Referencia
    Referencia del producto:
    CBL430

  • Polarized expression of the antidepressant-sensitive serotonin transporter in epinephrine-synthesizing chromaffin cells of the rat adrenal gland. 9245500

    Antidepressant-sensitive serotonin (5-hydroxytryptamine, 5HT) transporters (SERTs) clear the amine from extracellular spaces in the CNS and periphery as a mechanism for transmitter inactivation and recycling. Although it is known that SERTs are preferentially expressed on basolateral domains in transfected epithelial cells, details of the transporter's membrane localization in vivo are lacking. 5HT and 5HT receptors have been identified in the rodent adrenal gland. Using SERT antagonist autoradiography, we establish the presence of antidepressant-sensitive transport sites in the rat adrenal medulla. Immunofluorescence experiments using antibodies specific for the SERT COOH and NH2 termini, for 5HT, or for catecholamine biosynthetic enzymes suggest that SERT mediates intra-cellular 5HT accumulation by epinephrine-secreting chromaffin cells. Using confocal microscopy, we establish that SERT expression is nonuniformly distributed along the plasma membrane of chromaffin cells. Notably, SERT immunoreactivity is largely absent from plasma membranes bordering smooth muscle that surrounds vascular sinusoids. Rather, SERT is highly expressed in membranes adjoining other chromaffin cells, consistent with a role for 5HT and SERT in autocrine or paracrine control of chromaffin cell physiology. SNAP-25, a t-SNARE protein implicated in neurotransmitter release, was found to colocalize with SERT. In contrast, Na,K ATPase and NCAM are uniformly distributed along the entire perimeter of chromaffin cell membranes. These findings underscore a role for 5HT and SERT in adrenal physiology, reveal unrecognized polarity of chromaffin cell plasma membranes, and warrant a consideration of common targeting mechanisms localizing amine transporters near release sites.
    Tipo de documento:
    Referencia
    Referencia del producto:
    MAB1564
    Nombre del producto:
    Anti-Serotonin Transporter Antibody, clone 17-7A4

  • Amine oxidase copper-containing 1 (AOC1) is a downstream target gene of the Wilms tumor protein, WT1, during kidney development. 25037221

    Amine oxidase copper-containing 1 (AOC1; formerly known as amiloride-binding protein 1) is a secreted glycoprotein that catalyzes the degradation of putrescine and histamine. Polyamines and their diamine precursor putrescine are ubiquitous to all organisms and fulfill pivotal functions in cell growth and proliferation. Despite the importance of AOC1 in regulating polyamine breakdown, very little is known about the molecular mechanisms that control its expression. We report here that the Wilms tumor protein, WT1, which is necessary for normal kidney development, activates transcription of the AOC1 gene. Expression of a firefly luciferase reporter under control of the proximal AOC1 promoter was significantly enhanced by co-transfection of a WT1 expression construct. Binding of WT1 protein to a cis-regulatory element in the AOC1 promoter was confirmed by electrophoretic mobility shift assay and chromatin immunoprecipitation. Antisense inhibition of WT1 protein translation strongly reduced Aoc1 transcripts in cultured murine embryonic kidneys and gonads. Aoc1 mRNA levels correlated with WT1 protein in several cell lines. Double immunofluorescent staining revealed a co-expression of WT1 and AOC1 proteins in the developing genitourinary system of mice and rats. Strikingly, induced changes in polyamine homeostasis affected branching morphogenesis of cultured murine embryonic kidneys in a developmental stage-specific manner. These findings suggest that WT1-dependent control of polyamine breakdown, which is mediated by changes in AOC1 expression, has a role in kidney organogenesis.
    Tipo de documento:
    Referencia
    Referencia del producto:
    Múltiplo
    Nombre del producto:
    Múltiplo

  • Cervicothalamic tract termination: a reexamination and comparison with the distribution of monoclonal antibody Cat-301 immunoreactivity in the cat. 9833685

    The distribution of cervicothalamic tract (CTT) terminations, labeled with anterogradely transported tracers (WGA-HRP or biotinylated dextran amine) injected into the lateral cervical nucleus of cats, was compared with the distribution of immunoreactivity for a cell-surface antigen detected with the monoclonal antibody Cat-301. The most abundant CTT termination is present in the ventrobasal complex (VB), mainly in its lateral part (VPL) and only sparsely in its medial part (VPM). In the VPL, the CTT preferentially terminates in a Cat-301-sparse peripheral rim of the nucleus and in between its lateral and medial subdivisions (VPLI and VPLm). CTT terminations are sparse in the central Cat-301-dense parts of the VPL. In the ventral periphery of VB (VBvp), situated in between the VPL/VPM and the external medullary lamina, thin CTT fibers with spaced varicosities is seen among the large fibers of passage. The VBvp is essentially devoid of Cat-301 immunoreactivity. Scattered clusters of CTT termination are also seen caudal and dorsal to the VB in the medial division of the posterior complex (POm), which is virtually devoid of Cat-301 immunoreactivity. In the caudal thalamus, dense and focused CTT termination is present in the medial extension of the magnocellular medial geniculate nucleus (MGmc) but absent from its main lateral part. The termination in the MGmc is centered upon clusters of cells displaying dense Cat-301 immunoreactivity. The present study demonstrates previously unrecognized or unconfirmed CTT terminations in the VPM and in the VBvp, and confirm previously described projections to the VPL, POm and MGmc. The preferential termination of the CTT in the Cat-301-sparse peripheral region of the VPL demonstrates that the CTT is related to a chemically defined VPL compartment. In the light of previous data, this observation suggests that the CTT is related to one or more thalamocortical channels that are partly or completely separate from that (those) activated through the dorsal column-medial lemniscal pathway. The organization of the thalamocortical channel(s) activated through the CTT remains to be elucidated. In contrast to the termination in the VPL, CTT termination in the medial MGmc is focused to clusters of Cat-301 immunolabeled cells. The significance of this difference between CTT recipient cells in the VPL and in the MGmc is unclear.
    Tipo de documento:
    Referencia
    Referencia del producto:
    MAB5284
    Nombre del producto:
    Anti-Chondroitin Sulfate Proteoglycan Antibody, Brain (core protein), clone Cat-301

  • Ergopeptines bromocriptine and ergovaline and the dopamine type-2 receptor inhibitor domperidone inhibit bovine equilibrative nucleoside transporter 1-like activity. 21790119

    Neotyphodium coenophialum-infected tall fescue contains ergopeptines. Except for interactions with biogenic amine receptors (e.g., dopamine type-2 receptor, D2R), little is known about how ergopeptines affect animal metabolism. The effect of ergopeptines on bovine nucleoside transporters (NT) was evaluated using Madin-Darby bovine kidney (MDBK) cells. Equilibrative NT1 (ENT1)-like activity accounted for 94% of total NT activity. Inhibitory competition (IC(50)) experiments found that this activity was inhibited by both bromocriptine (a synthetic model ergopeptine and D2R agonist) and ergovaline (a predominant ergopeptine of tall fescue). Kinetic inhibition analysis indicated that bromocriptine inhibited ENT1-like activity through a competitive and noncompetitive mechanism. Domperidone (a D2R antagonist) inhibited ENT1 activity more in the presence than in the absence of bromocriptine and displayed an IC(50) value lower than that of bromocriptine or ergovaline, suggesting that inhibition was not through D2R-mediated events. These novel mechanistic findings imply that cattle consuming endophyte-infected tall fescue have reduced ENT1 activity and, thus, impaired nucleoside metabolism.
    Tipo de documento:
    Referencia
    Referencia del producto:
    07-134

  • Transport of biogenic amine neurotransmitters at the mouse blood-retina and blood-brain barriers by uptake1 and uptake2. 22850405

    Uptake1 and uptake2 transporters are involved in the extracellular clearance of biogenic amine neurotransmitters at synaptic clefts. We looked for them at the blood-brain barrier (BBB) and blood-retina barriers (BRB), where they could be involved in regulating the neurotransmitter concentration and modulate/terminate receptor-mediated effects within the neurovascular unit (NVU). Uptake2 (Oct1-3/Slc22a1-3, Pmat/Slc29a4) and Mate1/Slc47a1 transporters are also involved in the transport of xenobiotics. We used in situ carotid perfusion of prototypic substrates like [(3)H]-1-methyl-4-phenylpyridinium ([(3)H]-MPP(+)), [(3)H]-histamine, [(3)H]-serotonin, and [(3)H]-dopamine, changes in ionic composition and genetic deletion of Oct1-3 carriers to detect uptake1 and uptake2 at the BBB and BRB. We showed that uptake1 and uptake2 are involved in the transport of [(3)H]-dopamine and [(3)H]-MPP(+) at the blood luminal BRB, but not at the BBB. These functional studies, together with quantitative RT-PCR and confocal imaging, suggest that the mouse BBB lacks uptake1 (Net/Slc6a2, Dat/Slc6a3, Sert/Slc6a4), uptake2, and Mate1 on both the luminal and abluminal sides. However, we found evidence for functional Net and Oct1 transporters at the luminal BRB. These heterogeneous transport properties of the brain and retina NVUs suggest that the BBB helps protect the brain against biogenic amine neurotransmitters in the plasma while the BRB has more of a metabolic/endocrine role.
    Tipo de documento:
    Referencia
    Referencia del producto:
    MAB369
    Nombre del producto:
    Anti-Dopamine Transporter Antibody, NT, clone DAT-Nt

  • Serotonin augments smooth muscle differentiation of bone marrow stromal cells. 24595007

    Bone marrow stromal cells (BMSCs) contain a subset of multipotent stem cells. Here, we demonstrate that serotonin, a biogenic amine released by platelets and mast cells, can induce the smooth muscle differentiation of BMSCs. Brown Norway rat BMSCs stimulated with serotonin had increased expression of the smooth muscle markers smooth muscle myosin heavy chain (MHC) and α actin (α-SMA) by qPCR and Western blot, indicating smooth muscle differentiation. This was accompanied by a concomitant down-regulation of the microRNA miR-25-5p, which was found to negatively regulate smooth muscle differentiation. Serotonin upregulated serum response factor (SRF) and myocardin, transcription factors known to induce contractile protein expression in smooth muscle cells, while it down-regulated Elk1 and Kruppel-like factor 4 (KLF4), known to induce proliferation. Serotonin increased SRF binding to promoter regions of the MHC and α-SMA genes, assessed by chromatin immunoprecipitation assay. Induction of smooth muscle differentiation by serotonin was blocked by the knock-down of SRF and myocardin. Transforming growth factor (TGF)-β1 was constitutively expressed by BMSCs and serotonin triggered its release. Inhibition of miR-25-5p augmented TGF-β1 expression, however the differentiation of BMSCs was not mediated by TGF-β1. These findings demonstrate that serotonin promotes a smooth muscle-like phenotype in BMSCs by altering the balance of SRF, myocardin, Elk1 and KLF4 and miR-25-5p is involved in modulating this balance. Therefore, serotonin potentially contributes to the pathogenesis of diseases characterized by tissue remodeling with increased smooth muscle mass.
    Tipo de documento:
    Referencia
    Referencia del producto:
    17-10086
    Nombre del producto:
    EZ-Magna ChIP™ A/G Chromatin Immunoprecipitation Kit

  • Modulating cell adhesion and spreading by control of FnIII7-10 orientation on charged self-assembled monolayers (SAMs) of alkanethiolates. 16514600

    In this work, we demonstrate that surface charge can be used to modulate cell adhesion/spreading through the control of the orientation of adsorbed FnIII(7-10), which is a cell-adhesive protein containing RGD residues. Carboxylic acid (COOH) and amine (NH(2))-terminated self-assembled monolayers (SAMs) of alkanethiolates were used as model negatively and positively charged surfaces, respectively. The adsorbed amount of FnIII(7-10) is controlled to be equivalent on both SAMs as confirmed by the adsorption isotherms determined using I(125)-radiolabeled FnIII(7-10.) The binding of a monoclonal antibody specific for the cell-binding domain of FnIII(7-10) was measured by surface plasmon resonance (SPR) to evaluate FnIII(7-10) orientations on different SAMs. Results indicate that adsorbed FnIII(7-10) on NH(2)-SAM has an orientation with more cell-binding domains accessible than on COOH-SAM, confirming our predictions from Monte Carlo simulations. Both phase contrast images and Vybrant MTT cell proliferation assays show that the adhesion/spreading of bovine aortic endothelial cells (BAECs) on the NH(2)-SAM is significantly better than that on the COOH-SAM coated with an equivalent amount of FnIII(7-10). These results indicate that surface charge can be used to specifically orient cell adhesive proteins such as FnIII(7-10), thus providing a promising strategy to increase the activity of materials incorporating biological moieties.
    Tipo de documento:
    Referencia
    Referencia del producto:
    MAB1934
    Nombre del producto:
    Anti-Fibronectin Antibody, cell binding peptide, clone 784A2A6

  • Projections from the paraventricular nucleus of the thalamus to the forebrain, with special emphasis on the extended amygdala. 18022956

    The paraventricular nucleus of the thalamus (PVT) is part of a group of midline and intralaminar thalamic nuclei implicated in arousal and attention. This study examined the connections between the PVT and the forebrain by using the retrograde tracer cholera toxin B (CTb) and the anterograde tracer biotin dextran amine (BDA). The anterior and posterior regions of the PVT were found to send a dense projection to the nucleus accumbens. The posterior PVT was also found to provide a strong projection to the lateral bed nucleus of the stria terminalis (BST), interstitial nucleus of the posterior limb of the anterior commissure (IPAC), and central nucleus of the amygdala (CeA), regions associated with the extended amygdala. In contrast, the anterior PVT was found to send a weaker projection to the extended amygdala. The basolateral nucleus of the amygdala and the medial prefrontal cortex were found to receive a relatively weak projection from the PVT, and other regions of the BST and amygdala were found to be poorly innervated by the PVT. In addition, the PVT was found to innervate regions in the extended amygdala that contained corticotropin-releasing factor (CRF) neurons, many of which were found to receive apparent contacts from PVT fibers. The projection from the PVT to the nucleus accumbens and extended amygdala places the PVT in a key anatomical position to influence adaptive behaviors as well as the physiological and neuroendocrine responses associated with these behaviors.
    Tipo de documento:
    Referencia
    Referencia del producto:
    AB3704
    Nombre del producto:
    Anti-Orexin-A Antibody