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  • Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. 8360275

    The band 4.1 superfamily of proteins show approx. 30% sequence identity in their amino-terminal region to the membrane binding domain of erythrocyte band 4.1. Within this superfamily are three members, ezrin, radixin and moesin, that show approx. 75% overall sequence identity. A comparison of the domain structure and intracellular localization of ezrin and moesin in cultured cells is reported here. Limited proteolytic digestion of ezrin or moesin yields a relatively stable 32 kDa domain derived from the amino-terminal region that is homologous to the protease-resistant membrane binding domain of erythrocyte band 4.1. The remaining regions of the two proteins give rise to very different fragments, suggesting that the secondary/tertiary structures of the two proteins are different in these regions. We have generated polyclonal antibodies that discriminate between ezrin and moesin, and do not react with radixin. All cultured cell lines investigated contain ezrin, whereas moesin is variably expressed. Cells that contain both ezrin and moesin show a very similar pattern: both proteins are enriched and colocalize with actin in cell surface structures. Ezrin is also detected in the cytoplasm. In cells with few or no surface structures, both proteins show a patchy distribution in regions of the cell that contain fine networks of actin filaments. No staining of focal contacts or adherens junctions was observed. These results, together with those of others, lead to the conclusion that, of the members of this protein family, only radixin is an authentic component of adherens junctions and focal contacts. Ezrin and moesin are both found in cell surface structures after treatment of human A431 cells with epidermal growth factor, and ezrin, but not moesin, becomes phosphorylated on tyrosine. This study shows that ezrin and moesin have a similar subcellular distribution in cultured cells, yet are distinguishable in their expression, structure and ability to serve as a kinase substrate.
    Document Type:
    Reference
    Product Catalog Number:
    07-121

  • Insulin like growth factor 2 regulation of aryl hydrocarbon receptor in MCF-7 breast cancer cells. 24380854

    Insulin like growth factor (IGF)-1 and IGF-2 stimulate normal growth, development and breast cancer cell proliferation. Cyclin D1 (CCND1) promotes cell cycle by inhibiting retinoblastoma protein (RB1). The aryl hydrocarbon receptor (AHR) is a major xenobiotic receptor that also regulates cell cycle. The purpose of this study was to investigate whether IGF-2 promotes MCF-7 breast cancer proliferation by inducing AHR. Western blot and quantitative real time PCR (Q-PCR) analysis revealed that IGF-2 induced an approximately 2-fold increase (Pless than .001) in the expression of AHR and CCND1. Chromatin immunoprecipitation (ChIP), followed by Q-PCR indicated that IGF-2 promoted (Pless than .001) a 7-fold increase in AHR binding on the CCND1 promoter. AHR knockdown significantly (Pless than .001) inhibited IGF-2 stimulated increases in CCND1 mRNA and protein. AHR knockdown cells were less (Pless than .001) responsive to the proliferative effects of IGF-2 than control cells. Collectively, our findings have revealed a new regulatory mechanism by which IGF-2 induction of AHR promotes the expression of CCND1 and the proliferation of MCF-7 cells. This previously uncharacterized pathway could be important for the proliferation of IGF responsive cancer cells that also express AHR.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Vanilloid receptor like 1 (VRL1) immunoreactivity in mammalian retina: colocalization with somatostatin and purinergic P2X1 receptors. 15174083

    The distribution of vanilloid receptor like1 immunoreactivity (VRL1-IR) in the retinas of rat, cat, and monkey was studied by single- and double-labeling immunocytochemistry. The patterns were similar for all three species in that VRL1-IR was most prominent in the inner plexiform layer, with scattered compact projections to the outer plexiform layer (OPL). VRL1-immunoreactive cell bodies were present throughout the rat retina, represented by amacrine cells in the inner nuclear layer and ganglion cell layer (GCL). In cat and monkey retinas, VRL1-immunoreactive cell bodies were restricted to the GCL in the inferior retina. Occasional cell bodies were associated with retinal blood vessels, but their identity as pericytes, glia, or neurons is uncertain. All VRL1-immunoreactive cells and processes colocalized with somatostatin and purinergic P2X1 receptor-IR but not with tyrosine hydroxylase-IR. VRL1-immunoreactive processes in the OPL did not label with antisera against synaptic vesicle 2 (SV2), suggesting that they were dendritic and did not derive from interplexiform cells. However, VRL1-immunoreactive processes in the far periphery toward the pars plana labeled for SV2, suggesting that these processes were presynaptic. The VRL1-immunoreactive cell bodies in the monkey GCL were not calbindin-immunoreactive, demonstrating that they were not displaced H2 horizontal cells. The VRL1-immunoreactive cells in cat and monkey could represent biplexiform and/or associational ganglion cells that receive input in the OPL throughout the retina and direct output to the far periphery. The presence of P2X1 receptors and vanilloid receptor like 1 protein on somatostatin-containing neurons in mammalian retina adds to the growing complexity regarding the chemical control of retinal function that is likely to include the microcirculation.
    Document Type:
    Reference
    Product Catalog Number:
    AB5398P
    Product Catalog Name:
    Anti-Vanilloid Receptor Like Protein Antibody, pain, CT

  • The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity. 25481026

    The outcome of a viral infection is regulated by complex interactions of viral and host factors. SARS coronavirus (SARS-CoV) engages and regulates several innate immune response pathways during infection. We have previously shown that the SARS-CoV Papain-like Protease (PLpro) inhibits type I interferon (IFN) by inhibiting IRF3 phosphorylation thereby blocking downstream Interferon induction. This finding prompted us to identify other potential mechanisms of inhibition of PLpro on IFN induction.We have used plasmids expressing PLpro and IRF3 including an IRF3 mutant that is constitutively active, called IRF3(5D). In these experiments we utilize transfections, chromatin immunoprecipitation, Electro-mobility Shift Assays (EMSA) and protein localization to identify where IRF3 and IRF3(5D) are inhibited by PLpro.Here we show that PLpro also inhibits IRF3 activation at a step after phosphorylation and that this inhibition is dependent on the de-ubiquitination (DUB) activity of PLpro. We found that PLpro is able to block the type I IFN induction of a constitutively active IRF3, but does not inhibit IRF3 dimerization, nuclear localization or DNA binding. However, inhibition of PLpro's DUB activity by mutagenesis blocked the IRF3 inhibition activity of PLpro, suggesting a role for IRF3 ubiquitination in induction of a type I IFN innate immune response.These results demonstrate an additional mechanism that PLpro is able to inhibit IRF3 signaling. These data suggest novel innate immune antagonism activities of PLpro that may contribute to SARS-CoV pathogenesis.
    Document Type:
    Reference
    Product Catalog Number:
    06-599
    Product Catalog Name:
    Anti-acetyl-Histone H3 Antibody

  • Lnc‑IL7R promotes the growth of fibroblast‑like synoviocytes through interaction with enhancer of zeste homolog 2 in rheumatoid arthritis. 28138707

    Rheumatoid arthritis (RA) is an inflammatory and autoimmune disease that affects ~1% of the world's population. Although the precise mechanism of RA has yet to be elucidated, accumulating evidence suggests that fibroblast‑like synoviocytes (FLSs) serve critical roles in the initiation and progression of RA. However, the underlying molecular mechanisms of FLS proliferation have yet to be elucidated. Long noncoding‑interleukin‑7 receptor (lnc‑IL7R) has been recently identified, which is activated by lipopolysaccharide (LPS) stimulation and diminishes the LPS‑induced inflammatory response. In the present study, gain‑ and loss‑of‑function assays were performed in order to investigate the role of lnc‑IL7R in FLS. It is demonstrated, to the best of the authors' knowledge for the first time, that lnc‑IL7R promotes cell proliferation, cell cycle progression and inhibits apoptosis in FLS. Further investigation identified that lnc‑IL7 interacts with enhancer of zeste homolog 2 (EZH2) and is required for polycomb repressive complex 2 (PRC2)‑mediated suppression, including cyclin‑dependent kinase inhibitor 1A and cyclin‑dependent kinase inhibitor 2A. Lnc‑IL7R may be a promising therapeutic target for the treatment of RA.
    Document Type:
    Reference
    Product Catalog Number:
    17-701
    Product Catalog Name:
    EZ-Magna RIP™ RNA-Binding Protein Immunoprecipitation Kit