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  • 1
    Online Resource
    Online Resource
    EVI1 Acts as an Inducible Negative-Feedback Regulator of NF-κB by Inhibiting p65 Acetylation
    The American Association of Immunologists ; 2012
    In:  The Journal of Immunology Vol. 188, No. 12 ( 2012-06-15), p. 6371-6380
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 188, No. 12 ( 2012-06-15), p. 6371-6380
    Abstract: Inflammation is a hallmark of many important human diseases. Appropriate inflammation is critical for host defense; however, an overactive response is detrimental to the host. Thus, inflammation must be tightly regulated. The molecular mechanisms underlying the tight regulation of inflammation remain largely unknown. Ecotropic viral integration site 1 (EVI1), a proto-oncogene and zinc finger transcription factor, plays important roles in normal development and leukemogenesis. However, its role in regulating NF-κB–dependent inflammation remains unknown. In this article, we show that EVI1 negatively regulates nontypeable Haemophilus influenzae- and TNF-α–induced NF-κB–dependent inflammation in vitro and in vivo. EVI1 directly binds to the NF-κB p65 subunit and inhibits its acetylation at lysine 310, thereby inhibiting its DNA-binding activity. Moreover, expression of EVI1 itself is induced by nontypeable Haemophilus influenzae and TNF-α in an NF-κB–dependent manner, thereby unveiling a novel inducible negative feedback loop to tightly control NF-κB–dependent inflammation. Thus, our study provides important insights into the novel role for EVI1 in negatively regulating NF-κB–dependent inflammation, and it may also shed light on the future development of novel anti-inflammatory strategies.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.1103527
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2012
    detail.hit.zdb_id: 1475085-5
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  • 2
    Online Resource
    Online Resource
    Abstract 1496: Proteolytic regulation of the Wnt/PCP pathway in cancer
    American Association for Cancer Research (AACR) ; 2011
    In:  Cancer Research Vol. 71, No. 8_Supplement ( 2011-04-15), p. 1496-1496
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 71, No. 8_Supplement ( 2011-04-15), p. 1496-1496
    Abstract: The non-canonical Wnt signaling pathway regulates planar cell polarity (PCP) and directed cell motility in processes as diverse as embryogenesis and cancer cell invasion. Here, we establish that the protein tyrosine kinase-7 (PTK7), an essential component of the Wnt/PCP pathway, strongly inhibits cancer cell invasion by reorganizing the actin cytoskeleton and altering actomyosin contraction. We also demonstrate that the pro-invasive membrane type-1 matrix metalloproteinase (MT1-MMP) functions as a principal sheddase of PTK7 and reverses its inhibition of cell invasion. MT1-MMP directly cleaves the PKP621↓LI sequence localized in an exposed region of the seventh Ig-like domain, generating an N-terminal, soluble PTK7 species (sPTK7) that interacts with membrane PTK7 in a dominant-negative fashion. Protease activity was reciprocally correlated with levels of PTK7 in several cell types and during zebrafish embryogenesis. Reduced PTK7 levels were observed in breast tumours compared to normal breast tissue. Conceptually, our data suggest that the Wnt/PCP pathway converges with pericellular proteolysis to regulate cell motility in normal development and cancer. Further insight into MT1-MMP regulation of Wnt/PCP may promote understanding of directional cell motility in embryogenesis and cancer and lead to identification of therapeutics to treat PCP-related developmental disorders and malignancy. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 1496. doi:10.1158/1538-7445.AM2011-1496
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2011-1496
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2011
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 3
    Online Resource
    Online Resource
    Globular Adiponectin Enhances Muscle Insulin Action via Microvascular Recruitment and Increased Insulin Delivery
    Ovid Technologies (Wolters Kluwer Health) ; 2013
    In:  Circulation Research Vol. 112, No. 9 ( 2013-04-26), p. 1263-1271
    Details
    In: Circulation Research, Ovid Technologies (Wolters Kluwer Health), Vol. 112, No. 9 ( 2013-04-26), p. 1263-1271
    Abstract: Adiponectin enhances insulin action and induces nitric oxide–dependent vasodilatation. Insulin delivery to muscle microcirculation and transendothelial transport are 2 discrete steps that limit insulin’s action. We have shown that expansion of muscle microvascular surface area increases muscle insulin delivery and action. Objective: To examine whether adiponectin modulates muscle microvascular recruitment thus insulin delivery and action in vivo. Methods and Results: Overnight fasted adult male rats were studied. We determined the effects of adiponectin on muscle microvascular recruitment, using contrast-enhanced ultrasound, on insulin-mediated microvascular recruitment and whole-body glucose disposal, using contrast-enhanced ultrasound and insulin clamp, and on muscle insulin clearance and uptake with 125 I-insulin. Globular adiponectin potently increased muscle microvascular blood volume without altering microvascular blood flow velocity, leading to a significantly increased microvascular blood flow. This was paralleled by a ≈30% to 40% increase in muscle insulin uptake and clearance, and ≈30% increase in insulin-stimulated whole-body glucose disposal. Inhibition of endothelial nitric oxide synthase abolished globular adiponectin-mediated muscle microvascular recruitment and insulin uptake. In cultured endothelial cells, globular adiponectin dose-dependently increased endothelial nitric oxide synthase phosphorylation but had no effect on endothelial cell internalization of insulin. Conclusions: Globular adiponectin increases muscle insulin uptake by recruiting muscle microvasculature, which contributes to its insulin-sensitizing action.
    Type of Medium: Online Resource
    ISSN: 0009-7330 , 1524-4571
    URL: Article
    DOI: 10.1161/CIRCRESAHA.111.300388
    RVK:
    XA 10000
    Language: English
    Publisher: Ovid Technologies (Wolters Kluwer Health)
    Publication Date: 2013
    detail.hit.zdb_id: 1467838-X
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