7 results match your criteria: "Research Institute of the Vancouver Hospital and Health Sciences Center[Affiliation]"

Molecular cloning, biochemical and structural analysis of elongation factor-1 alpha from Leishmania donovani: comparison with the mammalian homologue.

Biochem Biophys Res Commun

March 2003

Department of Medicine, Division of Infectious Diseases, Faculty of Medicine, The Research Institute of the Vancouver Hospital and Health Sciences Center, The University of British Columbia, Vancouver, BC, Canada V5Z 3J5.

The Src-homology 2 domain containing protein tyrosine phosphatase-1 (SHP-1) is involved in the pathogenesis of infection with Leishmania. Recently, we identified elongation factor-1 alpha (EF-1 alpha) from Leishmania donovani as a SHP-1 binding and activating protein [J. Biol.

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The 19-kDa Mycobacterium tuberculosis protein induces macrophage apoptosis through Toll-like receptor-2.

J Immunol

March 2003

Department of Medicine, Division of Infectious Diseases, University of British Columbia, Faculty of Medicine and Science, The Research Institute of the Vancouver Hospital and Health Sciences Center, Vancouver, British Columbia, Canada.

Macrophages infected with Mycobacterium tuberculosis undergo increased rates of apoptosis. Important objectives are to define the microbial factors that cause apoptosis, the mechanisms involved and the impact on infection. The 19-kDa M.

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Leishmania EF-1alpha activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation.

J Biol Chem

December 2002

Department of Medicine, Division of Infectious Diseases, The University of British Columbia, Research Institute of the Vancouver Hospital and Health Sciences Center, Vancouver, British Columbia V5Z 3J5, Canada.

The human leishmaniasis are persistent infections of macrophages caused by protozoa of the genus Leishmania. The chronic nature of these infections is in part related to induction of macrophage deactivation, linked to activation of the Src homology 2 domain containing tyrosine phosphatase-1 (SHP-1) in infected cells. To investigate the mechanism of SHP-1 activation, lysates of Leishmania donovani promastigotes were subjected to SHP-1 affinity chromatography and proteins bound to the matrix were sequenced by mass spectrometry.

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1alpha,25-Dihydroxyvitamin D3-induced monocyte antimycobacterial activity is regulated by phosphatidylinositol 3-kinase and mediated by the NADPH-dependent phagocyte oxidase.

J Biol Chem

September 2001

Department of Medicine (Division of Infectious Diseases), University of British Columbia, Faculties of Medicine and Science, Research Institute of the Vancouver Hospital and Health Sciences Center, Vancouver, British Columbia V5Z 3J5, Canada.

We investigated the basis for the induction of monocyte antimycobacterial activity by 1alpha,25-dihydroxyvitamin D(3) (D(3)). As expected, incubation of Mycobacterium tuberculosis-infected THP-1 cells or human peripheral blood, monocyte-derived macrophages with hormone resulted in the induction of antimycobacterial activity. This effect was significantly abrogated by pretreatment of cells with either of the phosphatidylinositol 3-kinase (PI 3-K) inhibitors, wortmannin or LY294002, or with antisense oligonucleotides to the p110 subunit of PI 3-Kalpha.

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Article Synopsis
  • 1alpha,25-dihydroxyvitamin D(3) (D(3)) enhances the maturation of myeloid cells and increases surface markers CD14 and CD11b, indicating cell differentiation.
  • The activation of phosphatidylinositol 3-kinase (PI 3-kinase) is crucial for D(3)-induced CD14 and CD11b expression, as evidenced by the inhibition of these effects using specific PI 3-kinase inhibitors and antisense oligonucleotides.
  • Unlike CD14 and CD11b, the expression of the Cdk inhibitor p21 is not affected by the inhibitors, suggesting that PI 3-kinase's role in D
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Monocyte adherence induced by lipopolysaccharide involves CD14, LFA-1, and cytohesin-1. Regulation by Rho and phosphatidylinositol 3-kinase.

J Biol Chem

January 1999

Department of Medicine (Division of Infectious Diseases), The University of British Columbia, Faculties of Medicine and Science, The Research Institute of the Vancouver Hospital and Health Sciences Center, Vancouver, British Columbia V5Z 3J5, C.

Mechanisms regulating lipopolysaccharide (LPS)-induced adherence to intercellular adhesion molecule (ICAM)-1 were examined using THP-1 cells transfected with CD14-cDNA (THP-1wt). THP-1wt adherence to ICAM-1 was LPS dose-related, time-dependent, and inhibited by antibodies to either CD14 or leukocyte function associated antigen (LFA)-1, but was independent of any change in the number of surface expressed LFA-1 molecules. A potential role for phosphatidylinositol (PI) 3-kinase (PI 3-kinase) in LPS-induced adherence was examined using the PI 3-kinase inhibitors LY294002 and Wortmannin.

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The isoform identity of activated protein kinase C (PKC) and its regulation were investigated in bacterial lipopolysaccharide (LPS)-treated human monocytes. Resolution of detergent-soluble lysates prepared from LPS-treated, peripheral blood monocytes using Mono Q anion-exchange chromatography revealed two principal peaks of myelin basic protein kinase activity. Immunoblotting and immunoprecipitation with isoform-specific anti-PKC antibodies showed that the major and latest eluting peak is accounted for by PKC-zeta.

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