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Sökning: WFRF:(Lopez Aparicio Pilar)

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1.
  • Hudson, Thomas J., et al. (författare)
  • International network of cancer genome projects
  • 2010
  • Ingår i: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 464:7291, s. 993-998
  • Tidskriftsartikel (refereegranskat)abstract
    • The International Cancer Genome Consortium (ICGC) was launched to coordinate large-scale cancer genome studies in tumours from 50 different cancer types and/or subtypes that are of clinical and societal importance across the globe. Systematic studies of more than 25,000 cancer genomes at the genomic, epigenomic and transcriptomic levels will reveal the repertoire of oncogenic mutations, uncover traces of the mutagenic influences, define clinically relevant subtypes for prognosis and therapeutic management, and enable the development of new cancer therapies.
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2.
  • Lopez-Aparicio, Pilar, et al. (författare)
  • Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets
  • 1992
  • Ingår i: Biochemical and Biophysical Research Communications. - 1090-2104. ; 186:1, s. 517-523
  • Tidskriftsartikel (refereegranskat)abstract
    • Insulin induced phosphorylation and activation of the cGMP inhibited cAMP phosphodiesterase (cGI-PDE) in human platelets were demonstrated after isolation of the enzyme with specific polyclonal cGI-PDE antibodies. The demonstration of this insulin effect required suppression of basal cGI-PDE phosphorylation, through the use of the protein kinase inhibitor H-7 (1-(5-isoquinolinylsulfonyl)-2-methylpiperazine). The human platelet insulin receptor beta-subunit, previously identified as a 97 kDa polypeptide, was detected with the use of wheat germ agglutinin chromatography and anti-phosphotyrosine antibodies. These results suggest that insulin, through phosphorylation/activation of cGI-PDE, could decrease cAMP/cAMP dependent protein kinase (cAMP-PK) activity and thereby make the platelets more sensitive towards aggregating agents.
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3.
  • Lopez-Aparicio, Pilar, et al. (författare)
  • Stimulation by insulin of a serine kinase in human platelets that phosphorylates and activates the cGMP-inhibited cAMP phosphodiesterase
  • 1993
  • Ingår i: Biochemical and Biophysical Research Communications. - : Elsevier BV. - 1090-2104 .- 0006-291X. ; 193:3, s. 1137-1144
  • Tidskriftsartikel (refereegranskat)abstract
    • We previously reported that insulin stimulation of human platelets induces serine phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase (cGI-PDE). Here, we describe methods to detect and partially purify an insulin-stimulated cGI-PDE kinase (cGI-PDE ISK) from lysates of platelets incubated with insulin. Incubation of human platelets with 10(-8) M insulin increased cGI-PDE ISK activity two-fold. The DEAE-Sephacel-purified cGI-PDE ISK phosphorylated the cGI-PDE on serine in a time- and concentration-dependent manner resulting in an increased incorporation of about 0.2 mol of [32P]/mol of cGI-PDE and 15-20% increase in cGI-PDE activity. The phosphorylation of cGI-PDE was not affected by 10 microM PKI, 1 microgram/ml of heparin, 3 mM CaCl2 or 1 mM MnCl2. cGI-PDE ISK did not adsorb to antiphosphotyrosine antibodies. To maintain its activation it was necessary to add protein phosphatase inhibitors to the lysate-buffers. All of these findings are consistent with the conclusion that a serine/threonine phosphorylation of the cGI-PDE ISK is involved in its activation by insulin.
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