Catálogo de publicaciones - revistas

<jats:title>Local macrophage clean-up</jats:title> <jats:p> Infection, especially by helminths or bacteria, can cause tissue damage (see the Perspective by Bouchery and Harris). Minutti <jats:italic>et al.</jats:italic> studied mouse models of helminth infection and fibrosis. They expressed surfactant protein A (a member of the complement component C1q family) in the lung, which enhanced interleukin-4 (IL-4)-mediated proliferation and activation of alveolar macrophages. This activation accelerated helminth clearance and reduced lung injury. In the peritoneum, C1q boosted macrophage activation for liver repair after bacterial infection. By a different approach, Bosurgi <jats:italic>et al.</jats:italic> discovered that after wounding caused by migrating helminths in the lung or during inflammation in the gut of mice, IL-4 and IL-13 act only in the presence of apoptotic cells to promote tissue repair by local macrophages. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1076" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aaj2067">1076</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1072" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aai8132">1072</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1014" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aan6782">1014</jats:related-article> </jats:p>

<jats:title>Local macrophage clean-up</jats:title> <jats:p> Infection, especially by helminths or bacteria, can cause tissue damage (see the Perspective by Bouchery and Harris). Minutti <jats:italic>et al.</jats:italic> studied mouse models of helminth infection and fibrosis. They expressed surfactant protein A (a member of the complement component C1q family) in the lung, which enhanced interleukin-4 (IL-4)-mediated proliferation and activation of alveolar macrophages. This activation accelerated helminth clearance and reduced lung injury. In the peritoneum, C1q boosted macrophage activation for liver repair after bacterial infection. By a different approach, Bosurgi <jats:italic>et al.</jats:italic> discovered that after wounding caused by migrating helminths in the lung or during inflammation in the gut of mice, IL-4 and IL-13 act only in the presence of apoptotic cells to promote tissue repair by local macrophages. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1076" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aaj2067">1076</jats:related-article> , p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1072" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aai8132">1072</jats:related-article> ; see also p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1014" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aan6782">1014</jats:related-article> </jats:p>

<jats:title>Polycomb steps to inactivate X</jats:title> <jats:p> XX females silence one of their X chromosomes. This involves a process whereby a noncoding RNA known as Xist coats one of the X chromosomes and recruits chromatin silencing factors. The Polycomb complexes PRC1 and PRC2 are also known to be involved in X chromosome inactivation. Almeida <jats:italic>et al.</jats:italic> elucidate a key role of a specific complex, PCGF3/5-PRC1, in initiating Polycomb recruitment by Xist RNA. They further demonstrate that Polycomb recruitment is critical for Xist-mediated chromosome silencing and female embryogenesis. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1081" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aal2512">1081</jats:related-article> </jats:p>

<jats:title>A clue to a drug's neurotoxicity?</jats:title> <jats:p> The drug BIA 10-2474 inhibits fatty acid amide hydrolase (FAAH), a lipase that degrades a specific endocannabinoid. On the basis of this activity, BIA 10-2474 was being developed as a potential treatment for anxiety and pain. In a phase 1 trial of the drug, one subject died, and four others suffered brain damage. As an initial step in investigating whether inhibition of off-target proteins by BIA 10-2474 might contribute to its clinical neurotoxicity, van Esbroeck <jats:italic>et al.</jats:italic> used activity-based proteomic assays to identify proteins targeted by the drug. Studying human cells and brain samples from subjects not associated with the trial, they found that BIA 10-2474 targeted several different lipases in addition to FAAH. It also substantially altered lipid metabolism in cultured neurons. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6342" page="1084" related-article-type="in-this-issue" vol="356" xlink:href="10.1126/science.aaf7497">1084</jats:related-article> </jats:p>

<jats:p>A weekly roundup of information on newly offered instrumentation, apparatus, and laboratory materials of potential interest to researchers.</jats:p>