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From www.bloodjournal.org by guest on June 17, 2017. For personal use only. Errata Nichol D, Shawber C, Fitch MJ, et al. Impaired angiogenesis and altered Notch signaling in mice overexpressing endothelial Egfl7. Blood. 2010;116(26):6133-6143. On page 6140 in the 23 December 2010 issue, there are errors in Figure 7A and 7C. In 7A, the DSL domain of Jagged, Serrate, Delta, and Lag-2 are not properly aligned with the putative DSL domain in EGFL7. In 7C, the Notch4 pull-down panels i and iv are the same; panel i was duplicated and used in both panels. In addition, the input and EGFL7 pull-down lanes in panel i are inverted. In the corrected figure, panels i and iv now also show the IgG bands for the EGFL7 pull-downs, and panels ii and iii show the lanes in the order they appear on the original blot. These changes do not in any way alter the results or the conclusion that EGFL7 directly interacts with endothelial Notch. The corrected Figure 7 and legend are shown. Figure 7. EGFL7 interacts with Notch receptors and regulates Notch target gene expression in vivo. (A) Alignment of the DSL domain of Jagged, Serrate, Delta, and Lag-2 with the putative DSL domain in EGFL7. Red letters represent the consensus sequence. (B) Yeast-2-hybrid assay (left panel): EGFL7 interacts with NOTCH4 and DLL4. Full-length EGFL7, DLL4, or the extracellular domain of NOTCH4 were fused to either the DNA-binding domain or the transcriptional activation domain of GAL4, and protein-protein interactions were monitored by the ability of the transformed yeast to grow on defined medium, and expression of ␣-galactosidase. Yeast-3-hybrid assay (right panels): EGFL7 abolishes NOTCH4-DLL4 interaction. The Egfl7 ORF was cloned downstream of a methionine repressible promoter (Met25) and transformed into a yeast strain expressing Notch4-GAL activating domain and DLL4-GAL4 DNA-binding domain fusions. Expression of ␣-galactosidase was then assayed on X-gal selection plates with or without methionine. (Ci-ii) Coimmunoprecipitation assays with protein extracts prepared from HEK293 cells transfected with plasmids encoding MYC/His-tagged-Egfl7 and Notch4 ECD or Notch1 ECD. (i) A NOTCH4 antibody was used to immunoprecipitate NOTCH4 ECD, and protein complexes were probed for NOTCH4 and EGFL7 by Western blot. (ii) A MYC antibody was used to immunoprecipitate EGFL7, and protein complexes were probed for NOTCH1 and EGFL7 by Western blot. (iii) Coimmunoprecipitation assay with protein extracts prepared from HUVECs infected with an adenovirus encoding MYC-tagged-Egfl7. A MYC antibody was used to immunoprecipitate EGFL7, and 6738 BLOOD, 16 JUNE 2011 䡠 VOLUME 117, NUMBER 24 From www.bloodjournal.org by guest on June 17, 2017. For personal use only. BLOOD, 16 JUNE 2011 䡠 VOLUME 117, NUMBER 24 ERRATA 6739 Demarest RM, Dahmane N, Capobianco AJ. Notch is oncogenic dominant in T-cell acute lymphoblastic leukemia. Blood. 2011;117(10):2901-2909. On page 2901 in the 10 March 2011 issue, there is an error in the second sentence of the “Introduction”; the statistics for T-ALL occurrence in adults and children with ALL were inverted. The sentence read, “T-ALL accounts for approximately 10% to 15% of adult and 25% of childhood ALL cases.” The sentence should have read: “T-ALL accounts for approximately 10% to 15% of childhood and 25% of adult ALL cases.” Li H, Malani N, Hamilton SR, et al. Assessing the potential for AAV vector genotoxicity in a murine model. Blood. 2011;117(12):3311-3319. On pages 3311 and 3314 in the 24 March 2011 issue, the word “cysteine” should be “cytosine.” In the “Abstract” on page 3311, the seventh sentence read, “Integration patterns in tumor tissue and adjacent normal tissue were similar to each other, showing preferences for active genes, cytosine-phosphate-guanosine islands, and guanosine/cysteine-rich regions.” The correct sentence should have read: “Integration patterns in tumor tissue and adjacent normal tissue were similar to each other, showing preferences for active genes, cytosine-phosphate-guanosine islands, and guanosine/cytosine-rich regions.” In “Results,” under the heading “Profiling of AAV2-hFIX16 vector integration sites,” the second sentence of the third paragraph on page 3314 read, “In normal liver tissue there was a preference for integrating near genes (P ⬍ .001), CpG islands (P ⬍ .05), and guanosine/cysteine-rich (G-C rich) regions (P ⬍ .05) (Figure 2B).” The correct sentence should have read: “In normal liver tissue there was a preference for integrating near genes (P ⬍ .001), CpG islands (P ⬍ .05), and guanosine/cytosine-rich (G-C rich) regions (P ⬍ .05; Figure 2B).” Figure 7. (continued) protein complexes were probed for NOTCH1 and EGFL7 by Western blot. (iv) Coimmunoprecipitation assays using protein lysates prepared from E12.5 embryos. An antibody against NOTCH4 was used to immunoprecipitate NOTCH4, and protein complexes were probed for NOTCH4 and EGFL7 by Western blot. Vertical lines have been inserted to indicate a repositioned gel lane. (D) Notch target gene expression in wild-type (䡺, n ⫽ 4) and Tie2-Egfl7 transgenic (f, n ⫽ 6) retinas. Gene expression was measured by quantitative RT-PCR and normalized to endothelial cell number using CD31 expression. (E) Notch target gene expression in wild-type (white bars, n ⫽ 6) and Tie2-Egfl7 transgenic embryos (black bars, n ⫽ 4). Data are represented as fold change compared with wild-type. *P ⬍ .05. From www.bloodjournal.org by guest on June 17, 2017. For personal use only. 2011 117: 6738-6739 doi:10.1182/blood-2011-04-348086 Nichol D, Shawber C, Fitch MJ, et al. Impaired angiogenesis and altered Notch signaling in mice overexpressing endothelial Egfl7. Blood. 2010;116(26):6133−6143. Updated information and services can be found at: http://www.bloodjournal.org/content/117/24/6738.full.html Articles on similar topics can be found in the following Blood collections Information about reproducing this article in parts or in its entirety may be found online at: http://www.bloodjournal.org/site/misc/rights.xhtml#repub_requests Information about ordering reprints may be found online at: http://www.bloodjournal.org/site/misc/rights.xhtml#reprints Information about subscriptions and ASH membership may be found online at: http://www.bloodjournal.org/site/subscriptions/index.xhtml Blood (print ISSN 0006-4971, online ISSN 1528-0020), is published weekly by the American Society of Hematology, 2021 L St, NW, Suite 900, Washington DC 20036. Copyright 2011 by The American Society of Hematology; all rights reserved.