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dc.contributor.authorVargas, Micaela
dc.contributor.authorKaramsetty, Raghavendra
dc.contributor.authorLeppla, Stephen H.
dc.contributor.authorChaudry, G. Jilani
dc.date.accessioned2013-11-22T23:20:31Z
dc.date.available2013-11-22T23:20:31Z
dc.date.issued2012-08
dc.identifier.bibliographicCitationVargas M, Karamsetty R, Leppla SH, Chaudry GJ (2012) Broad Expression Analysis of Human ANTXR1/TEM8 Transcripts Reveals Differential Expression and Novel Splizce Variants. PLoS ONE 7(8): e43174. doi:10.1371/journal.pone.0043174en_US
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/10027/10650
dc.description© 2012 Vargas et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The original version is available through Public Library of Science at DOI: 10.1371/journal.pone.0043174en_US
dc.description.abstractTumor endothelial marker 8 (TEM8; ANTXR1) is one of two anthrax toxin receptors; the other is capillary morphogenesis gene 2 protein (CMG2; ANTXR2). TEM8 shows enhanced expression in certain tumor endothelia, and is thought to be a player in tumor vasculature formation. However, a comprehensive expression profile of individual TEM8 variants in normal or cancerous tissues is lacking. In this work we carried out an extensive analysis of all splice variants of human TEM8 in 12 digestive tissues, and 8 each fetal and adult tissues, 6 of them cognate pairs. Using variant-specific primers, we first ascertained the status of full-length transcripts by nested PCR. We then carried out quantitative analysis of each transcript by real-time PCR. Three splice variants of TEM8 were reported before, two single-pass integral membrane forms (V1 and V2) and one secreted (V3). Our analysis has revealed two new variants, one encoding a membrane-bound form of the receptor and the other secreted, which we have designated V4 and V5, respectively. All tissues had V1, V2, V3, and V4, but only prostate had V5. Real-time PCR revealed that all variants are present at different levels in various tissues. V3 appeared the most abundant of all. To ascertain its functionality for anthrax toxin, we expressed the newly identified form V4 in a receptornegative host cell, and included V1 and V2 for comparison. Cytotoxicity, toxin binding, and internalization assays showed V4 to be as efficient a receptor as V1 and V2.en_US
dc.description.sponsorshipFunding for this work was provided to GJC by The University of Texas at San Antonio, San Antonio Area Foundation, and National Institute of Allergy and Infectious Diseases/National Institute of General Medical Sciences grant SC1AI081654 (Minority Biomedical Research Support-Support of Competitive Research). MV was supported for her PhD by the Minority Biomedical Research Support-Research Initiative for Scientific Enhancement grant GM60655 to the University of Texas at San Antonio.en_US
dc.language.isoen_USen_US
dc.publisherPublic Library of Scienceen_US
dc.subjectTumor endothelialen_US
dc.subjectanthraxen_US
dc.titleBroad Expression Analysis of Human ANTXR1/TEM8 Transcripts Reveals Differential Expression and Novel Splizce Variantsen_US
dc.typeArticleen_US


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