Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C1519670 (tumor angiogenesis)
6,052 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endosialin (tumor endothelial marker 1) is expressed preferentially by tumor endothelial cells but not by normal endothelium. Its protein domain architecture is homologous to that of CD93 and thrombomodulin (CD141), suggesting a similar function in mediating cell-cell interactions. The aim of this study was to investigate the expression pattern of endosialin in human brain tumors in a bid to decipher its contribution to tumor angiogenesis. We generated an antibody specifically recognizing human endosialin and used it to study endosialin expression in 30 human brain tumor specimens by immunoblotting and immunohistochemistry. Twenty of 30 tumors expressed endosialin in a heterogeneous manner. The largest proportion of endosialin-expressing tumors was found in highly invasive glioblastoma multiforme, anaplastic astrocytomas, and metastatic carcinomas. Endosialin was localized to the endothelium of small and large vessels strongly stained for CD31 and was also expressed by Thy-1-positive fibroblast-like cells close to the meninges and alpha-smooth muscle actin-positive cells in some vessels. Endosialin colocalized with thrombomodulin, suggesting the proteins may have complementary functions in tumor progression.
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PMID:Human endosialin (tumor endothelial marker 1) is abundantly expressed in highly malignant and invasive brain tumors. 1562 64

The inhibition of tumor angiogenesis is one of the main challenges in cancer therapy. With the aim of developing monoclonal antibodies able to inhibit angiogenesis, we immunized mice with proliferating human umbilical vein endothelial cells. We generated a library of monoclonal antibodies able to recognize antigens expressed on endothelial cells and screened the antibodies for their ability to inhibit endothelial cell proliferation, migration, and sprouting in vitro. Here, we show that the antibody, designated as 4E1, is able to neutralize the formation of new vessels both in vitro and in vivo without affecting endothelial cell survival. By mass spectrometry we identified CD93 as the antigen bound by 4E1 and mapped the recognized epitope. CD93 is a transmembrane protein heavily glycosylated preferentially expressed in the vascular endothelium. CD93 silencing by lentiviral-mediated small hairpin RNA expression impairs human endothelial cell proliferation, migration, and sprouting. Altogether these findings reveal 4E1 as a novel antiangiogenic antibody and identify CD93 as a new target suitable for antiangiogenic therapy.
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PMID:The characterization of a novel monoclonal antibody against CD93 unveils a new antiangiogenic target. 2480 68

Lung cancer, especially non-small cell lung cancer (NSCLC), is the most common malignant tumor associated with poor prognosis. Angiogenesis plays a vital role in NSCLC, and could be used in tumor staging and therapy evaluation. CD93 (C1q receptor) is reportedly a key regulator of tumor angiogenesis. In the present study, the efficacy and specificity of a 125I-labeled CD93-specific monoclonal antibody (125I-anti-CD93 mAb) in detecting NSCLC xenografts were analyzed, and the association between CD93 expression and 125I-anti-CD93 mAb uptake by tumors was evaluated. The targeting ability of 125I-anti-CD93 mAb enabled its rapid, continuous and highly specific accumulation in CD93-expressing tumors in vivo. These results revealed the potential applicability of 125I-anti-CD93 mAb for non-invasive imaging diagnosis of CD93-positive NSCLC.
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PMID:Radioimmunoimaging of 125I-labeled anti-CD93 monoclonal antibodies in a xenograft model of non-small cell lung cancer. 3181 75