Literature DB >> 12897135

Potential role for ADAM15 in pathological neovascularization in mice.

Keisuke Horiuchi1, Gisela Weskamp, Lawrence Lum, Hans-Peter Hammes, Hui Cai, Thomas A Brodie, Thomas Ludwig, Riccardo Chiusaroli, Roland Baron, Klaus T Preissner, Katia Manova, Carl P Blobel.   

Abstract

ADAM15 (named for a disintegrin and metalloprotease 15, metargidin) is a membrane-anchored glycoprotein that has been implicated in cell-cell or cell-matrix interactions and in the proteolysis of molecules on the cell surface or extracellular matrix. To characterize the potential roles of ADAM15 during development and in adult mice, we analyzed its expression pattern by mRNA in situ hybridization and generated mice carrying a targeted deletion of ADAM15 (adam15(-/-) mice). A high level of expression of ADAM15 was found in vascular cells, the endocardium, hypertrophic cells in developing bone, and specific areas of the hippocampus and cerebellum. However, despite the pronounced expression of ADAM15 in these tissues, no major developmental defects or pathological phenotypes were evident in adam15(-/-) mice. The elevated levels of ADAM15 in endothelial cells prompted an evaluation of its role in neovascularization. In a mouse model for retinopathy of prematurity, adam15(-/-) mice had a major reduction in neovascularization compared to wild-type controls. Furthermore, the size of tumors resulting from implanted B16F0 mouse melanoma cells was significantly smaller in adam15(-/-) mice than in wild-type controls. Since ADAM15 does not appear to be required for developmental angiogenesis or for adult homeostasis, it may represent a novel target for the design of inhibitors of pathological neovascularization.

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Year:  2003        PMID: 12897135      PMCID: PMC166329          DOI: 10.1128/MCB.23.16.5614-5624.2003

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN: 0270-7306            Impact factor:   4.272


  79 in total

1.  Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2.

Authors:  H Sato; T Kinoshita; T Takino; K Nakayama; M Seiki
Journal:  FEBS Lett       Date:  1996-09-09       Impact factor: 4.124

2.  Activated Notch4 inhibits angiogenesis: role of beta 1-integrin activation.

Authors:  Kevin G Leong; Xiaolong Hu; Linheng Li; Michela Noseda; Bruno Larrivée; Christopher Hull; Leroy Hood; Fred Wong; Aly Karsan
Journal:  Mol Cell Biol       Date:  2002-04       Impact factor: 4.272

3.  Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence.

Authors:  J Krätzschmar; L Lum; C P Blobel
Journal:  J Biol Chem       Date:  1996-03-01       Impact factor: 5.157

4.  Subcutaneous injection of a cyclic peptide antagonist of vitronectin receptor-type integrins inhibits retinal neovascularization.

Authors:  H P Hammes; M Brownlee; A Jonczyk; A Sutter; K T Preissner
Journal:  Nat Med       Date:  1996-05       Impact factor: 53.440

5.  KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis.

Authors:  J Rooke; D Pan; T Xu; G M Rubin
Journal:  Science       Date:  1996-08-30       Impact factor: 47.728

Review 6.  Vascular endothelial growth factor and its receptors.

Authors:  M Klagsbrun; P A D'Amore
Journal:  Cytokine Growth Factor Rev       Date:  1996-10       Impact factor: 7.638

7.  The cell surface metalloprotease/disintegrin Kuzbanian is required for axonal extension in Drosophila.

Authors:  D Fambrough; D Pan; G M Rubin; C S Goodman
Journal:  Proc Natl Acad Sci U S A       Date:  1996-11-12       Impact factor: 11.205

8.  Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life.

Authors:  Gisela Weskamp; Hui Cai; Thomas A Brodie; Shigeki Higashyama; Katia Manova; Thomas Ludwig; Carl P Blobel
Journal:  Mol Cell Biol       Date:  2002-03       Impact factor: 4.272

9.  Notch4/int-3, a mammary proto-oncogene, is an endothelial cell-specific mammalian Notch gene.

Authors:  H Uyttendaele; G Marazzi; G Wu; Q Yan; D Sassoon; J Kitajewski
Journal:  Development       Date:  1996-07       Impact factor: 6.868

10.  MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains.

Authors:  G Weskamp; J Krätzschmar; M S Reid; C P Blobel
Journal:  J Cell Biol       Date:  1996-02       Impact factor: 10.539

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  54 in total

1.  ADAM15 protein amplifies focal adhesion kinase phosphorylation under genotoxic stress conditions.

Authors:  Dorothee Fried; Beate B Böhm; Kristin Krause; Harald Burkhardt
Journal:  J Biol Chem       Date:  2012-04-27       Impact factor: 5.157

2.  Pathological neovascularization is reduced by inactivation of ADAM17 in endothelial cells but not in pericytes.

Authors:  Gisela Weskamp; Karen Mendelson; Steve Swendeman; Sylvain Le Gall; Yan Ma; Stephen Lyman; Akinari Hinoki; Satoru Eguchi; Victor Guaiquil; Keisuke Horiuchi; Carl P Blobel
Journal:  Circ Res       Date:  2010-01-28       Impact factor: 17.367

3.  ADAM15 disintegrin is associated with aggressive prostate and breast cancer disease.

Authors:  Rainer Kuefer; Kathleen C Day; Celina G Kleer; Michael S Sabel; Matthias D Hofer; Sooryanarayana Varambally; Christoph S Zorn; Arul M Chinnaiyan; Mark A Rubin; Mark L Day
Journal:  Neoplasia       Date:  2006-04       Impact factor: 5.715

4.  ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling.

Authors:  Karina Reiss; Thorsten Maretzky; Andreas Ludwig; Thomas Tousseyn; Bart de Strooper; Dieter Hartmann; Paul Saftig
Journal:  EMBO J       Date:  2005-02-03       Impact factor: 11.598

5.  L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth.

Authors:  Thorsten Maretzky; Marc Schulte; Andreas Ludwig; Stefan Rose-John; Carl Blobel; Dieter Hartmann; Peter Altevogt; Paul Saftig; Karina Reiss
Journal:  Mol Cell Biol       Date:  2005-10       Impact factor: 4.272

6.  ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation.

Authors:  Thorsten Maretzky; Karina Reiss; Andreas Ludwig; Julian Buchholz; Felix Scholz; Erhardt Proksch; Bart de Strooper; Dieter Hartmann; Paul Saftig
Journal:  Proc Natl Acad Sci U S A       Date:  2005-06-15       Impact factor: 11.205

7.  Expression of ADAM15 in lung carcinomas.

Authors:  A Schütz; W Härtig; M Wobus; J Grosche; Ch Wittekind; G Aust
Journal:  Virchows Arch       Date:  2005-03-09       Impact factor: 4.064

8.  An Adam15 amplification loop promotes vascular endothelial growth factor-induced ocular neovascularization.

Authors:  Bing Xie; Jikui Shen; Aling Dong; Mara Swaim; Sean F Hackett; Lorenza Wyder; Susanne Worpenberg; Samuel Barbieri; Peter A Campochiaro
Journal:  FASEB J       Date:  2008-04-01       Impact factor: 5.191

9.  ADAM15 Participates in Tick-Borne Encephalitis Virus Replication.

Authors:  Qi Yang; Rongjuan Pei; Yun Wang; Yuan Zhou; Min Yang; Xinwen Chen; Jizheng Chen
Journal:  J Virol       Date:  2021-01-28       Impact factor: 5.103

10.  A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src family kinase activity.

Authors:  Chongxiu Sun; Mack H Wu; Eugene S Lee; Sarah Y Yuan
Journal:  Arterioscler Thromb Vasc Biol       Date:  2012-08-16       Impact factor: 8.311

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