CLT1 targets angiogenic endothelium through CLIC1 and fibronectin View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2012-03

AUTHORS

Lynn M. Knowles, Gunjan Malik, Brian L. Hood, Thomas P. Conrads, Jan Pilch

ABSTRACT

Angiogenesis is important for tumor growth and metastasis. CLT1 (CGLIIQKNEC), a peptide that binds to tumor interstitial spaces in the presence of fibrin-fibronectin, has structural similarity to the anti-angiogenic β-sheet peptides anastellin and anginex. This similarity is reflected in the ability of CLT1 to form co-aggregates with fibronectin that induce an unfolded protein response and cause autophagic cell death in proliferating endothelial cells. CLT1 cytotoxicity is mediated at least in parts by a novel CLT1 binding protein, Chloride Intracellular Channel 1 (CLIC1), which promotes internalization of CLT1-fibronectin co-aggregates in a mechanism that depends on the LIIQK amino acid sequence of CLT1. LIIQK encompasses amino acid residues relevant for CLT1 binding to CLIC1 and in addition, facilitates the formation of CLT1-fibronectin co-aggregates, which in turn promote translocation of CLIC1 to the endothelial cell surface through ligation of integrin αvβ3. Paralleling the in vitro results, we found that CLT1 co-localizes with CLIC1 and fibronectin in angiogenic blood vessels in vivo, and that CLT1 treatment inhibited angiogenesis and tumor growth. Our findings show that CLT1 is a new anti-angiogenic compound, and its mechanism of action is to form co-aggregates with fibronectin, which bind to angiogenic endothelial cells through integrins, become internalized through CLIC1 and elicit a cytotoxic unfolded protein response. The simple structure and high potency of CLT1 make it a potentially useful compound for anti-angiogenic treatments. More... »

PAGES

115-129

Journal

TITLE

Angiogenesis

ISSUE

1

VOLUME

15

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s10456-011-9247-8

    DOI

    http://dx.doi.org/10.1007/s10456-011-9247-8

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1037596536

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/22203240


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