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By Gaetano Santulli

ISBN-10: 1626181144

ISBN-13: 9781626181144

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G. PDGF-A to D). The classical PDGFs include homo and heterodimeric associations of the A and B chains, forming PDGF AA, BB and AB respectively. The A and B polypeptides share similar protein domains, and are secreted as fully active factors. Like VEGF, these classical PDGFs also contain “retention matrix” motifs that allow them to interact with extracellular matrix proteins and regulate their biological availability to specific sites. [2, 12, 107, 108] Signaling occurs by three receptors tyrosine kinases resulting from the association of two transmembrane polypeptides: PDFGR-alpha and beta that also function as homo and heterodimers.

Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis. Science 1997;277:55-60. [99] Gale NW, Thurston G, Hackett SF et al. Angiopoietin-2 is required for postnatal angiogenesis and lymphatic patterning, and only the latter role is rescued by Angiopoietin-1. Dev Cell 2002;3:411-23. [100] Akhurst RJ. A sweet link between TGFbeta and vascular disease? Nat Genet 2006;38:400-1. [101] Chen YG, Hata A, Lo RS et al. Determinants of specificity in TGF-beta signal transduction.

Nat Med 2000;6:460-3. [95] Xu Y, Yu Q. Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide region. J Biol Chem 2001;276:34990-8. [96] Carlson TR, Feng Y, Maisonpierre PC, Mrksich M, Morla AO. Direct cell adhesion to the angiopoietins mediated by integrins. J Biol Chem 2001;276:26516-25. [97] Gale NW, Yancopoulos GD. Growth factors acting via endothelial cell-specific receptor tyrosine kinases: VEGFs, angiopoietins, and ephrins in vascular development.

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Angiogenesis: Insights from a Systematic Overview by Gaetano Santulli


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