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Literature summary for 3.4.21.68 extracted from

  • Su, L.; Xu, X.; Zhao, H.; Gu, Q.; Zou, H.
    In vitro and in vivo antiangiogenic activity of a novel deca-peptide derived from human tissue-type plasminogen activator kringle 2 (2010), Biochem. Biophys. Res. Commun., 396, 1012-1017.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information a synthetic deca-peptide corresponding to the amino acid sequence Arg54-Trp63 of human tissue-type plasminogen activator kringle 2 domain, named TKII-10, is produced and tested for its ability to inhibit endothelial cell proliferation, migration, tube formation in vitro, and angiogenesis in vivo. Another peptide TKII-10S, composed of the same 10 amino acids as TKII-10 but in a different sequence, is also produced and tested, showing that TKII-10 potently inhibits VEGF-stimulated endothelial cell migration and tube formation in a dose-dependent, as well as sequence-dependent manner in vitro while it is inactive in inhibiting endothelial cell proliferation. Furthermore, TKII-10 potently inhibits angiogenesis in chick chorioallantoic membrane and mouse cornea. The middle four amino acids DGDA in their sequence play an important role in TKII-10 angiogenesis inhibition Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
t-PA
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Homo sapiens
Tissue-type plasminogen activator
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Homo sapiens

General Information

General Information Comment Organism
additional information the synthetic deca-peptide corresponding to the amino acid sequence Arg54-Trp63 of human tissue-type plasminogen activator kringle 2 domain, i.e. TKII-10, effectively inhibits VEGF-stimulated HUVECs migration and tube formation, but it demonstrats no inhibitory effect on VEGF-stimulated HUVECs proliferation, overview. TKII-10 effectively inhibits angiogenesis in vivo Homo sapiens