Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.68 extracted from

  • Kim, H.; Joe, Y.
    DGDA, a local sequence of the kringle 2 domain, is a functional motif of the tissue-type plasminogen activators antiangiogenic kringle domain (2010), Biochem. Biophys. Res. Commun., 391, 166-169.
    View publication on PubMed
Search for more literature for 3.4.21.68

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the kringle domains 1 and 2 of tissue-type plasminogen activator, TK1–2, interact with endothelial vein cells via integrin and the kringle domain DGDA amino acid sequence, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the kringle domains 1 and 2 of tissue-type plasminogen activator, TK1–2, interact with endothelial vein cells via integrin and the kringle domain DGDA amino acid sequence, overview Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
Tissue-type plasminogen activator
-
 Homo sapiens

General Information

General Information Comment Organism
additional information the DGDA sequence presents a functional epitope of TK1–2 and can be used as a potential novel antiangiogenic peptide Homo sapiens
physiological function antiangiogenic activity can be elicited by the kringle domains 1 and 2 of tissue-type plasminogen activator, TK1–2, or the kringle 2 domain alone, overview. The anti-migratory effect of TK1–2 is mediated in part by its interference with integrin alpha2beta1, which is blocked by the Asp-Gly-Glu-Ala, DGDA, amino acid sequence, the DGDA peptide alone shows antiangiogenic activity and effectively inhibites VEGF-induced migration of HUVECs Homo sapiens