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Purpurin Inhibits Adipocyte-Derived Leucine Aminopeptidase and Angiogenesis in a Zebrafish Model

Purpurin Inhibits Adipocyte-Derived Leucine Aminopeptidase and Angiogenesis in a Zebrafish Model

Hyomi Park, Joong Sup Shim, Beom Seok Kim, Hye Jin Jung, Tae-Lin Huh, Ho Jeong Kwon

Biochem Biophys Res Commun. 2014 Jul 18;450(1):561-7.

PMID: 24928393

Abstract:

Adipocyte-derived leucine aminopeptidase (A-LAP) is a novel member of the M1 family of zinc metallopeptidases, which has been reported to play a crucial role in angiogenesis. In the present study, we conducted a target-based screening of natural products and synthetic chemical libraries using the purified enzyme to search novel inhibitors of A-LAP. Amongst several hits isolated, a natural product purpurin was identified as one of the most potent inhibitors of A-LAP from the screening. In vitro enzymatic analyses demonstrated that purpurin inhibited A-LAP activity in a non-competitive manner with a Ki value of 20 M. In addition, purpurin showed a strong selectivity toward A-LAP versus another member of M1 family of zinc metallopeptidase, aminopeptidase N (APN). In angiogenesis assays, purpurin inhibited the vascular endothelial growth factor (VEGF)-induced invasion and tube formation of human umbilical vein endothelial cells (HUVEC). Moreover, purpurin inhibited in vivo angiogenesis in zebrafish embryo without toxicity. These data demonstrate that purpurin is a novel specific inhibitor of A-LAP and could be developed as a new anti-angiogenic agent.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP81549	Purpurin		81-54-9	Price

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