Potent homophthalimide-type inhibitors of B16F10/L5 mouse melanoma cell invasion.

@article{Kagechika1999PotentHI,
  title={Potent homophthalimide-type inhibitors of B16F10/L5 mouse melanoma cell invasion.},
  author={Hiroyuki Kagechika and Masato Komoda and Yasuyuki Fujimoto and Yukiko Koiso and Hisae Takayama and Shizuo Kadoya and K Miyata and Fuminori Kato and M Kato and Yuichi Hashimoto},
  journal={Biological \& pharmaceutical bulletin},
  year={1999},
  volume={22 9},
  pages={
          1010-2
        }
}
Recently, we developed a series of novel and potent aminopeptidase inhibitors with a homophthalimide skeleton. Among them, N-(2,6-diethylphenyl)homophthalimide (PIQ-22) possesses a specific aminopeptidase-inhibiting activity more potent than that of bestatin or actinonin, as assayed in terms of hydrolysis of L-alanine 4-methylcoumaryl-7-amide (Ala-AMC) by human acute lymphoblastic leukemia MOLT-4 cells. We show here that PIQ-22 and its 2,6-dimethylphenyl derivative (PIQ-11) are more potent… 

Specific nonpeptide inhibitors of puromycin-sensitive aminopeptidase with a 2,4(1H,3H)-quinazolinedione skeleton.

These potent and specific PSA inhibitors showed dose-dependent cell invasion-inhibitory activity in a Matrigel assay using mouse melanoma B16F10/L5 cells, in spite of their low cell toxicity.

Structural development of biological response modifiers based on thalidomide.

  • Y. Hashimoto
  • Biology, Medicine
    Bioorganic & medicinal chemistry
  • 2002

Aminopeptidase‐N/CD13 (EC 3.4.11.2) inhibitors: Chemistry, biological evaluations, and therapeutic prospects

An update on the biological and pharmacological profiles of known natural and synthetic APN inhibitors and current status on their potential use as therapeutic agents is discussed with regard to toxicity and specificity.

A Puromycin-Sensitive Aminopeptidase Is Essential for Meiosis in Arabidopsis thalianaw⃞

An Arabidopsis thaliana mutant (mpa1) is identified and characterized from a pool of T-DNA tagged lines that lacks PSA activity, revealing that both male and female meiosis are defective.

The Caenorhabditis elegans Orthologue of Mammalian Puromycin-sensitive Aminopeptidase Has Roles in Embryogenesis and Reproduction*

It is concluded that pam-1 encodes an aminopeptidase that clusters phylogenetically with the PSAs, despite attenuated sensitivity toward puromycin, and that it functions in embryo development and reproduction of the nematode.