Disease relevance of Arphamenine A

• Arphamenine A was synthesized in a cell-free system obtained from the arphamenine-producing strain, Chromobacterium violaceum BMG361-CF4 [1].

High impact information on Arphamenine A

• Actinonin was a tight binding competitive inhibitor (K(i) approximately 1 nm), whereas arphamenine A (K(i) approximately 70 microm) and L-leucinol (K(i) approximately 100 microm) were non-tight binding competitive inhibitors [2].
• All ketomethylene isosteres examined were weak inhibitors of both leucine aminopeptidase and aminopeptidase M. However, the ketomethylene inhibitor LysK(RS)Phe (58) (Ki = 4 nM) is a potent inhibitor comparable to the natural product, arphamenine A (ArgKPhe; Ki = 2.5 nM) [3].
• Separation of enkephalin-degrading enzymes from longitudinal muscle layer of bovine small intestine. Enzyme inhibition by arphamenine A [4].
• Among them, arphamenine A, a new potent inhibitor for aminopeptidase B, was shown to be a useful compound in inhibiting all of the enkephalin-degrading enzymes in small intestine [4].
• In control and TGF-beta1-treated cardiac fibroblasts, 100 micromol/L leuhistin or arphamenine A only partially inhibited alanine aminopeptidase activity, whereas bestatin (100 micromol/L) completely inhibited the alanine aminopeptidase activity [5].

Anatomical context of Arphamenine A

• The angiotensin II-stimulated collagen gel contraction in control and TGF-beta1-treated fibroblasts was almost completely reversed by leuhistin and arphamenine A (100 micromol/L) [5].

Associations of Arphamenine A with other chemical compounds

• Cardiac fibroblasts from passage 2 from normal male adult rats were cultured to confluency and incubated with and without 600 pmol/l TGF-ss1 for 2 days in serum-free Dulbecco's modified Eagle's medium and then incubated with 100 mol/l arphamenine A for 1 day in this medium with added ascorbic acid, ss-aminopropionitrile and titriated proline [6].

Gene context of Arphamenine A

• Lysyl oxidase, MMP-1 and MMP-2 activity were inhibited by arphamenine A in the conditioned media of control and TGF-ss1-treated cardiac fibroblasts [6].
• Arginine aminopeptidase activity was only partially inhibited by leuhistin and arphamenine A at 100 micromol/L in control and TGF-beta1-treated fibroblasts [5].
• To determine whether the aminopeptidase B inhibitor, arphamenine A, could affect collagen production and expression in control and TGF-ss1-treated cardiac fibroblasts [6].

References