Amastatin, an inhibitor of aminopeptidase A, produced by Actinomycetes.

Aoyagi, Takaaki; Tobe, Hiroyasu; Kojima, Fukiko; Hamada, Masa; Takeuchi, Tomio; Umezawa, Hamao

doi:10.7164/antibiotics.31.636

Cited by 217 publications

(75 citation statements)

References 10 publications

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“…The inhibitors and their respective targets used in this study were amastatin, for aminopeptidase A (AP-A), Leu-AP, and triaminopeptidase [7] ; bestatin, for AP-B, Leu-AP, and triaminopeptidase [8]; leupeptin, for trypsin, plasmin, papain, and cathepsin B [91; esterastin, for esterase and lipase [10] ; and ebelactone B, for esterase, lipase, and formylmethionine aminopeptidase (f Met-AP) [11].…”

Section: Methodsmentioning

confidence: 99%

“…The ab- sorbance values actually measured were translated into these units from the standard curves which had been prepared in advance. For the assay of aminopeptidases and Post-Pro-Enz, the reaction mixture was prepared by mixing 0.25 ml of 2 mM j3-naphthylamide derivatives, and the absorbance at 525 nm of the final mixture was determined [7,8,12]. For the assays of CP-A, CP-B, and ACE, the reaction mixture was prepared by mixing 0.05 ml of 10 mM hippuryl derivatives, and the absorbance at 382 nm of the final mixture was determined [13][14][15].…”

Section: Methodsmentioning

confidence: 99%

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Bestatin Suppresses the Serum Levels of Several Hydrolytic Enzymes in a Patient with Progressive Muscular Dystrophy

Aoyagi

Wada

Kojima

et al. 1986

J. Clin. Biochem. Nutr.

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SummaryWe tested the effect of bestatin [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine] on the serum levels of various hydrolytic enzymes in a patient with progressive muscular dystrophy. Long-term administration of bestatin significantly suppressed the serum levels of aspartate aminopeptidase, arginine aminopeptidase, carboxypeptidase, alkaline phosphatase, and esterase. The results of multivariate study performed on the enzyme networks are compatible with the notion that this drug has a synchronizing effect on the movements of enzyme networks. Although in this middle-aged patient with an established disease the levels of enzymes of muscular origin were not significantly suppressed by this treatment, the present findings may warrant a therapeutic trial with this agent on young patients with initial symptoms of the disease.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Bestatin Suppresses the Serum Levels of Several Hydrolytic Enzymes in a Patient with Progressive Muscular Dystrophy

Aoyagi

Wada

Kojima

et al. 1986

J. Clin. Biochem. Nutr.

Self Cite

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“…After the reaction, the mixture was processed as described elsewhere [8][9][10][11][12], and the absorbance at 525 nm of the final mixture was then determined. For the ACE assay, 0.05 ml of 20 mM Pz-Gly-His-Leu, 0.4 ml of 0.5 M Tris-HC1 buffer, and 0.05 ml of the desired enzyme source were mixed.…”

Section: Methodsmentioning

confidence: 99%

Enzymatic Changes in Pancreas and Liver of the KK Mouse As an Animal Model of Diabetes Mellitus

Aoyagi

Wada

Kojima

et al. 1986

J. Clin. Biochem. Nutr.

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“…All subsequent experiments were performed using H-Glu-AMC-OH at 200μM and the reaction was allowed to proceed for 1 hour at 37°C. Brain tissue homogenates (triton X-100) (100ug total protein), or recombinant AP-A (serially diluted to produce a standard curve (400 -3.2 ng/ml)) were diluted in assay buffer (25mM Tris pH 8.0, 50mM CaCl2, 200uM NaCl) and incubated in the presence of amastatin-HCl a general aminopeptidase inhibitor [39] (10uM) (Enzo Life Sciences, Exeter, UK), or assay buffer alone, for 10 mins at 37°C prior to the addition of HGlu-AMC-OH (200uM diluted in assay buffer). The reaction was incubated at 37°C for 1 hour in the dark and fluorescence was read at an excitation/emission of 390/450nm using a using a FLUOstar OPTIMA plate reader (BMG labtech, Aylesbury, BUCKS, UK).…”

Section: Angiotensin-iii Direct Elisamentioning

confidence: 99%

Angiotensin-III is Increased in Alzheimer’s Disease in Association with Amyloid-β and Tau Pathology

Kehoe

Hibbs

Palmer

et al. 2017

JAD

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Hyperactivity of the renin-angiotensin system (RAS) is associated with the pathogenesis of Alzheimer's disease (AD) believed to be mediated by angiotensin-II (Ang-II) activation of the angiotensin type 1 receptor (AT1R). We previously showed that angiotensin-converting enzyme-1 (ACE-1) activity, the rate-limiting enzyme in the production of Ang-II, is increased in human postmortem brain tissue in AD. Angiotensin-III (Ang-III) activates the AT1R and angiotensin type-2 receptor (AT2R) but its potential role in the pathophysiology of AD remains unexplored. We measured Ang-II and Ang-III levels by ELISA, and the levels and activities of aminopeptidase-A (AP-A) and aminopeptidase-N (AP-N) (responsible for the production and metabolism of Ang-III respectively) in human post-mortem brain tissue in the mid-frontal cortex (Brodmann area 9) in a cohort of AD (n=90) and age-matched non-demented controls (n=59), for which we had previous measurements of ACE-1 activity, Aβ level and tau pathology (also in the mid-frontal cortex). We found that both Ang-II and Ang-III levels were significantly higher in AD compared to age-matched controls and that Ang-III, rather than Ang-II, was strongly associated with Aβ load and tau load.Levels of AP-A were significantly reduced in AD but AP-A enzyme activity was unchanged whereas AP-N activity was reduced in AD but AP-N protein level was unchanged. Together, these data indicate that the APA/Ang-III/APN/Ang-IV/AT4R pathway is dysregulated and that elevated Ang-III could contribute to the pathogenesis of AD.

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Amastatin, an inhibitor of aminopeptidase A, produced by Actinomycetes.

Cited by 217 publications

References 10 publications

Bestatin Suppresses the Serum Levels of Several Hydrolytic Enzymes in a Patient with Progressive Muscular Dystrophy

Bestatin Suppresses the Serum Levels of Several Hydrolytic Enzymes in a Patient with Progressive Muscular Dystrophy

Enzymatic Changes in Pancreas and Liver of the KK Mouse As an Animal Model of Diabetes Mellitus

Angiotensin-III is Increased in Alzheimer’s Disease in Association with Amyloid-β and Tau Pathology

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