Hormonal regulation of dipeptidyl-aminopeptidase I activity in cultured human fibroblasts

Davis, Martin

doi:10.1016/0003-9861(87)90129-9

Cited by 2 publications

(2 citation statements)

References 15 publications

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“…That this enzyme, which had a digitonin solubilization profile comparable to that of the lysosomal marker enzyme, is inactivated by cysteine peptidase inhibitors and by diprotin B, appears not to cleave Boc-Ala-Ala-pNA or Ala-pNA supports the hypothesis that cleavage of Ala-Ala-pNA is due to a cysteine-type dipeptidyl aminopeptidase. Dipeptidyl aminopeptidases have been detected and characterized in other organisms (Davis, 1987;Hui, 1988), although, to our knowledge, this is the first evidence for the occurrence of such an enzyme in a trypanosomatid. Cleavage of Boc-Ala-Ala-pNA, on the other hand, has characteristics of a cytosolic serine peptidase.…”

Section: Discussionmentioning

confidence: 74%

Detection of peptidases inTrypanosoma cruziepimastigotes using chromogenic and fluorogenic substrates

et al. 1992

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SUMMARYDetergent extracts of Trypanosoma cruzi epimastigotes catalysed the hydrolysis of a range of amino-acyl and peptidyl />-nitro-anilides and aminomethylcoumarins. At least three enzymes were detected that cleave Z-Phe-Arg-MCA. Two of these were optimally active at alkaline pH, the other at pH 4-0. Of the two enzymes with alkaline pH optima, one was a cysteine peptidase and was unable to cleave Bz-Arg-MCA readily, whilst the other cleaved Bz-Arg-MCA and was inhibited by diisopropyl fluorophosphate. The acidic enzyme was similar to cathespin L of other eukayrotes with respect to its pH profile, substrate-specificity and inhibitor-sensitivity. Evidence was presented that epimastigotes contain a cysteine-type dipeptidyl aminopeptidase, one or more aminopeptidases, and a serine peptidase that cleaves Boc-AlaAla-pNA. Digitonin solubilization of the activities from cells supports the hypothesis that the cathespin L-like enzyme and the dipeptidyl aminopeptidase are lysosomal, whilst the Bz-Arg-MCA hydrolase, the aminopeptidases and the Boc-Ala-Ala-pNA serine peptidase are cytosolic.

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Section: Discussionmentioning

confidence: 74%

Detection of peptidases inTrypanosoma cruziepimastigotes using chromogenic and fluorogenic substrates

et al. 1992

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“…The induction of brush border enzymes such as aminopeptidase N (EC 3.4.11.2) in the small intestine of developing animals by corticosteroids is well known [21]. Corticosteroids increase also the activities of such as angiotensin converting enzyme (ACE) in rabbit macrophages in cultures [22] and cathepsin C in cultured human fibroblasts [23]. In addition, physiological levels of cortisol (30 nM to 3 µM) increased aminopeptidase N, P-LAP and APA activities in placental tissue culture [24].…”

Section: Relationship Among Sex Steroids Aps and Fetal Peptide Hormomentioning

confidence: 99%

New Insights into the Role of Sex Steroid Hormones in Pregnancy: Possible Therapeutic Approach by Sex Steroid Hormones for the Treatment of Both Preeclampsia and Preterm Labor

Mizutani

2015

Exp Clin Endocrinol Diabetes

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Fetal peptide hormones are essential for the development of fetus, which increase in accordance with pregnancy term. Concentration of these hormones within the feto-placental unit is normally higher than that of maternal circulation. Since these hormones are biologically active, the leakage of these hormones into the maternal circulation is regulated by degradation activity by placental aminopeptidases, in order to maintain the balance between carriage of pregnancy and onset of labor.Because the concentration of these hormones, being regulated by the amount of endogenous production and by physiological degradation by enzymes in the blood and tissue, the balance between production and degradation is a definitive element for maintaining normal gestation and term delivery.The changes of the balance between fetal angiotensin II (A-II) and vasopressin (AVP) andA-II and AVP degrading enzymes, between aminopeptidase A (APA) and placental leucine aminopeptidase( P-LAP) - in the placenta and maternal blood due to fetal stress such as hypoxia - are the provable causes of preeclampsia or preterm labor.Induction of APA and P-LAP by estradiol benzoate (E2) and progesterone (P) from placenta has been demonstrated. They are involved in the regulation of fetal peptide hormones via placental aminopeptidases in homeostasis of pregnancy.Recently it was shown that both APA and P-LAP could be potentially safe and effective drugs for preeclampsia and preterm labor. The authors' proposed sex steroid treatment with dose increasing manner by gestational week (sex steroid treatment) for severe preeclampsia and preterm labor could be candidates replacing conventional treatments. In light of lacking safe and effective medication, the proposed sex steroid treatment is worthwhile for the prospective controlled studies for the treatment of both preeclampsia and preterm labor.

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Hormonal regulation of dipeptidyl-aminopeptidase I activity in cultured human fibroblasts

Cited by 2 publications

References 15 publications

Detection of peptidases inTrypanosoma cruziepimastigotes using chromogenic and fluorogenic substrates

Detection of peptidases inTrypanosoma cruziepimastigotes using chromogenic and fluorogenic substrates

New Insights into the Role of Sex Steroid Hormones in Pregnancy: Possible Therapeutic Approach by Sex Steroid Hormones for the Treatment of Both Preeclampsia and Preterm Labor

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