Clinical studies on the balance between isooxytocinases in the blood of pregnant women

Klimek, R

doi:10.1016/0009-8981(68)90155-1

Cited by 12 publications

(5 citation statements)

References 7 publications

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“…Oxytocinases (cystine aminopeptidases) have been studied by Yman (1970), Klimek (1968 and Klimek & Malolepszy (1968) in human blood and serum. Aminopeptidase A (Nagatsu et al, 1970) and angiotensinase (an aminopeptidase) were studied in plasma (Kurtz & Wachsmuth, 1969), and several other aminopeptidases were demonstrated in platelets (Greiff et al, 1969).…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of two human erythrocyte arylamidases preferentially hydrolysing N-terminal arginine or lysine residues

Mäkinen¹,

Mäkinen²

1978

Biochemical Journal

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Two arylamidases (I and II) were purified from human erythrocytes by a procedure that comprised removal of haemoglobin from disrupted cells with CM-Sephadex C-50, followed by treatment of the haemoglobin-free preparation subsequently with DEAEcellulose, gel-permeation chromatography on Sephadex G-200, gradient solubilization on Celite, isoelectric focusing in a pH gradient from 4 to 6, gel-permeation chromatography on Sephadex G-100 (superfine), and finally affinity chromatography on Sepharose 4B covalently coupled to L-arginine. In preparative-scale purifications, enzymes I and II were separated at the second gel-permeation chromatography. Enzyme II was obtained as a homogeneous protein, as shown by several criteria. Enzyme I hydrolysed, with decreasing rates, the L-amino acid 2-naphthylamides of lysine, arginine, alanine, methionine, phenylalanine and leucine, and the reactions were slightly inhibited by 0.2M-NaCl. Enzyme II hydrolysed most rapidly the corresponding derivatives of arginine, leucine, valine, methionine, proline and alanine, in that order, and the hydrolyses were strongly dependent on Cl-. The hydrolysis of these substrates proceeded rapidly at physiological Cl-concentration (0.15M). The molecular weights (by gel filtration) of enzymes I and II were 85000 and 52500 respectively. The pH optimum was approx. 7.2 for both enzymes. The isoelectric point of enzyme II was approx. 4.8. Enzyme I was activated by Co2'+ which did not affect enzyme II to any noticeable extent. The kinetics of reactions catalysed by enzyme I were characterized by strong substrate inhibition, but enzyme II was not inhibited by high substrate concentrations. The Cl--activated enzyme II also showed endopeptidase activity in hydrolysing bradykinin.

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Section: Discussionmentioning

confidence: 99%

Purification and characterization of two human erythrocyte arylamidases preferentially hydrolysing N-terminal arginine or lysine residues

Mäkinen¹,

Mäkinen²

1978

Biochemical Journal

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“…Immunoassay was used to measure ACTH (Immulite 2000 ACTH, DPC Ltd-US). The CAP serum activity was measured by the method of Tuppy and Nesvadba, modified by Klimek in pH 7.6 (CAP 1 ) and 6.9 (CAP 2 ) buffer using L-cystine-di- β -naphthylamide as a substrate [ 3 – 5 ]. Statistical calculations were performed using Statistica computer program (Stat Soft, Poland).…”

Section: Exemplary Results Of Adrenocortical Therapymentioning

confidence: 99%

“…During pregnancy, there is also an increase in the production of hormones and enzymes of the placenta, the function that has an essential meaning in the mutual mother-fetus neuro-immunoendocrine relationship [ 1 – 4 ]. This applies especially to the synthesis and concentration adjustment of isooxytocinases (cystine-beta-aminopeptidase (CAP 1 ) and isocystine-beta-aminopeptidase (CAP 2 )), which decompose hypothalamic hormones [ 5 – 7 ]. Any damage to the placenta (partial separation, calcification and vascular clots), or only hypoxia, leads to a decrease of the concentration of these enzymes in the mother's blood, which automatically results in the increase of not only oxytocin and vasopressin but also corticotropin-realising hormone (CRH) and gonadotropin-realising hormone (GnRH), which, in consequence, provokes a change in the production of steroid hormones, essential for the pregnancy.…”

Section: Introductionmentioning

confidence: 99%

Causal ACTH-Depot Therapy during Pregnancies following Infertility Treatment

Klimek¹,

Klimek²,

Gralek³

et al. 2012

Obstetrics and Gynecology International

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The aim of this paper was to confirm the efficacy of adrenocorticotropin depot (ACTH-depot) therapy in pregnancies with threatened miscarriage and preterm delivery through the desired stimulation of the adrenal glands controlled by the rest of organism. The activity of hypothalamic-pituitary-adrenal axis plays a key role in pregnancy. Such naturally stimulated endogenous corticosteroid hormones are free from unwanted side effects of their synthetics analogs. Low level of maternal blood ACTH and insufficient increase of induced by hypothalamic hormones oxytocinases (cystine-β-aminopeptidases) were indication to ACTH-depot therapy (0.5 mg/week) in our consecutive prospective studies. Contrary to antenatal use of synthetic corticosteroids, there are no temporal limits of this therapy, which has to be more often recommended into clinical prevention of fetal morbidity, treatment of premature delivery, and finally elimination of the newborn's mortality caused by the neuroendocrinological gestoses.

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“…A novel approach to the assay of oxytocinase has been described by Chard et al (1970), who followed the destruction of 131I-labelled oxytocin by measuring its ability to bind to specified oxytocin antibody. Klimek (1968) has shown that the pH optimum of oxytocinase activity changes from pH 6.0 in the first trimester to pH 7.8 in the third. He suggested that this may be due to a change in the ratio of isoenzymes and recommends simultaneous estimations at both pH values.…”

Section: Cystine Aminopeptidase (Oxytocinase)mentioning

confidence: 98%