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.
Nagoya, Japan. In Exp Clin Endocrinol Diabetes, Mar 2015
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.
Positioning of aminopeptidase inhibitors in next generation cancer therapy.
Amsterdam, Netherlands. In Amino Acids, 2014
This review focuses on the function and subcellular location of five key aminopeptidases (aminopeptidase N, leucine aminopeptidase, puromycin-sensitive aminopeptidase, leukotriene A4 hydrolase and endoplasmic reticulum aminopeptidase 1/2) and their association with different diseases, in particular cancer and their current position as target for therapeutic intervention by aminopeptidase inhibitors.
Inhibitors of the Plasmodium falciparum M17 Leucine Aminopeptidase
Bethesda, United States. In Unknown Journal, 2014
For survival, the Plasmodium falciparum (Pf) malaria parasite requires the action of a number of metallo-aminopeptidases, including PfM1MAA (membrane alanine aminopeptidase), PfM17LAP (leucine aminopeptidase), and PfM18AAP (aspartyl aminopeptidase).
Inhibitors of the Plasmodium falciparum M18 Aspartyl Aminopeptidase
Bethesda, United States. In Unknown Journal, 2013
For survival, the Plasmodium falciparum (Pf) malaria parasite requires the action of a number of metallo-aminopeptidases that each display restricted amino acid specificities, including PfM1MAA (membrane alanine aminopeptidase), PfM17LAP (leucine aminopeptidase), and PfM18AAP (aspartyl aminopeptidase), which are thought to act in concert to degrade host erythrocyte hemoglobin that the parasite uses as a source of amino acid building blocks for the synthesis of its own proteins.
The Reaction Mechanism of Bovine Lens Leucine Aminopeptidase.
Burgess Hill, United Kingdom. In J Phys Chem B, 2002
We present a quantum mechanical/molecular mechanical (QM/MM) study using the AM1 Hamiltonian and a flexible MM part on the mode of action of the bovine lens leucine aminopeptidase (blLAP), a cytosolic exopeptidase that catalyzes the cleavage of the N-terminal amide bond of peptides.
Subfractionation of human serum enzymes.
In Science, 1960
These subfractions and unfractionated leucine aminopeptidase are localized with respect to the protein zones of the Smithies starch gel pattern.