Publications by authors named "O V Kryukova"

Article Synopsis
  • Recent analysis identified over 400 damaging missense ACE mutations, suggesting that carriers of heterozygous loss-of-function ACE mutations may be at risk for late-onset Alzheimer's disease (AD).
  • A study measuring blood ACE levels in 41 subjects with different heterozygous mutations revealed that certain mutations (Y215C and G325R) significantly reduced ACE levels, while the R1250Q mutation did not impact ACE levels.
  • The findings indicate that measuring blood ACE levels in patients with ACE mutations could help identify those at increased risk for AD, potentially guiding future preventive treatments involving chaperones and proteasome inhibitors to improve ACE function.
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Background: Analysis of existing mutations of Angiotensin-I-Converting Enzyme (ACE) led us to hypothesize that the carriers of damaging ACE mutations (accompanied by low ACE levels) could be at risk for the development of late-onset Alzheimer's disease (AD).

Methodology/principal Findings: We quantified blood ACE levels in EDTA-containing plasma from 15 patients with 11 different heterozygous ACE mutations and estimated the effects of these mutations on ACE phenotypes, using a set of mAbs to ACE and two ACE substrates. We confirmed prior observations that the relatively frequent Y215C mutation in the N domain of ACE (present in ~1% of the population) is associated with both Alzheimer's disease (AD) and reduced plasma levels of ACE (~50% of controls), indicating that it likely results in a transport-deficient protein.

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Article Synopsis
  • Low-quality transplants affected by hypoxic injury can result in complications after surgery.
  • This research uses mathematical modeling to analyze how oxygen absorption through the liver impacts its metabolism when oxygen levels are low.
  • Findings indicate that lower oxygenation of the perfusion medium reduces oxygen uptake, requiring more energy for the liver's metabolism, while energy resources are optimally allocated among various metabolic processes.
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Angiotensin I-converting enzyme (ACE) is a peptidase widely presented in human tissues and biological fluids. ACE is a glycoprotein containing 17 potential N-glycosylation sites which can be glycosylated in different ways due to post-translational modification of the protein in different cells. For the first time, surface-enhanced Raman scattering (SERS) spectra of human ACE from lungs, mainly produced by endothelial cells, ACE from heart, produced by endothelial heart cells and miofibroblasts, and ACE from seminal fluid, produced by epithelial cells, have been compared with full assignment.

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Epithelial cells of prostate express significant level of ACE and, as a result, seminal fluid has 50-fold more ACE than plasma. The substitution of highly specialized prostate epithelial cells by tumor cells results in dramatic decrease in ACE production in prostate tissues. We performed detailed characterization of ACE status in prostate tissues from patients with benign prostate hyperplasia (BPH) and prostate cancer (PC) using new approach- ACE phenotyping, that includes evaluation of: 1) ACE activity with two substrates (HHL and ZPHL); 2) the ratio of the rates of their hydrolysis (ZPHL/HHL ratio); 3) the ratio of immunoreactive ACE protein to ACE activity; 4) the pattern of mAbs binding to different epitopes on ACE - ACE conformational fingerprint - to reveal conformational changes in prostate ACE due to prostate pathology.

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