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Abstract

The aim of this study was to identify the proteoforms of albumin and kallikrein in stallion seminal plasma (SP), and to determine their correlations with sperm motility parameters. The experimental material consisted of ejaculates from 8 stallions, which were collected during the breeding and non-breeding seasons (BS and NBS, respectively). SP proteins were identified by 2-D PAGE and mass spectrometry (MALDI TOT/TOF MS). Sperm motility parameters were analyzed using the CASA system. Protein expression (integrated optical density-IOD) of albumin proteoforms 1 (ALB 1) and 2 (ALB 2) and kallikrein proteoforms 1 (KAL 1) and 2 (KAL 2) was correlated (p<0.05) with sperm motility parameters (total motility and progressive motility) during the BS. No significant correlations were found between the expression of albumin or kallikrein and sperm motility parameters during the NBS. The presence of correlations between the expression of ALB 1, ALB 2, KAL 1, KAL 2 and selected sperm motility parameters could suggest that the analyzed components of the SP belong to the group of fertility-associated pro- teins (FAPs).

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Authors and Affiliations

M. Mogielnicka-Brzozowska
L. Fraser
A. Dziekońska
K. Gackowska
M. Sobiewska
A. Kuzborska
A.M. Majewska
K. Filipowicz
W. Kordan
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Abstract

Oxidative stress (OxS) has been implicated in the pathogenesis of Crohn’s disease (CD). The aim of this study was to examine whether nonenzymatic antioxidants are associated with active CD, by using the FRAP and GSH assay in plasma. Additionally, we measured bilirubin and albumin levels as two individual components of the plasma antioxidant system. A total of 55 patients with established CD, 30 with active CD and 25 with inactive disease, and 25 healthy individuals were prospectively enrolled in this study. We evaluated CD activity index, BMI and blood morphology, platelet count, serum CRP level, and bochemical parameters of OxS: ferric reducing ability of plasma (FRAP), reduced glutathione (GSH) in plasma and bilirubin and albumin levels in serum. Plasma FRAP and GSH concentrations were decreased in both CD groups compared to controls and negatively correlated with CDAI values (FRAP: r = –0.572, p = 0.003; GSH: r = –0.761, p = 0.001), CRP and platelet count. Bilirubin and albumin levels were lower in the serum of active CD patients than inactive CD patients and controls and negatively correlated with the CD activity index (r = –0328, p = 0.036, r = –0.518, p = 0.002) and CRP (r = –0.433, p = 0.002). The decreased FRAP and GSH levels in plasma and bilirubin and albumin levels in serum of patients with active CD compared to inactive CD and controls underlines the importance of OxS in the pathophysiology and activity of CD.

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Authors and Affiliations

Katarzyna Szczeklik
Wirginia Krzyściak
Dorota Cibor
Kamil Kozioł
Halina Pocztar
Jolanta Pytko-Polończyk
Tomasz Mach
Danuta Owczarek
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Abstract

Platelet aggregation contributes to the pathogenesis of cardiovascular diseases. After activation it leads to dense granule secretion and 5-HT release. The question arises; how platelet aggregation is endogenously controlled during blood circulation. In preliminary studies, we observed that human plate-lets aggregate more rapidly when suspended in buffer as compared to those suspended in plasma (PRP). These observations point to the presence of an endogenous substance that may inhibit arachidonic acid– induced platelet aggregation. An analysis of plasma Cohn fractions demonstrated that most of the plasma inhibitory activity was associated with albumin–rich and α-globulin rich protein fractions. The identity of plasma endogenous inhibitors of platelet aggregation (EIPA) was established by affinity chromatography on Cibacron Blue F3G-A for specific removal of albumin. The association of α-globulins to EIPA activity was recognized as due to haptoglobin by affinity chromatography on a column of hemoglobin-sepharose. In addition, we also found that the distribution of EIPA activity varies according to sex and physiological state. These findings reveal that EIPA may act by modulation of arachidonic acid metabolism or seques-tering the fatty acid substrate.
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Authors and Affiliations

Nadia Khan
1 2 3
Magdalena Kurnik-Łucka
2
Gniewomir Latacz
3
Krzysztof Gil
2
Sheikh Arshad Saeed
1

  1. Dr. Panjwani Center for Molecular Medicine and Drug Research (PCMD), University of Karachi, Karachi, Pakistan
  2. Department of Pathophysiology, Faculty of Medicine, Jagiellonian University Medical College, Kraków, Poland
  3. Department of Technology & Biotechnology of Drugs, Faculty of Pharmacy, Jagiellonian University Medical College, Kraków, Poland

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