Analyses of soluble endoglin and matrix metalloproteinase 14 using enzyme-linked immunosorbent assay in the diagnosis and/or the determination of the severity of late/early-onset preeclampsia

Objective. The aim of this study was to determine whether maternal serum matrix metalloproteinases 2, 3, 9, and 13 levels differ in early- and late-onset preeclampsia and uncomplicated pregnancies. Patients and Methods. The study was carried out in 125 pregnant women (29 with early-onset preeclampsia; 31 preeclamptic patients with late-onset preeclampsia; and 65 healthy pregnant controls). Levels of MMP-2, MMP-3, MMP-9, and MMP-13 were measured in the maternal serum using an enzyme-linked immunosorbent assay. Results. Maternal serum MMP-2 levels in both the groups of preeclamptic women were significantly higher than those in the controls. Levels of MMP-3 were significantly higher in preeclamptic patients with early-onset disease; however, the MMP-3 levels in patients with late-onset preeclampsia were similar to those observed in the control subjects. MMP-9 levels were lower whereas the levels of MMP-13 were higher in both preeclamptic groups of pregnant women than in the healthy controls, but these differences were statistically insignificant. Conclusions. One important finding of the present study was that MMP-3 appears to be involved solely in early-onset preeclampsia, but not in late-onset preeclampsia. Higher levels of MMP-2 and MMP-13 and lower levels of MMP-9 seem to be related to both early- and late-onset severe preeclampsia.

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Serum Galectin-3 Levels Are Unlikely to Be a Useful Predictive Marker for Early-onset Preeclampsia Development

Prague Medical Report ◽

10.14712/23362936.2020.16 ◽

2020 ◽

Vol 121 (3) ◽

pp. 172-180

Author(s):

Asparuh Nikolov ◽

Nikola Popovski ◽

Alexander Blazhev

Keyword(s):

Early Onset ◽

Maternal Age ◽

Predictive Marker ◽

Serum Levels ◽

Matrix Proteins ◽

Enzyme Linked Immunosorbent Assay ◽

Hypertensive Disorders In Pregnancy ◽

Galectin 3 ◽

Early Onset Preeclampsia

Galectin-3 (gal-3) is lectin which is presumed to interact with extracellular matrix proteins and cell surface glycoproteins in normal and pathophysiological conditions. The expression of gal-3 at the fetal-maternal interface partially overlaps that of gal-1, suggesting that an interplay between them might be important for hypertensive disorders in pregnancy like preeclampsia. The aim of our study was to test the hypothesis whether galectin-3 could be used as a predictive marker for early-onset preeclampsia development. 32 patients with early-onset preeclampsia were examined, mean age 28.8 ± 5.5; and 22 age matched normal pregnancies mean age 28.5 ± 6.0. The enzyme-linked immunosorbent assay (ELISA) was used for measuring serum galectin-3 levels. There were no significant differences between serum levels of galectin-3 in sera of preeclampsia patients compared to normal pregnant women – 14.1 ± 4.77 vs. 15.7 ± 5.95 ng/ml (p>0.05). Serum galectin-3 levels correlated with maternal age (r=0.33; p=0.03) and BMI (body mass index) (r=0.52; p=0.01). Our data suggest that determination of serum galectin-3 levels may not be a useful method for prediction of early-onset preeclampsia. Studies should be aimed to other categories of biomarkers.

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EVALUATION OF A RECENTLY DEVELOPPED ENZYME LINKED IMMUNOSORBENT ASSAY FOR THE DETERMINATION OF ANTI-PHOSPHOLIPASE A2 RECEPTOR ANTIBODIES

10.26226/morressier.56e174d9d462b8028d88aca7 ◽

2016 ◽

Author(s):

Anne-Sophie Messiaen

Keyword(s):

Phospholipase A2 ◽

Immunosorbent Assay ◽

Enzyme Linked Immunosorbent Assay ◽

Phospholipase A2 Receptor ◽

Receptor Antibodies

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Biotin-avidin Mediated Competitive Enzyme-linked Immunosorbent Assay for Determination of Ketamine

CHINESE JOURNAL OF ANALYTICAL CHEMISTRY (CHINESE VERSION) ◽

10.3724/sp.j.1096.2010.00117 ◽

2010 ◽

Vol 38 (1) ◽

pp. 117-120

Author(s):

Wen-Di ZHANG ◽

Ping SU ◽

Yi YANG ◽

Zhen-Quan GUO

Keyword(s):

Immunosorbent Assay ◽

Enzyme Linked Immunosorbent Assay

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SENSITIVE AND SPECIFIC ENZYME-LINKED IMMUNOSORBENT ASSAY FOR UROKINASE-TYPE PLASMINOGEN ACTIVATOR IN HUMAN PLASMA

10.1055/s-0038-1644425 ◽

1987 ◽

Cited By ~ 1

Author(s):

J Grøndahl-HANSEN ◽

N Agerlin ◽

L S Nielsen ◽

K Danø

Keyword(s):

Plasminogen Activator ◽

Immunosorbent Assay ◽

Enzyme Linked Immunosorbent Assay ◽

Mean Values ◽

Amino Terminal ◽

Type Plasminogen Activator ◽

Healthy Donors ◽

Urokinase Type Plasminogen Activator ◽

The Mean

An enzyme-linked immunosorbent assay (ELISA) was developed for the measurement of human urokinase-type plasminogen activator (u-PA) in plasma and serum. Microtiter plates were coated with a monoclonal antibody and incubated with standard or sample. Bound u-PA was quantitated with polyclonal antibodies conjugated with biotin, followed by avidin-peroxidase. The assay was 10-fold as sensitive as other previously reported ELISAs, the detection limit being approximately 1 pg of u-PA in a volume of 100 μl with a linear dose-response up to 15 pg of u-PA. The assay detected active u-PA and its inactive proenzyme form equally well and the recovery of both forms was higher than 90% in plasma. A variety of structurally related proteins, including t-PA, were tested, but no reaction with proteins other than u-PA and its amino-terminal degradation product were observed. The intra-assay and inter-assay coefficients of variation for determination of u-PA in plasma were 7.6% and 8.4%, respectively. The assay was equally applicable to serum. The values obtained with plasma and serum were similar, and the results were not affected by small variations in the preparation of the samples. The ELISA was used to measure the concentration of u-PA in plasma from 34 healthy donors. The mean values for u-PA in plasma from healthy donors was 1.1 ng/ml ± 0.3 ng/ml (SD) (range 0.6 - 1.5 ng/ml). No significant differences were found between men and women and no correlation between u-PA concentration and age could be demonstrated.The mean u-PA concentration in plasma from healthy donors obtained in this study is substantially lower than that reported by others. This might be due to different methods of determination of the protein content of the standard preparations or to differences in the specificity of the assays.

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