Reversible Acid Activation of Amniotic Fluid Inactive Renin

1983 ◽  
Vol 64 (5) ◽  
pp. 481-486 ◽  
Author(s):  
Robert C. Franks ◽  
Francis Bodola ◽  
Robert D. Renthal ◽  
Robert H. Hayashi
Keyword(s):  
Amniotic Fluid ◽  
Human Plasma ◽  
Conformational Change ◽  
Deae Cellulose ◽  
Acid Activation ◽  
Human Amniotic Fluid ◽  
Before And After ◽  
Inactive Renin ◽  
Ph Dependent ◽  
Cibacron Blue F3ga

1. Inactive renin was isolated from human amniotic fluid by chromatography with DEAE-cellulose, pepstatin-aminobutyl-agarose, octylagarose and Cibacron Blue F3GA columns. 2. Before and after isolation from amniotic fluid, inactive renin could be activated by incubation with pepsin and by dialysis to pH 3.3, and the acid activation could be reversed by subsequent incubation at pH 7.4 and 37°C. 3. Inactive renin was not activated by procedures expected to dissociate renin from an inhibitor. 4. The results suggest a pH-dependent conformational change as the mechanism of reversible acid activation of inactive renin in amniotic fluid. 5. There are chromatographic and activation similarities of inactive renin from human plasma, kidney and amniotic fluid.

The Nature of Inactive Renin in Human Plasma and Amniotic Fluid

1978 ◽  
Vol 55 (1) ◽  
pp. 41-50 ◽  
Author(s):  
A. A. Shulkes ◽  
R. R. Gibson ◽  
S. L. Skinner
Keyword(s):  
Molecular Weight ◽  
Amniotic Fluid ◽  
Human Plasma ◽  
Gel Filtration ◽  
Dilution Effect ◽  
Exchange Chromatography ◽  
Acid Activation ◽  
Temperature Dependent ◽  
Inactive Renin ◽  
Full Activation

1. The properties of inactive and active renin in human plasma and amniotic fluid were studied chromatographically. Activation was achieved at pH 3.3 with and without added pepsin. 2. Acid activation of renin was time- and temperature-dependent but was inhibited by dilution of the sample. The dilution effect was corrected by adding pepsin. Such characteristics indicate that activation at low pH is catalysed by intrinsic enzymes. 3. Separation and/or dilution of the activating enzyme during ion-exchange chromatography concealed the eluted position of inactive renin and reduced the amount recovered. Only after full activation of the eluted renin was achieved with added pepsin was a distinct peak of inactive renin exposed. 4. At pH 7.5 inactive renin carried a lower negative charge than the active enzyme. This charge difference was lost after activation. 5. No molecular-weight differences between active, inactive renin or the International Renin Standard were detected by gel filtration. No renin of larger molecular weight was present. 6. These findings will be helpful in purification studies of human inactive renin.

Fluorometric procedure for determining "lamellar body" phospholipids in the particulate fraction of amniotic fluid after filtration.

1983 ◽  
Vol 29 (2) ◽  
pp. 362-365 ◽  
Author(s):  
J Egberts ◽  
W Soederhuizen ◽  
D O Gebhardt
Keyword(s):  
Amniotic Fluid ◽  
Lung Surfactant ◽  
Lamellar Body ◽  
Fetal Lung ◽  
Human Amniotic Fluid ◽  
Wide Range ◽  
Before And After ◽  
The Difference ◽  
Filtration Step ◽  
Good Agreement

Abstract A rapid (30-min) semiautomated continuous-flow procedure is described for use in assessing the phospholipids of the particulate ("lamellar body") fraction of human amniotic fluid. The method is based on measuring the difference in fluorescence of 1,6,-diphenyl-1,3,5-hexatriene added to amniotic fluid before and after micropore filtration. The filtration step removes "lamellar body" particles, which are considered to contain the fetal lung surfactant. The phospholipid values for the filtered particles are independent of background fluorescence, which increases when amniotic fluid is contaminated by bilirubin pigments or blood components. Over a wide range (3-150 mumols/L) the fluorescence increases linearly with the phospholipid concentration of the amniotic fluid. There is a good agreement between the value for particulate "lamellar body" phospholipid, the ratio of the "lamellar body" phospholipids to total amniotic fluid phospholipids, and the lecithin/sphingomyelin ratio.

Changes in Human Amniotic Fluid Fibrinolytic Inhibitor Levels during Pregnancy

1976 ◽  
Vol 35 (02) ◽  
pp. 382-385 ◽  
Author(s):  
J Aznar ◽  
A Hernandez ◽  
J.J Parrilla ◽  
A Estelles ◽  
J Gilabert
Keyword(s):  
Amniotic Fluid ◽  
Lytic Activity ◽  
Human Amniotic Fluid ◽  
Fetal Maturity ◽  
Fibrinolytic Inhibitors ◽  
Before And After ◽  
The Moment

SummaryThe amniotic fluid (AF) when incubated with the patient’s own plasma diminishes the lytic activity of the plasma. It is suggested that this inhibition is due to the presence of fibrinolytic inhibitors in the AF. The inhibitors rate increases as pregnancy advances. Evaluating these inhibitors in a group of 65 women before and after the 38th week of pregnancy, a higher rate of fibrinolytic inhibitors is found after the 38th week. The said differences are statistically significant. For the moment it does not seem that the increasing of the inhibitors in the last part of pregnancy might be used as a fetal maturity test.

An Endogenous Protease Activating Plasma Inactive Renin

1978 ◽  
Vol 55 (s4) ◽  
pp. 133s-134s ◽  
Author(s):  
B. J. Leckie
Keyword(s):  
Human Plasma ◽  
Serine Protease ◽  
Protease Inhibitors ◽  
Trypsin Inhibitor ◽  
Soya Bean ◽  
Acid Activation ◽  
Bean Trypsin Inhibitor ◽  
Inactive Renin ◽  
Inhibited Acid ◽  
Endogenous Protease

1. The protease inhibitors Trasylol and soya-bean trypsin inhibitor prevented the activation of plasma inactive renin by acid. 2. N-Ethylmaleimide inhibited acid-activation to some extent but o-phenanthroline had no effect. 3. Acid-activation of the inactive renin in human plasma is mediated by a serine protease.

scholarly journals Human amniotic fluid stem cells (hAFSCs) expressing p21 and cyclin D1 genes retain excellent viability after freezing with (dimethyl sulfoxide) DMSO

2019 ◽  
Vol 19 (1) ◽  
pp. 43-51 ◽  
Author(s):  
Shiva Gholizadeh-Ghaleh Aziz ◽  
Zahra Fardyazar ◽  
Fatima Pashaei-Asl ◽  
Mohammad Rahmati-Yamchi ◽  
Khodadad Khodadadi ◽  
...  
Keyword(s):  
Stem Cells ◽  
Amniotic Fluid ◽  
Cyclin D1 ◽  
Slow Freezing ◽  
Human Amniotic Fluid ◽  
Trypan Blue Exclusion ◽  
Amniotic Fluid Stem Cells ◽  
Before And After ◽  
Cluster Of Differentiation

Human amniotic fluid stem cells (hAFSCs) have features intermediate between embryonic and adult SCs, can differentiate into lineages of all three germ layers, and do not develop into tumors in vivo. Moreover, hAFSCs can be easily obtained in routine procedures and there is no ethical or legal limitations regarding their use for clinical and experimental applications. The aim of this study was to assess the effect of slow freezing/thawing and two different concentrations of DMSO (10% DMSO + 90% fetal bovine serum [FBS] and 5% DMSO + 95% FBS) on the survival of hAFSCs. hAFSCs were obtained from 5 pregnant women during amniocentesis at 16–22 weeks of gestation. The expression of pluripotency markers (Octamer-binding transcription factor 4 [Oct4] and NANOG) by reverse transcription polymerase chain reaction and cell surface markers (cluster of differentiation [CD31], CD44, CD45, and CD90) by flow cytometry was analyzed before and after the slow-freezing. Cell viability was assessed by trypan blue exclusion or MTT assay. Quantitative mRNA expression of Oct4, NANOG, cyclin D1 and p21 was determined by real-time PCR before and after the slow-freezing. Pluripotency of hAFSCs was confirmed by NANOG and POU5F1 (Oct4) gene expression before and after slow-freezing. All hAFSC cultures were positive for CD44 and CD90. A higher viability of hAFSCs was observed after freezing with 90% FBS + 10% DMSO. There was increased expression of NANOG and decreased expression of POU5F1 gene after freezing, compared to control cells (before freezing). DMSO and the process of freezing did not significantly change the expression of p21 and cyclin D1 genes in hAFSCs. Overall, our results indicate the applicability of slow-freezing and DMSO in cryopreservation of SCs.

scholarly journals Reversibility of acid-activation and cryoactivation of inactive renin in human plasma.

1981 ◽  
Vol 45 (9) ◽  
pp. 1090-1091
Author(s):  
MASATO MATSUNAGA ◽  
KENICHI MORIMOTO ◽  
AKIRA HARA ◽  
CHUN HO PAK ◽  
CHUICHI KAWAI
Keyword(s):  
Human Plasma ◽  
Acid Activation ◽  
Inactive Renin
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