Synthesis and release of placental proteins by in vitro perfused human placental tissue

SUMMARY Short-term incubation of human placental tissue in Krebs–Ringer bicarbonate buffered media with various concentrations of K+ and Ca2+ showed a graded response in human placental lactogen (HPL) release at different Ca2+ concentrations, but no effect at increased K+ concentration. Media with high Ca2+ caused an inhibition of release, while Ca2+-free media caused a stimulation in HPL release. High concentrations of Mg2+ inhibited release minimally, while Ba2+ had no effect. There was no change in HPL release when Na+ concentration was increased. La3+-Locke's solution markedly inhibited release of HPL but the significance of this effect is unknown. These results suggest that Ca2+ is not required for HPL secretion from placental tissue. It seems that HPL secretion in vitro does not follow the usual pattern where a physiological stimulus or high K+ concentration causes inward movement of calcium which couples stimulation to secretion.

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TRANSFORMATION IN VITRO OF [4-14C]DEHYDROEPIANDROSTERONE TO 7-OXYGENATED DERIVATIVES BY NORMAL EARLY HUMAN PLACENTAL TISSUE

Journal of Endocrinology ◽

10.1677/joe.0.0500301 ◽

1971 ◽

Vol 50 (2) ◽

pp. 301-306 ◽

Cited By ~ 10

Author(s):

Y. W. MIRHOM ◽

F. E. SZONTÁGH

Keyword(s):

Placental Tissue ◽

Human Placental Tissue ◽

Early Human ◽

Human Placentae

SUMMARY Samples from three early human placentae were incubated with [4-14C]-dehydroepiandrosterone (DHA). It was found that [4-14C]DHA was transformed into 7-oxygenated derivatives in yields decreasing in the order: 7-oxo-DHA > 7β-hydroxy-DHA > 7α-hydroxy-DHA. These products were only slowly transformed into other derivatives.

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Adrenomedullin gene expression in human placental tIssue and leukocytes: a potential marker of severe tIssue hypoxia in neonates with birth asphyxia

Acta Endocrinologica ◽

10.1530/eje.0.1470711 ◽

2002 ◽

pp. 711-716 ◽

Cited By ~ 24

Author(s):

R Trollmann ◽

E Schoof ◽

E Beinder ◽

D Wenzel ◽

W Rascher ◽

...

Keyword(s):

Gene Expression ◽

Perinatal Asphyxia ◽

Newborn Infants ◽

Birth Asphyxia ◽

Placental Tissue ◽

Tissue Hypoxia ◽

Mrna Levels ◽

Potential Marker ◽

Human Placental Tissue

OBJECTIVE: The aim of the present study was to investigate the role of adrenomedullin (ADM) as a hypoxia-inducible marker of clinically relevant tIssue hypoxia in acute birth asphyxia of term newborn infants. METHODS: For this purpose, ADM mRNA was determined in human placental tIssue of 20 term pregnancies complicated by birth asphyxia (pH and base deficit values, clinical score). In addition, ADM mRNA was measured in leukocytes of the asphyxiated newborn infants during the first 12 h of life (n=12). Controls were available from ten healthy term pregnancies. In vitro, hypoxia-inducible expression of ADM mRNA was evaluated in human choriocarcinoma cells (BeWo) and human leukocytes exposed to hypoxia (1% O(2)) for 1-24 h. mRNA levels were measured by TaqMan real-time PCR. RESULTS: In vitro, ADM mRNA related to porphobilinogen deaminase (PBGD) mRNA levels significantly increased in response to hypoxia within a period of 4 h in leukocytes and 12 h in BeWo cells. In human placental tIssue, significantly higher levels of ADM/PBGD mRNA were present in asphyxiated newborn infants with severe hypoxic-ischemic encephalopathy (HIE) (n=5) compared with patients with mild or no HIE (n=15). Increased levels of ADM/PBGD mRNA levels were found during the first hours of life in leukocytes of neonates with severe HIE compared with controls. CONCLUSIONS: Our results indicate an upregulation of ADM gene expression in human placenta and leukocytes in clinically relevant hypoxic-ischemic birth complications and suggest ADM gene expression as a promising marker for severe complications due to perinatal asphyxia such as HIE.

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Simple method for extracting RNA from cultured cells and tissue with guanidine salts

Clinical Chemistry ◽

10.1093/clinchem/39.7.1408 ◽

1993 ◽

Vol 39 (7) ◽

pp. 1408-1411 ◽

Cited By ~ 20

Author(s):

R Zolfaghari ◽

X Chen ◽

E A Fisher

Keyword(s):

Cultured Cells ◽

Guanidine Hydrochloride ◽

Placental Tissue ◽

Animal Origin ◽

Clinical Samples ◽

Simple Method ◽

Simple Protocol ◽

Human Placental Tissue ◽

Polymerase Chain

Abstract We have developed a simple protocol for isolating RNA from both cell culture and tissue from human and animal sources, using guanidine thiocyanate and guanidine hydrochloride, but no organic solvents. The protocol reproducibly yielded 15 to 25 micrograms of high-quality RNA per 10(6) cells of human and animal origin and 1 to 1.1 mg of RNA per gram of human placental tissue. The RNA so obtained was ribonuclease-free and not contaminated by DNA. It was suitable for reverse transcription-polymerase chain reaction, Northern blot analysis, and in vitro expression of proteins. Thus, the molecular assessment of both research and clinical samples can be readily and reliably initiated by the application of this protocol.

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Prostate-Specific Antigen Synthesis and Secretion by Human Placenta: A Physiological Kallikrein Source during Pregnancy1

The Journal of Clinical Endocrinology & Metabolism ◽

10.1210/jcem.85.1.6302 ◽

2000 ◽

Vol 85 (1) ◽

pp. 317-321 ◽

Cited By ~ 1

Author(s):

Manuela Malatesta ◽

Ferdinando Mannello ◽

Francesca Luchetti ◽

Francesco Marcheggiani ◽

Leone Condemi ◽

...

Keyword(s):

Prostate Specific Antigen ◽

Human Placenta ◽

Specific Antigen ◽

Placental Tissue ◽

Maternal Serum ◽

Rt Pcr ◽

Messenger Ribonucleic Acid ◽

17Β Estradiol ◽

Human Placental Tissue

Prostate-specific antigen (PSA), a kallikrein-like serine protease until recently thought to be prostate specific, has been demonstrated in various nonprostatic tissues and body fluids. PSA has been also found in human endometrium and amniotic fluids, even if the significance of this novel expression is unclear. In this study, we have demonstrated by multiple techniques that human placental tissue, obtained at delivery from normal full-term pregnancies, synthesizes and secretes PSA. RT-PCR showed the presence of PSA messenger ribonucleic acid; biochemical, chromatographic, and immunological studies revealed the expression of both free and complexed PSA forms; immunoelectron microscopy indicated the syncytiotrophoblast as the site of PSA synthesis and secretion. Moreover, in vitro experiments demonstrated that PSA production and secretion are up-regulated by 17β-estradiol, a pregnancy-related steroid hormone. These results suggest that human placenta is a source of the PSA present in amniotic fluid and maternal serum during pregnancy.

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