scholarly journals Studies on sex-organ development. Changes in chemical composition and oestradiol-binding capacity in chromatin during the differentiation of chick Müllerian ducts

1978 ◽  
Vol 172 (3) ◽  
pp. 361-370 ◽  
Author(s):  
Ching Sung Teng ◽  
Christina T. Teng
Keyword(s):  
Binding Sites ◽  
Binding Capacity ◽  
Mullerian Duct ◽  
Histone Protein ◽  
Oestrogen Treatment ◽  
Müllerian Duct ◽  
Mullerian Ducts ◽  
Early Embryonic Stage ◽  
The Right

Biochemical and immunochemical techniques were used to probe the changes in composition of the chromatin of differentiating Müllerian ducts. The non-histone protein increases gradually in the left duct and reaches a constant amount at day 15 of incubation, then remains at the same value until after birth. In the regressing right duct, the non-histone protein increases and then decreases. Gel electrophoresis indicated an increased heterogeneity in the composition of the non-histone protein corresponding to Müllerian-duct differentiation. Little variation in quantity and quality of the histone was observed; however, immunochemical assay confirmed the structural change of Müllerian-duct chromatin during development. An antibody against the chromatin of the newborn-chick oviduct was produced in the rabbit. The chromatin of Müllerian ducts from the early embryonic stage showed a small affinity with the antibody; the affinity increased during the late embryonic stages. The affinity was greatly decreased in the regressing right duct. Oestrogen-binding sites were present in the chromatin of the left and right Müllerian ducts during differentiation, with more sites in the left duct than in the right one during the late stages of development. After oestrogen treatment in vivo, the oestrogen-binding sites on the chromatin of both the left and the right ducts were increased, with a greater increase in the left duct than in the right. In the developing left duct the binding sites reach a maximum on day 15 of incubation, and remain constant at that value until birth.

scholarly journals Studies on sex-organ development. Oestrogenic effect on ornithine decarboxylase activity in the differentiating Müllerian ducts and other organs of the chick embryo

1978 ◽  
Vol 176 (1) ◽  
pp. 143-149 ◽  
Author(s):  
C S Teng ◽  
C T Teng
Keyword(s):  
Enzyme Activity ◽  
Ornithine Decarboxylase ◽  
Decarboxylase Activity ◽  
Mullerian Duct ◽  
Stages Of Development ◽  
Müllerian Duct ◽  
Mullerian Ducts ◽  
The Right ◽  
The Brain

The activity of ornithine decarboxylase in the differentiating left and right Müllerian ducts was assayed and compared with that in other embryonic organs, i.e. the liver and the brain throughout the stages of development. In general the enzyme activity was high in the early stages and decreased extensively in the late stages of development. Specifically, in the left and righ Müllerian ducts, the enzyme activity was high from day 8 to day 9 of incubation. In the right duct the enzyme activity started to decline on day 9 and then continuously decreased to an almost undetectable value on day 18 of incubation. In the left duct the enzyme activity also decreased slightly from day 9 to day 12; however, it increased from day 13 to day 15 and finally decreased to a constant value from day 18 until hatching. The alteration in enzyme activity in the Müllerian duct as assayed in vitro during development is not due to the effect of the size of the endogenous ornithine pool. When the enzyme activity was subjected to oestrogen stimulation, an increase of 5–10-fold for the left duct and of 5–3-fold for the right duct was observed during the course of development. No such stimulation was observed with the treatment of progesterone. Testosterone consistently caused a 25–30% inhibition of the enzyme activity in the Müllerian duct. Oestrogen slightly stimulated the enzyme activity in the developing liver but inhibited that of the brain. The concentration of the three polyamines measured in the Müllerian duct corresponds to the activity of the enzyme determined.

scholarly journals Study on sex-organ development. Oestrogen-receptor translocation in the developing chick Müllerian duct

1976 ◽  
Vol 154 (1) ◽  
pp. 1-9 ◽  
Author(s):  
C S Teng ◽  
C T Teng
Keyword(s):  
Binding Sites ◽  
Developmental Stages ◽  
Dissociation Constants ◽  
Duct Cell ◽  
Mullerian Duct ◽  
Embryonic Chick ◽  
Müllerian Duct ◽  
Initial Content

After oestradiol administration in vivo, 87-95% of the initial concentration of oestradiol receptor in the cytoplasm of the embryonic-chick Müllerian-duct cell was translocated into the nucleus. The process of translocation depends on the amount of oestardiol administered in vivo. At 6 h after oestradiol administration in vivo, about 30% replenishment of the initial content of the cytosol receptor was observed in the cytoplasm. The Müllerian-duct nuclei, after exposure to non-radioactive oestradiol, exhibit saturable exchange with [3H]oestradiol in vitro. The exchange of oestradiol is temperature- and time-dependent. The optimal temperature and time for exchange are 37-41 degrees C and 2h respectively. The [3H]oestradiol-receptor complex extracted from the exchanged nuclei is present in 5-6S form, and its isoelectric point is 6.8. The number of nuclear oestradiol-binding sites of the developing Müllerian duct are 1.66, 2.22, 2.63, and 2.50 pmol/mg of DNA respectively for embryos of 10, 12, 15 and 18 days. The dissociation constants of the nuclear oestradiol receptor of the four observed developmental stages range from 3.0 to 3.1 nM.

scholarly journals THE BINDING OF MYOGLOBIN BY PLASMA PROTEIN

1960 ◽  
Vol 111 (1) ◽  
pp. 65-75 ◽  
Author(s):  
Willoughby Lathem
Keyword(s):  
Plasma Protein ◽  
Binding Sites ◽  
Binding Capacity ◽  
Plasma Hemoglobin ◽  
Renal Threshold ◽  
Dog Plasma ◽  
Beta Globulin ◽  
Maximal Binding

When added to dog plasma in vitro and in vivo, myoglobin was bound to plasma protein in a concentration which, maximally, averaged 21 ± 6 mg. per cent. Electrophoretically, bound myoglobin was separated from free myoglobin and migrated between alpha-2 and beta globulin. The electrophoretic characteristics of protein-bound myoglobin were similar to, although not identical with, those of protein-bound hemoglobin. The maximal binding capacity of plasma for myoglobin was less than for hemoglobin, which averaged 123 mg. per cent. At concentrations below the maximal binding capacity, from 15 to 50 per cent of the myoglobin was in the free, unbound state, differing from hemoglobin which was completely bound at all concentrations below the binding capacity. When myoglobin and hemoglobin were added together to plasma, hemoglobin appeared to interfere with the binding of myoglobin or to replace it at the binding sites. Myoglobin, however, did not appear to interfere with the binding of hemoglobin. These observations suggested that myoglobin and hemoglobin were bound at least in part by the same protein. When myoglobin was given intravenously, free myoglobin was excreted in the urine, whereas protein-bound myoglobin was not excreted. This suggests that protein-binding contributes to or determines the apparent renal threshold to myoglobin.

Molecular mechanisms of hormone-mediated Mullerian duct regression: involvement of beta-catenin

Development ◽  
2000 ◽  
Vol 127 (15) ◽  
pp. 3349-3360 ◽  
Author(s):  
S. Allard ◽  
P. Adin ◽  
L. Gouedard ◽  
N. di Clemente ◽  
N. Josso ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Male Rat ◽  
Beta Catenin ◽  
Mullerian Duct ◽  
Hormone Action ◽  
Male Embryo ◽  
Müllerian Duct ◽  
Enhancer Factor

Regression of the Mullerian duct in the male embryo is one unequivocal effect of anti-Mullerian hormone, a glycoprotein secreted by the Sertoli cells of the testis. This hormone induces ductal epithelial regression through a paracrine mechanism originating in periductal mesenchyme. To probe the mechanisms of action of anti-Mullerian hormone, we have studied the sequence of cellular and molecular events involved in duct regression. Studies were performed in male rat embryos and in transgenic mice overexpressing or lacking anti-Mullerian hormone, both in vivo and in vitro. Anti-Mullerian hormone causes regression of the cranial part of the Mullerian duct whereas it continues to grow caudally. Our work shows that this pattern of regression is correlated with a cranial to caudal gradient of anti-Mullerian hormone receptor protein, followed by a wave of apoptosis spreading along the Mullerian duct as its progresses caudally. Apoptosis is also induced by AMH in female Mullerian duct in vitro. Furthermore, apoptotic indexes are increased in Mullerian epithelium of transgenic mice of both sexes overexpressing the human anti-Mullerian hormone gene, exhibiting a positive correlation with serum hormone concentration. Inversely, apoptosis is reduced in male anti-Mullerian hormone-deficient mice. We also show that apoptosis is a decisive but not sufficient process, and that epitheliomesenchymal transformation is an important event of Mullerian regression. The most striking result of this study is that anti-Mullerian hormone action in peri-Mullerian mesenchyme leads in vivo and in vitro to an accumulation of cytoplasmic beta-catenin. The co-localization of beta-catenin with lymphoid enhancer factor 1 in the nucleus of peri-Mullerian mesenchymal cells, demonstrated in primary culture, suggests that overexpressed beta-catenin in association with lymphoid enhancer factor 1 may alter transcription of target genes and may lead to changes in mesenchymal gene expression and cell fate during Mullerian duct regression. To our knowledge, this is the first report that beta-catenin, known for its role in Wnt signaling, may mediate anti-Mullerian hormone action.

Effects of vasopressin and aldosterone on amiloride binding in toad bladder epithelial cells

1975 ◽  
Vol 189 (1097) ◽  
pp. 543-575 ◽  
Keyword(s):  
Epithelial Cells ◽  
Sodium Transport ◽  
Binding Sites ◽  
Specific Binding ◽  
Sodium Concentration ◽  
Isolated Cells ◽  
The Right ◽  
Transepithelial Sodium Transport

Methods have been devised to measure the binding of [ 14 C]amiloride to isolated cells from bladders of toads, Bufo marinus . This agent blocks transepithelial sodium transport across bladders by preventing sodium entry to the transporting mechanism. A saturable binding component has been found with an affinity of 5.6 x 10 7 m -1 in the presence of 1.1 mM Na + , which corresponds to the affinity of amiloride when used as a transport inhibitor at the same sodium concentration. In freshly isolated cells the capacity of the binding sites is 3.6 x 10 5 sites/cell, but this value falls to about one third in aged suspensions. When cells are treated with vasopressin (100 mU/ml) somewhat less specific binding is measured at an amiloride concentration giving 50 % occupancy. The results are consistent with the view that vasopressin moves the binding curve to the right along the concentration axis, reducing the affinity of amiloride by a factor of approximately two, while leaving the total capacity unaffected. The affinity of amiloride when used as an inhibitor of transport is also found to be reduced by a factor of two by vasopressin, and complete inhibition of transport can still be achieved. d -Aldosterone in vitro increases the number of amiloride binding sites in isolated cells by approximately 115%, and results from transport studies indicate that there is no significant change in the affinity of amiloride after d -aldosterone treatment. Inhibitors of transcription and translation (actinomycin D and cycloheximide) prevent the increase in amiloride binding caused by d -aldosterone. In vivo the effects of d -aldosterone are more complex, but it is shown that the steroid increases the transport capacity of the tissue, when this is expressed as the number of amiloride binding sites per unit mass of tissue. The results are discussed in terms of the ways in which the two hormones may alter the entry of sodium into the epithelial cells, and so in turn affect transepithelial sodium transport.

scholarly journals Adhesion G-protein-coupled receptor, GPR56, is required for Müllerian duct development in the chick

2020 ◽  
Vol 244 (2) ◽  
pp. 395-413 ◽  
Author(s):  
Zahida Yesmin Roly ◽  
Andrew T Major ◽  
Alex Fulcher ◽  
Martin A Estermann ◽  
Claire E Hirst ◽  
...  
Keyword(s):  
G Protein ◽  
Female Reproductive Tract ◽  
Mullerian Duct ◽  
G Protein Coupled Receptor ◽  
Endocrine Control ◽  
Müllerian Duct ◽  
Collagen Iii ◽  
Mullerian Ducts ◽  
Duct Development ◽  
G Protein Coupled

The embryonic Müllerian ducts give rise to the female reproductive tract (fallopian tubes, uterus and upper vagina in humans, the oviducts in birds). Embryonic Müllerian ducts initially develop in both sexes, but later regress in males under the influence of anti-Müllerian hormone. While the molecular and endocrine control of duct regression in males have been well studied, early development of the ducts in both sexes is less well understood. Here, we describe a novel role for the adhesion G protein-coupled receptor, GPR56, in development of the Müllerian ducts in the chicken embryo. GPR56 is expressed in the ducts of both sexes from early stages. The mRNA is present during the elongation phase of duct formation, and it is restricted to the inner Müllerian duct epithelium. The putative ligand, Collagen III, is abundantly expressed in the Müllerian duct at the same developmental stages. Knockdown of GPR56 expression using in ovo electroporation results in variably truncated ducts, with a loss of expression of both epithelial and mesenchymal markers of duct development. Over-expression of GPR56 in vitro results in enhanced cell proliferation and cell migration. These results show that GPR56 plays an essential role in avian Müllerian duct development through the regulation of duct elongation.

scholarly journals Pregnancy in uterus didelphys delivered by caesarean section: a case report

2017 ◽  
Vol 6 (11) ◽  
pp. 5166 ◽  
Author(s):  
Devyani Sawai ◽  
Susheel Kumar Sharma ◽  
Devashish Singh Sawai ◽  
Uttkarsha Sawai ◽  
Sangeeta Sharma ◽  
...  
Keyword(s):  
Caesarean Section ◽  
High Risk Group ◽  
Congenital Defects ◽  
Mullerian Duct ◽  
Müllerian Duct ◽  
Uterus Didelphys ◽  
Müllerian Duct Anomalies ◽  
Mullerian Anomaly ◽  
Mullerian Ducts ◽  
Mullerian Duct Anomalies

The aim of this study is to report a rare case of pregnancy in uterus didelphys. Mullerian duct anomalies are congenital defects of the female genital system that arise from abnormal embryological development of the Mullerian ducts. A didelphys uterus, also known as double uterus is one of the least common amongst the various Mullerian duct anomalies. It results from complete failure of fusion of Mullerian ducts. There is presence of double uterine bodies with two separate cervices and often double or septate vagina. We report the case in our institute of a pregnancy in the left sided body of a didelphys uterus, delivered by caesarean section. Patients with uterus didelphys belong to high risk group and complications are increased in malformed uterus. Such cases need a meticulous prenatal care. It is a rare Mullerian anomaly and can present with varied obstetrical and gynaecological complications. Prompt and accurate diagnosis of uterine malformations and appropriate surgical intervention are essential to prevent complications.

Orchiectomy and Hysterectomy for Persistent Müllerian Duct Syndrome Associated-Seminoma in a 35-Year-Old Father: A Rare Case Report

2021 ◽  
Author(s):  
Marah Mansour ◽  
Abdullah Fattal ◽  
Yassamine Ouerdane ◽  
Tamim Alsuliman ◽  
Omar Kanjawi
Keyword(s):  
Undescended Testis ◽  
Exploratory Laparotomy ◽  
Normal Male ◽  
Mullerian Duct ◽  
Müllerian Duct ◽  
Persistent Müllerian Duct Syndrome ◽  
Persistent Mullerian Duct Syndrome ◽  
Rare Case Report ◽  
The Right ◽  
Duct Syndrome

Abstract Background A persistent Müllerian duct syndrome is a rare disorder of sexual differentiation characterized by the presence of the female reproductive system in a normal male. Case presentation Herein, we report a case of a 35-year-old father with the persistent Müllerian duct syndrome and seminoma in the right undescended testis. The exploratory laparotomy was performed and revealed a mass in the right undescended testis and Müllerian duct structures. Conclusions For patients with cryptorchidism and inguinal hernia, the persistent Müllerian duct syndrome should be considered, and radiological evaluation of the genitourinary system is recommended for early diagnosis of persistent Müllerian duct syndrome. The persistent Müllerian duct syndrome is usually detected during surgical operation, and it is considered a risk factor for developing testicular malignancies.

Does atrial natriuretic factor protect against right ventricular overload? II. Tissue binding

1989 ◽  
Vol 67 (4) ◽  
pp. 1612-1616 ◽  
Author(s):  
L. C. Ou ◽  
S. Yen ◽  
G. L. Sardella ◽  
N. S. Hill
Keyword(s):  
Right Ventricle ◽  
Binding Sites ◽  
Atrial Natriuretic Factor ◽  
Binding Capacity ◽  
Specific Binding ◽  
Peripheral Tissues ◽  
Natriuretic Factor ◽  
Target Organs ◽  
The Right ◽  
Atrial Natriuretic

Previous studies have led us to hypothesize that the physiological significance of the diuretic and pulmonary vaso-relaxant effects of atrial natriuretic factor (ANF) is to protect the right heart. This study was designed to evaluate the relative importance of various peripheral tissues as sites of ANF action by tracing the temporal pattern of distribution of 125I-ANF and quantitating the specific binding sites. An in vivo approach, utilizing trace amount of 125I-ANF was adopted to simulate physiological conditions. 125I-ANF injected either intravenously or intra-arterially was quickly bound to peripheral tissues with less than 5% remaining in the circulation after 1 min. The relative binding capacity was greatest in the lung, followed by the kidney, right ventricle, adrenal gland, and left ventricle. The magnitude of specific ANF binding sites per gram of tissue weight followed a similar order. The data demonstrate that ANF released under all circumstances is quickly bound to the target organs, particularly the lung and the kidney, and suggest that these two organs could be the most important target organs of ANF. This evidence provides further support for the proposed hypothesis that a major evolutionary role of ANF is the protection of the right ventricle from mechanical loads.

Human syncytiotrophoblast NPY receptors are located on BBM and activate PLC-to-PKC axis

1998 ◽  
Vol 274 (3) ◽  
pp. E502-E509 ◽  
Author(s):  
Jacques Robidoux ◽  
Lucie Simoneau ◽  
Serge St-Pierre ◽  
Hafid Ech-Chadli ◽  
Julie Lafond
Keyword(s):  
Binding Sites ◽  
Plasma Membranes ◽  
Peptide Yy ◽  
Binding Capacity ◽  
Rank Order ◽  
Receptor Activation ◽  
Response Curves ◽  
Pi3k Activation ◽  
Basal Plasma ◽  
The Right

Neuropeptide Y (NPY) is abundant in plasma and amniotic fluid of women throughout pregnancy, during which its involvement in placental hormonogenesis has been proposed. In accordance with its putative role, the aim of this study was to characterize the human placental syncytiotrophoblast receptivity to NPY. Thus we performed this study on brush-border membranes (BBM) and basal plasma membranes (BPM). Specific125I-labeled NPY (125I-NPY) binding to BBM was rapid (20 min), saturable, with a maximum binding capacity of 604 ± 100 fmol/mg protein, and of high affinity, with a dissociation constant of 11 ± 3 nM. No saturable binding could be shown in BPM. The rank order of affinity of NPY and related peptides to compete for 125I-NPY binding sites was peptide YY (PYY) > NPY = [Leu31,Pro34]NPY > 13–36NPY >> pancreatic polypeptide (PP). It is noteworthy that PYY displaced only 45% of the binding sites. In BBM, both NPY and PYY were potent phospholipase C (PLC) stimulators, leading to a four- to fivefold increase of control phosphodiesterase activity. The latter effect could be prevented by preincubation of membranes with 5 μM U-73122, a known inhibitor of G protein-linked receptor activation of PLC-β. Furthermore, 5 μM BIBP-3226, a Y1-receptor antagonist, shifted both dose-response curves to the right in a similar fashion for both peptides. In accordance with the PLC stimulation, both peptides also induced stimulation of protein kinase C (PKC) activity, which could be partially but additively prevented by U-73122 and LY-294002, a selective inhibitor of phosphatidylinositol-3 kinase (PI3K). Taken together, these data suggest that placental and blood-derived NPY binds to a mixed population of receptors composed of Y1 and Y3 subtypes on the maternal side of the syncytiotrophoblast, where it can mediate its physiological purposes via PLC-β and PI3K activation, both of which lead to PKC activation. However, because BIBP-3226 antagonized both effects, the physiological relevance of the apparent Y3 fraction is still unsolved.

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