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At least 19 recordsLinked to original sources
PubMed1976

Interaction of uteroglobin with progesterone, 5alphapregnane-3,20-dione and estrogens.

Uteroglobin was obtained from 5 day pregnant rabbits and purified to homogeneity by Sephadex G 75 and DEAE-cellulose chromatographies. Progesterone binding to uteroglobin was decreased by lyophilization and enhanced by SH-reducing agents. Dithiothreitol was more effective than dithioerythritol, and beta-mercaptoethanol was only active at 25 to 100 mM concentrations. SH-blocking agents (iodoacetate, iodoacetamide, phydroxymercuribenzoate and, dithiobisnitrobenzoic acid) inhibited binding. In the absence of SH-reducing agents only one in every 500 uteroglobin molecules bound the hormone, whereas under optimal conditions (20 mM dithiothreitol) one in every two molecules bound progesterone. There was no significant difference in equilibrium dissociation constants under these two conditions. Uteroglobin had a relatively high affinity for progesterone (KD=4.1 X 10(-7)M) but a threefold higher affinity for 5alpha-pregnane-3,20-dione (KD=1.3 X 10(-7)M). Estradiol was bound but non-specifically with a very low affinity, and its binding was not enhanced by SH-reducing agents. Hormonal specificity of binding to uteroglobin was different from that of binding to rabbit uterine progesterone receptor. Various synthetic progestagens (chlormadinone acetate, norethisterone, R5020) were bound to the latter but not to the former protein. Diethylstilbestrol had some affinity (15% of that of progesterone) for uteroglobin and no affinity for the progesterone receptor. Uteroglobin incubated in the presence or absence of cofactors (NADH and NADPH) with or without dithiothreitol did not metabolize progesterone.

Androgens↗
PubMed1978

Uteroglobin-like antigen in the pulmonary epithelium and secretion of the lung.

The immunological identity of a uteroglobin-like protein, occurring in respiratory tract secretions and tissue, with uteroglobin from rabbit endometrial secretion is demonstrated. A uteroglobin-like antigen has been localized in bronchial epithelial cells and in bronchioles by immunofluorescence. This secretory protein is, in contrast to the authentic uteroglobin, hormone-independent, as far as estrogens and progesterone are concerned. The possible significance of comparative studies on uteroglobin and the uteroglobin-like antigen is discussed, taking into account cytological, endocrinological, and molecularbiological aspects.

Animals↗
PubMed1978

Characteristics of the purified uteroglobin-like protein from rabbit lung.

A uteroglobin-like protein was prepared from lung extracts of female rabbits by absorption to immobilized anti-uteroglobin immunoglobulin and purified to homogeneity by gel filtration on Sephacryl S-200. The final preparation is indistinguishable from uteroglobin according to its behaviour in Ouchterlony double-diffusion, polyacrylamide gel electrophoresis under denaturing and non-denaturing conditions, ultraviolet spectrum, tryptic peptide analysis, and progesterone-binding properties. Progesterone binding to the lung protein exhibits an affinity similar to that observed with authentic uteroglobin and is equally enhanced by reduction of the protein with dithiothreitol. Competition experiments with non-radioactive steroids demonstrate a similar steroid-specificity for both proteins. Progesterone binding causes a perturbation in the ultraviolet absorbance of tyrosine residues of the lung protein similar to that observed with uteroglobin. These data suggest that the proteins prepared from both sources are biochemically identical.

Animals↗
PubMed1975

Binding of progesterone to the proteins of the uterine luminal fluid. Identification of uteroglobin as the binding protein.

1. The uterine luminal fluid of rabbits treated with estradiol and progesterone contains a protein factor with high affinity for [3-H] progesterone which is not present in the uterine secretion of control rabbits treated with estradiol. 2. This progesterone dependent factor is shown by gel filtration and polyacrylamide gel electrophoresis to be identical with the uterus specific protein uteroglobin, which seems to be required during the preimplantation phase. Uteroglobin specific antiserum, prepared in guinea pigs, completely inhibits the progesterone binding activity of the proteins of the uterine fluid. 3. Progesterone binding to uteroglobin is dependent upon millimolar concentrations of dithioerythritol. At saturation, one molecule of progesterone binds per uteroglobin molecule and the apparent association constant is 2 x 10-6 M-1 at 0 degrees C. 4. The progesterone binding species of uteroglobin exhibits a molecular weight of around 12 000 on polyacrylamide gels containing dodecylsulfate, and of 15 000 upon gel filtration, indicating a non-globular shape. This molecule is compased of two subunits of similar molecular size which are held together by a disulfide bridge among other forces.

Animals↗
PubMed1979

[Confirmation of the presence of uteroglobin in tubal secretions].

The acrylamide gel electrophoresis of rabbit serum, of rabbit tubal secretions at the oestrus stage (STO) and at the luteal stage (STL), followed by immunodiffusion with anti-serum, was done to detect any tubal proteins which were not found in the rabbit serum. The anti-rabbit STO goat anti-serum was absorbed with rabbit plasma in order to purify antibodies to proteins found specifically in tubal secretions. This technique revealed the presence of a protein (STx) in STO and STL but not in the rabbit serum. The electrophoretic migration (Rf = 0.72) of the tubal protein (STx) is similar to uteroglobin (Rf = 0.74). The tubal protein was detected immunologically only in tissues where uteroglobin had been found by other workers: lungs, semen, Fallopian tubes and uterine secretions (5 days post-ovulation); further more a complete identity for the precipitating line existed between these extracts. These results corroborate the presence of uteroglobin or of a very similar protein in oestrus of luteal tubal secretions and in some other rabbit tissues.

Animals↗
PubMed1978

Evidence of a uteroglobin-like protein in epithelial cells of reproductive and non-reproductive tissues of the rabbit.

An antiserum raised in a goat to a uteroglobin-like protein isolated from uterine fluid of oestrous rabbits was used in an immune fluorescence test to localize an antigen present in the reproductive tract of oestrous and pseudopregnant rabbits and mammary gland tissue. The antigen was also present in the vas deferens and seminal vesicle, but not in testis. Non-reproductive tissues, such as lung, small intestine, bladder and thyroid showed specific fluorescent staining which was eliminated or significantly reduced by absorption of the antiserum with a purified uteroglobin preparation.

Animals↗
PubMed1978

Non-specific effects of passive immunization on implantation in the rabbit.

Passive immunization with goat anti-rabbit uteroglobin antiserum prevents implantation in the rabbit. The dose of antiserum was too low to neutralize all of the uteroglobin present on Day 5 of pregnancy, however, and the effect could not be shown to be specific, because 'control' treatments with goat antiserum to chick avidin or normal goat serum also prevented implantation. Non-specific antisera raised in rabbits had little or no effect on implantation. Partial purification of antibodies from the non-specific goat antisera reversed their effect, while anti-uteroglobin gamma globulin still reduced implantation. Fluorescein-labelled gamma globulin fractions of anti-avidin and anti-uteroglobin both bound to blastocysts, but pure FITC-IgG showed binding only of anti-uteroglobin. Both anti-avidin and anti-uteroglobin IgG prevented implantation. It is concluded that the effect on implantation is not necessarily achieved via a specific antigen.

Animals↗
PubMed1979

Immunohistochemical localization of secretory proteins in the endometrial epithelium of the rabbit.

Proteins of uterine fluid and lung homogenates of the rabbit were separated by gel and ion exchange chromatography. Purified protein fractions were used for immunisation and antiserum production. By means of several absorptions, six monospecific antisera against uteroglobin and five other proteins were obtained. Using immunohistochemistry, four of them could be localised in the uterine epithelium from oestrus and the first and the seventh day post coitum, and also in the blastocyst. The present study indicates the involvement of different endometrial cells in the synthesis and release of the various proteins of uterine secretion.

Animals↗
PubMed1978

Amino acid sequence of a progesterone-binding protein.

The amino acid sequence of blastokinin, also called uteroglobin, has been determined by a combined study of both the intact native molecule and the peptide fragments resulting from tryptic and chymotryptic digestions. Sequence analyses performed by automated methods and by sequential digestion with leucine aminopeptidase and carboxypeptidase Y demonstrate that blastokinin is a dimer of identical 69-amino acid subunits held together in parallel orientation by two disulfide bridges at positions 3 and 68. The polypeptide chains are further characterized by the absence of tryptophan residues and by single residues of histidine and tyrosine at positions 8 and 21, respectively. Six of eight amino acids, positions 17--24, near the progesterone binding site of blastokinin contain a hydroxyl group. Knowledge of the chemistry of this receptor site should allow better perspectives of the chemistry of molecules in normal tissues that are dependent on progesterone for growth and development, as well as compounds that could act as cancer antagonists for endocrine therapy of hormone-dependent tumors.

Amino Acid Sequence↗
PubMed1978

Significance of maternal uterine proteins in the establishment of pregnancy.

Mammalian embryonic development depends on extrinsic support by the maternal organism. During the preimplantation period the growing blastocyst needs favourable environmental conditions, which are provided by endometrial transformations and secretion. The macromolecular composition of uterine secretion at different times before implantation is characterized by a spectrum of protein patterns which change daily. In an attempt to shed light on the significance of the uterine secretion proteins, particularly uteroglobin in the rabbit, in the establishment of early pregnancy, analyses are reported which demonstrate the origin and endocrine control of the synthesis and release of these proteins. In a comparative study of blastocyst development in vivo and in vitro the significance and consequences of asynchrony between the embryonic and maternal reproductive phases are investigated. Particular attention is drawn to uterine influences on the rabbit blastocyst coverings, and how embryonic development can be retarded by abnormal structural transformation of the zona pellucida and the mucin coat. Finally, the covenient experimental systems of pseudopregnancy and of delayed uterine secretion in the rabbit permit an approach the question of whether the uterine macromolecular components constitute a maternal response to the presence of the as yet unimplanted blastocyst.

Animals↗
PubMedDate not supplied

Hormonal regulation of cultured rabbit endometrial cells.

A technique for culturing primary explants of rabbit endometrial cells in chemically defined medium has been developed. Diethylstilbestrol and natural estrogens were found to increase the rate of DNA initiation while progesterone had the opposite effect. Ultrastructural studies revealed that with estrogens, the cultures had the appearance of rapidly dividing cells having large euchromatic nuclei and prominent nucleoli, with aboundant free ribosomes in the cytoplasm. On the other hand, progesterone induced the formation of large multinucleated cells and also converted the cells to a more secretory type. When the cultures appear secretory, a protein called blastokinin (uteroglobin) is believed secreted. We have found that cultured cells synthesize blastokinin and progesterone is necessary for its continuous synthesis. The cultures were found to have receptors for the ovarian hormones and these receptors exhibited saturation kinetics. The dissociation constants for the receptors were also determined. A hypothetical model for the hormonal regulation of cell proliferation and differentiation is proposed.

Animals↗
PubMed1977

Induction of uterine protein synthesis by synthetic progestins.

The capacity of artificial progestins, each possessing a C-19 methyl group, to stimulate protein synthesis in the uteri of castrated New Zealand White rabbits was studied in an attempt to screen for this type of progestational activity. It is apparent that modifications of the 4-pregnen-3,20-dione molecule not only alter total protein production, but also effect changes in the synthesis of the uterine protein, blastokinin, in comparison with the effect of unaltered progesterone. This indicates that altering the molecular configuration of progesterone offers contraceptive potential through its ability to influence the preimplantation uterine environment.

Animals↗
PubMed2026

Pulmonary fibrosis after COVID-19 is characterized by airway abnormalities and elevated club cell secretory protein-16.

BACKGROUNDThere are no known serum biomarkers that provide mechanistic insight or prognostic enrichment for post-COVID-19 pulmonary fibrosis.METHODSWe tested associations of serum biomarkers with radiographic fibrosis-like abnormalities (reticulation, traction bronchiectasis, or honeycombing) on thoracic computed tomography (CT) scans 4 months, 15 months, and 3 years after hospitalization in an American discovery cohort of severe-to-critical COVID-19 survivors, and externally validated findings in 2 Canadian cohorts of moderate-to-critical COVID-19 survivors. In the discovery cohort, we investigated the dose-response relationship of the biomarker with CT-derived airway-to-lung ratio. We performed single-cell RNA sequencing (scRNA-seq) of transbronchial lung biopsies from COVID-19 survivors obtained 3 years after COVID-19 hospitalization and conducted immunofluorescence analysis of COVID-19 lung explants.RESULTSAmong 150 discovery cohort participants, only higher levels of circulating club cell secretory protein-16 (CC16, encoded by the SCGB1A1 gene) at hospital discharge, 4 months, 15 months, and 3 years were associated with thoracic CT fibrosis-like abnormalities in cross-sectional and longitudinal analyses. Higher CC16 levels were associated with thoracic CT fibrosis-like abnormalities in 2 validation cohorts (n = 56 and n = 37). CC16 levels were linearly associated with increased airway-to-lung ratio. scRNA-seq revealed increased proportions of epithelial cells expressing SCGB1A1 and SCGB1A1/MUC5B in COVID-19 survivors with fibrosis. Immunofluorescence analysis of COVID-19 lung explants demonstrated increased numbers of SCGB1A1-expressing epithelial cells only in small (<100 &#x3bc;m) airways, with 3-fold more CC16/MUC5B-coexpressing cells in respiratory bronchioles..CONCLUSION. Higher CC16 levels are associated with CT fibrosis-like abnormalities for up to 3 years following moderate-to-critical COVID-19. Increased CC16 reflects dysregulated small airway epithelial progenitor cell remodeling and increased expansion of CC16+MUC5B+ epithelial cells in respiratory bronchioles after COVID-19.TRIAL REGISTRATIONNot applicable.FUNDINGDepartment of Defense, NIH, and Japan Society for the Promotion of Science for Young Scientists.

Humans↗