Ontogeny of oestrogen-sensitive mesenchymal cells in the bursa of Fabricius of the chick embryo. An immunohistochemical study on progesterone receptor

Development ◽  
1987 ◽  
Vol 101 (1) ◽  
pp. 61-66
Author(s):  
T. Ylikomi ◽  
J.M. Gasc ◽  
P. Tuohimaa ◽  
E.E. Baulieu
Keyword(s):  
Progesterone Receptor ◽  
Polyclonal Antibodies ◽  
Mesenchymal Cells ◽  
Bursa Of Fabricius ◽  
Exogenous Oestrogen ◽  
Sensitive Organ ◽  
Chicken Oviduct ◽  
Embryonic Life ◽  
Endogenous Oestrogen ◽  
Haemopoietic Cells

The expression of progesterone receptor (PR) and its induction by oestradiol during the embryogenesis of the chick bursa of Fabricius (BF) were studied by immunohistochemistry using three different polyclonal antibodies to the chicken oviduct PR. Mesenchymal cells of the cloacal area surrounding the bursa primordium in controls (without exogenous oestrogen) express the PR between 9 and 11 days of incubation. In the same cells, PR was induced experimentally by oestradiol at 9 days. Mesenchymal cells in the bursa did not express PR after oestradiol treatment before the age of 11 days. The PR was not inducible in the bursal epithelium or in haemopoietic cells. None of the bursal cells expressed the PR to a detectable level during embryonic life without exogenous treatment. Some haemopoietic cells showed strong artefactual staining in their nuclei. It is concluded that (1) the embryonic bursa of Fabricius is a sex-steroid-sensitive organ, (2) exogenous oestradiol is able to induce progesterone receptor in the mesenchymal cells, but (3) the PR is not expressed without exogenous oestrogen. This indicates that the PR becomes oestrogen inducible well before it is naturally expressed during sexual maturation and that the level of endogenous oestrogen during embryonic life is not high enough to affect the bursa significantly.

scholarly journals Progesterone receptor in the chick oviduct: an immunohistochemical study with antibodies to distinct receptor components.

1984 ◽  
Vol 99 (4) ◽  
pp. 1193-1201 ◽  
Author(s):  
J M Gasc ◽  
J M Renoir ◽  
C Radanyi ◽  
I Joab ◽  
P Tuohimaa ◽  
...  
Keyword(s):  
Progesterone Receptor ◽  
Polyclonal Antibodies ◽  
Smooth Muscles ◽  
Immunoperoxidase Technique ◽  
Cell Nuclei ◽  
Receptor Complexes ◽  
B Subunit ◽  
Chicken Oviduct ◽  
A Subunit ◽  
Immunohistochemical Studies

We performed immunohistochemical studies of chicken oviduct after different fixation procedures, by using antibodies against the progesterone receptor: polyclonal antibodies IgG-G3 against the "8S" form (an oligomere containing progesterone-binding and nonprogesterone-binding units), polyclonal antibodies IgG-RB against the progesterone-binding B subunit, and monoclonal BF4 against the non-progesterone-binding 90,000-mol-wt protein component. Chickens were immature animals with or without estrogen priming, and with or without progesterone treatment. The antibodies were revealed by means of an immunoperoxidase technique that used the avidin-biotin-peroxidase complex, and controls were performed by presaturation of antibodies with the purified 8S-progesterone receptor, the B subunit, and 90,000-mol-wt protein. The progesterone receptor was detected not only in well-characterized target tissues, i.e., in glands and luminal epithelium, but also in stromal cells (some displayed the strongest reaction), in mesothelium, and in fibers of smooth muscles. Only in cell nuclei, whether or not the animals received an injection of progesterone was an antigen revealed corresponding to the B subunit (and/or to the A subunit, because there is immunoreactivity of IgG-RB with both hormone-binding subunits A and B). The 90,000-mol-wt protein was revealed in both cytoplasm and nuclei. These immunohistological data suggest that the concept of steroid action that necessarily involves the original formation of the hormone-receptor complexes in the cytoplasm before translocation to the nucleus, may have to be revised.

scholarly journals Phosphorylation in vivo of chicken oviduct progesterone receptor.

1982 ◽  
Vol 257 (23) ◽  
pp. 14226-14230
Author(s):  
J J Dougherty ◽  
R K Puri ◽  
D O Toft
Keyword(s):  
Progesterone Receptor ◽  
Chicken Oviduct

scholarly journals Monoclonal antibody to chicken oviduct progesterone receptor.

1983 ◽  
Vol 80 (10) ◽  
pp. 2854-2858 ◽  
Author(s):  
C. Radanyi ◽  
I. Joab ◽  
J. M. Renoir ◽  
H. Richard-Foy ◽  
E. E. Baulieu
Keyword(s):  
Monoclonal Antibody ◽  
Progesterone Receptor ◽  
Chicken Oviduct

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

1994 ◽  
Vol 14 (3) ◽  
pp. 1956-1963
Author(s):  
J L Johnson ◽  
T G Beito ◽  
C J Krco ◽  
D O Toft
Keyword(s):  
Progesterone Receptor ◽  
Cdna Clone ◽  
Peptide Fragments ◽  
Receptor Complexes ◽  
Human Cdna ◽  
Partial Clone ◽  
Chicken Oviduct ◽  
Brain Cdna Library ◽  
Carboxy Terminal ◽  
And Function

Immunoprecipitation of unactivated avian progesterone receptor results in the copurification of hsp90, hsp70, and three additional proteins, p54, p50, and p23. p23 is also present in immunoaffinity-purified hsp90 complexes along with hsp70 and another protein, p60. Antibody and cDNA probes for p23 were prepared in an effort to elucidate the significance and function of this protein. Antibodies to p23 detect similar levels of p23 in all tissues tested and cross-react with a protein of the same size in mice, rabbits, guinea pigs, humans, and Saccharomyces cerevisiae, indicating that p23 is a conserved protein of broad tissue distribution. These antibodies were used to screen a chicken brain cDNA library, resulting in the isolation of a 468-bp partial cDNA clone encoding a sequence containing four sequences corresponding to peptide fragments isolated from chicken p23. This partial clone was subsequently used to isolate a full-length human cDNA clone. The human cDNA encodes a protein of 160 amino acids that does not show homology to previously identified proteins. The chicken and human cDNAs are 88% identical at the DNA level and 96.3% identical at the protein level. p23 is a highly acidic phosphoprotein with an aspartic acid-rich carboxy-terminal domain. Bacterially overexpressed human p23 was used to raise several monoclonal antibodies to p23. These antibodies specifically immunoprecipitate p23 in complex with hsp90 in all tissues tested and can be used to immunoaffinity isolate progesterone receptor complexes from chicken oviduct cytosol.

Structural analysis of chicken oviduct progesterone receptor using monoclonal antibodies to the subunit B protein

Biochemistry ◽  
1984 ◽  
Vol 23 (19) ◽  
pp. 4427-4435 ◽  
Author(s):  
Dean P. Edwards ◽  
Nancy L. Weigel ◽  
William T. Schrader ◽  
Bert W. O'Malley ◽  
William L. McGuire
Keyword(s):  
Monoclonal Antibodies ◽  
Structural Analysis ◽  
Progesterone Receptor ◽  
Chicken Oviduct ◽  
Subunit B

Changes in the distribution of tenascin during tooth development

Development ◽  
1987 ◽  
Vol 101 (2) ◽  
pp. 289-296 ◽  
Author(s):  
I. Thesleff ◽  
E. Mackie ◽  
S. Vainio ◽  
R. Chiquet-Ehrismann
Keyword(s):  
Tooth Development ◽  
Polyclonal Antibodies ◽  
Staining Intensity ◽  
Mesenchymal Cells ◽  
Hard Tissue ◽  
Connective Tissues ◽  
Odontoblast Differentiation ◽  
Dental Papilla ◽  
Extracellular Matrix Molecule ◽  
Dental Papilla Cells

Tenascin is an extracellular matrix molecule that was earlier shown to be enriched in embryonic mesenchyme surrounding the budding epithelium in various organs including the tooth. In the present study tenascin was localized by immunohistology throughout the course of tooth development in the mouse and rat using polyclonal antibodies against chick tenascin. The results indicate that tenascin is expressed by the lineage of dental mesenchymal cells throughout tooth ontogeny. The intensity of staining with tenascin antibodies in the dental papilla mesenchyme was temporarily reduced at cap stage when the tooth grows rapidly and undergoes extensive morphogenetic changes. During the bell stage of morphogenesis, the staining intensity increased and tenascin was accumulated in the dental pulp even after completion of crown development and eruption. Tenascin was present in the dental basement membrane at the time of odontoblast differentiation. The dental papilla cells ceased to express tenascin upon differentiation into odontoblasts and tenascin was completely absent from dentin. It can be speculated that the remarkable expression of tenascin in the dental mesenchymal cells as compared to other connective tissues is associated with their capacity to differentiate into hard-tissue-forming cells.

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