Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 61 to 64 of 64

Publication Record

Connections

Inhibition of nuclear hormone receptor activity by calreticulin.
Dedhar S, Rennie PS, Shago M, Hagesteijn CY, Yang H, Filmus J, Hawley RG, Bruchovsky N, Cheng H, Matusik RJ
(1994) Nature 367: 480-3
MeSH Terms: Amino Acid Sequence, Androgen Receptor Antagonists, Animals, Base Sequence, Calcium-Binding Proteins, Calreticulin, Cell Line, Cell Nucleus, DNA, Gene Expression Regulation, Integrins, Molecular Sequence Data, Rats, Receptors, Androgen, Receptors, Retinoic Acid, Ribonucleoproteins, Tumor Cells, Cultured, Vero Cells
Show Abstract · Added June 11, 2010
We have shown that a polypeptide of M(r) 60,000 (60K) that shares N-terminal homology with a calcium-binding protein, calreticulin, can bind to an amino-acid sequence motif, KXGFFKR, found in the cytoplasmic domains of all integrin alpha-subunits. The homologous amino-acid sequence, KXFFKR (where X is either G, A or V), is also present in the DNA-binding domain of all known members of the steroid hormone receptor family; amino acids in this sequence make direct contact with nucleotides in their DNA-responsive elements and are crucial for DNA binding. Here we show that both the 60K protein (p60), purified on a KLGFFKR-Sepharose affinity matrix, and recombinant calreticulin can inhibit the binding of androgen receptor to its hormone-responsive DNA element in a KXFFKR-sequence-specific manner. Calreticulin can also inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Our results indicate that calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors.
1 Communities
1 Members
0 Resources
18 MeSH Terms
Cooperative binding of androgen receptors to two DNA sequences is required for androgen induction of the probasin gene.
Kasper S, Rennie PS, Bruchovsky N, Sheppard PC, Cheng H, Lin L, Shiu RP, Snoek R, Matusik RJ
(1994) J Biol Chem 269: 31763-9
MeSH Terms: Androgen-Binding Protein, Androgens, Base Sequence, Binding Sites, DNA-Binding Proteins, Gene Expression Regulation, Humans, In Vitro Techniques, Macromolecular Substances, Molecular Sequence Data, Oligodeoxyribonucleotides, RNA, Messenger, Receptor Aggregation, Receptors, Androgen, Regulatory Sequences, Nucleic Acid, Tumor Cells, Cultured
Show Abstract · Added June 11, 2010
The functional and structural interactions of two androgen receptor-binding sites in the 5'-flanking DNA of the rat probasin gene were determined. Deletion mapping and DNase I footprinting analysis had previously identified two androgen receptor-binding sites (ARBS) necessary for androgen induction of the probasin gene: ARBS-1, which resembled a glucocorticoid-responsive element, and ARBS-2, which had a unique sequence. In this study, maximal androgen induction in transient transfection studies only occurred when both sites were present. Neither binding site functioned independently, and deletion of the DNA sequence between the sites resulted in a 60% loss of androgen inducibility. Moreover, point mutations in either ARBS-1 or ARBS-2 led to > 90% loss in activity. Scatchard analysis indicated that ARBS-1 and ARBS-2 bound a synthetic androgen receptor, AR2, with Kd values of 20.0 and 6.7 nM, respectively. Consistent with the higher affinity, ARBS-2 bound AR2 at half the threshold concentration (200 ng) of that required in reciprocal DNase I footprinting experiments with ARBS-1. By comparison, protection occurred at a much lower threshold concentration of AR2 (60 ng) and to the same extent over each site when both sites were present, suggesting a cooperative interaction between the two sites. The cooperative effect was further substantiated when a point mutation in ARBS-1 blocked AR2 binding not only to ARBS-1, but also to ARBS-2. Similarly, a point mutation in ARBS-2 also prevented receptor binding to both sites. Androgen-specific regulation of probasin gene transcription therefore required an androgen-responsive region (positions -286 and +28) containing two androgen receptor-binding sites, where the binding of the androgen receptor to both sites occurred in a cooperative, mutually dependent manner.
1 Communities
1 Members
0 Resources
16 MeSH Terms
Effect of retinoic acid on the proliferation and secretory activity of androgen-responsive prostatic carcinoma cells.
Fong CJ, Sutkowski DM, Braun EJ, Bauer KD, Sherwood ER, Lee C, Kozlowski JM
(1993) J Urol 149: 1190-4
MeSH Terms: Androgens, Cell Division, Dihydrotestosterone, Flow Cytometry, Humans, Male, Metribolone, Prostate-Specific Antigen, Prostatic Neoplasms, Receptors, Androgen, Testosterone, Tretinoin, Tumor Cells, Cultured
Show Abstract · Added October 18, 2015
We studied the effect of retinoic acid on the growth and secretory activity of the androgen-responsive prostatic carcinoma cell line LNCaP. Our data showed that retinoic acid at 0.01 microM. stimulated the proliferation of LNCaP cells but inhibited their growth at 0.1 microM. under androgen-free conditions. In the presence of 0.1 nM. dihydrotestosterone (DHT), LNCaP cell proliferation was inhibited by 10 microM. retinoic acid but not by lower concentrations of retinoic acid. Retinoic acid reduced LNCaP cell growth at concentrations of 0.1 microM. in the presence of 10 nM. DHT. Retinoic acid (10 microM.) also reduced the growth response of LNCaP cells to epidermal growth factor and transforming growth factor alpha and potentiated the inhibitory effect of transforming growth factor beta. In additional studies, retinoic acid induced a dose-dependent increase in prostate specific antigen (PSA) secretion at concentrations of 0.1 to 1 microM. Dihydrotestosterone (10 nM.) also enhanced the secretion of PSA by LNCaP cells, and this effect was potentiated in a dose-dependent fashion by the addition of retinoic acid at 0.1-10 microM. Competitive binding studies showed that retinoic acid did not bind to androgen receptors. Overall, retinoic acid had a biphasic effect on LNCaP proliferation and promoted the secretion of PSA. The biphasic effect of retinoic acid on LNCaP growth should be considered in designing in vivo studies to determine the impact of retinoic acid on solid prostatic tumor growth. In addition, the ability of retinoic acid to increase PSA secretion may complicate the interpretation of serum PSA levels used for diagnostic and prognostic purposes.
0 Communities
1 Members
0 Resources
13 MeSH Terms
Establishment and characterization of an immortalized but non-transformed human prostate epithelial cell line: BPH-1.
Hayward SW, Dahiya R, Cunha GR, Bartek J, Deshpande N, Narayan P
(1995) In Vitro Cell Dev Biol Anim 31: 14-24
MeSH Terms: Aged, Aneuploidy, Animals, Antigens, Polyomavirus Transforming, Base Sequence, Cell Division, Cell Line, Epithelial Cells, Humans, Immunohistochemistry, Karyotyping, Keratins, Male, Mice, Mice, Nude, Molecular Sequence Data, Prostate, RNA, Messenger, Receptors, Androgen, Testosterone, Tumor Suppressor Protein p53
Show Abstract · Added May 27, 2014
This report describes the development and characterization of an epithelial cell line (BPH-1) from human prostate tissue obtained by transurethral resection. Primary epithelial cell cultures were immortalized with SV40 large T antigen. One of the isolated clones was designated BPH-1. These cells have a cobblestone appearance in monolayer culture and are non-tumorigenic in nude mice following subcutaneous injection or subrenal capsule grafting. They express the SV40 large T antigen and exhibit increased levels of p53, as determined by immunocytochemistry. Cytogenetic analysis by G-banding demonstrated an aneuploid karyotype with a modal chromosome number of 76 (range 71 to 79, n = 28) and 6 to 8 marker chromosomes. Some structurally rearranged chromosomes were observed, but the Y chromosome was normal. The expressed cytokeratin profile was consistent with a prostatic luminal epithelial cell. This profile was the same as that of primary prostatic epithelial cultures from which the BPH-1 cells were derived. In serum-free culture in plastic dishes epidermal growth factor (EGF), transforming growth factor (TGF)-alpha, fibroblast growth factor (FGF) 1 (aFGF), and FGF 7 (KGF) induced increased proliferation in these cells whereas FGF 2 (bFGF), TGF-beta 1, and TGF-beta 2 inhibited proliferative activity. Testosterone had no direct effect on the proliferative rate of BPH-1 cells. 5 alpha-Reductase, 3 alpha-hydroxysteroid oxidoreductase, and 17 beta-hydroxy-steroid oxidoreductase activities were detected in BPH-1 cells. Expression of androgen receptors and the secretory markers, prostate specific antigen and prostatic acid phosphatase, were not detectable by immunocytochemistry, biochemical assay, or RT-PCR analysis.
0 Communities
1 Members
0 Resources
21 MeSH Terms