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Section I: Research Areas<br />
8<br />
2012–2014 citations<br />
<strong>CST</strong> antibodies for Androgen Receptor<br />
have been cited over 8 times in<br />
high-impact, peer-reviewed publications<br />
from the global research community.<br />
Select Citations:<br />
Cuenca-Lopez, M.D. et al. (2014)<br />
Phospho-kinase profile of triple<br />
negative breast cancer and androgen<br />
receptor signaling. BMC Cancer<br />
14, 302.<br />
Boll, K. et al. (2013) MiR-130a,<br />
miR-203 and miR-205 jointly repress<br />
key oncogenic pathways and are<br />
downregulated in prostate carcinoma.<br />
Oncogene 32, 277−285.<br />
Krycer, J.R. et al. (2013) Does changing<br />
androgen receptor status during<br />
prostate cancer development impact<br />
upon cholesterol homeostasis PLoS<br />
One 8, e54007.<br />
Nie, H. et al. (2013) Acetylcholine<br />
acts on androgen receptor to promote<br />
the migration and invasion but inhibit<br />
the apoptosis of human hepatocarcinoma.<br />
PLoS One 8, e61678.<br />
Furu, K. et al. (2013) Tzfp represses<br />
the androgen receptor in mouse<br />
testis. PLoS One 8, e62314.<br />
Li, Y. et al. (2013) Functional domains<br />
of androgen receptor coactivator p44/<br />
Mep50/WDR77and its interaction<br />
with Smad1. PLoS One 8, e64663.<br />
Ota, H. et al. (2012) Testosterone<br />
deficiency accelerates neuronal<br />
and vascular aging of SAMP8 mice:<br />
protective role of eNOS and SIRT1.<br />
PLoS One 7, e29598.<br />
Krycer, J.R. et al. (2011) Cross-talk<br />
between the androgen receptor and<br />
the liver X receptor: implications for<br />
cholesterol homeostasis. J. Biol.<br />
Chem. 286, 20637−20647.<br />
Type II Nuclear Receptors<br />
Type II nonsteroid nuclear receptors include the thyroid hormone receptors (TRα and β), retinoic acid<br />
receptors (RARα, β, and γ), vitamin D receptor (VDR), and peroxisome proliferator-activated receptors<br />
(PPARα, β, and γ). Members of this family heterodimerize with the retinoid X receptor (RXR). Prior to<br />
ligand binding, receptor heterodimers are located in the nucleus as part of complexes with histone<br />
deacetylases (HDACs) and other co-repressors that keep target DNA in a tightly wound conformation,<br />
preventing exposure to transacting factors. Ligand binding results in co-repressor dissociation,<br />
chromatin derepression, and transcriptional activation.<br />
RARγ1, a type II nuclear receptor that regulates expression<br />
of genes involved in cellular differentiation, proliferation, and<br />
apoptosis, is expressed in cancer cells and epidermal cells.<br />
RARγ1 (D3A4) XP ® Rabbit mAb #8965:<br />
WB analysis of extracts from various cell lines<br />
(A) using #8965. IHC analysis of paraffinembedded<br />
human skin (B) using #8965.<br />
Lanes<br />
1. HaCaT<br />
2. A-375<br />
3. BxPC-3<br />
4. T-47D<br />
5. SK-BR-3<br />
A<br />
kDa<br />
100<br />
80<br />
60<br />
50<br />
40<br />
1 2 3 4 5<br />
Orphan Nuclear Receptors<br />
Orphan nuclear receptors are nuclear receptors where the endogenous ligands have not been identified.<br />
Structural studies suggest that some of the orphan receptors may not bind ligands. This class of nuclear<br />
receptors includes small heterodimer partner (SHP), reverse orientation c-ErbA (Rev-Erbα and β),<br />
testicular receptor 2 and 4 (TR2 and 4), tailless homolog orphan receptor (TLX), photoreceptor-specific<br />
NR (PNR), chicken ovalbumin upstream promoter transcription factor 1 and 2 (COUP-TF1 and 2), Nur77,<br />
Nur-related protein 1 (NURR1), neuron derived orphan receptor 1 (NOR1), estrogen-related receptor<br />
(ERR α, β, and γ), and germ cell nuclear factor (GCNF). Most of these receptors regulate transcription<br />
by binding to their target DNA elements either as monomers or homodimers and recruiting chromatin<br />
modifying coactivators and the transcription machinery. Nur77 and NURR1 can also heterodimerize<br />
with RXRs and these heterodimers are able to respond to RXR ligands to regulate transcription.<br />
Rev-Erbα (E1Y6D) Rabbit mAb #13418: Chromatin IPs were performed<br />
with cross-linked chromatin from 4 x 10 6 Hep G2 cells and either 10 μl of<br />
#13418 or 2 μl of Normal Rabbit IgG #2729 using SimpleChIP ® Enzymatic<br />
Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified<br />
by real-time PCR using human BMAL1 promoter primers, SimpleChIP ® Human<br />
NR1D1 Promoter Primers #13413, and SimpleChIP ® Human α Satellite<br />
Repeat Primers #4486. The amount of immunoprecipitated DNA in each<br />
sample is represented as a percent of the total input chromatin.<br />
Rev-Erbα (E1Y6D) Rabbit<br />
mAb #13418<br />
Normal Rabbit<br />
IgG #2729<br />
% of total input chromatin<br />
RARγ1<br />
Rev-Erbα, an orphan nuclear receptor involved in<br />
cell proliferation, differentiation, and circadian rhythms.<br />
0.7<br />
0.6<br />
0.5<br />
0.4<br />
0.3<br />
0.2<br />
0.1<br />
0<br />
BMAL1<br />
NR1D1<br />
B<br />
α Satellite<br />
chapter 01: GENE EXPRESSION, EPIGENETICS, AND NUCLEAR FUNCTION<br />
Select Reviews<br />
Ahmadian, M., Suh, J.M., and Hah, N. et al. (2013) Nat. Med. 19, 557−566. • Bondesson, M., Hao, R., Lin, C.Y., Williams, C., and Gustafsson, J.A. (2014) Biochim.<br />
Biophys. Acta. Jun 17 [Epub ahead of print]. • Evans, R.M. and Mangelsdorf, D.J. (2014) Cell 157, 255−266. • Kojetin, D.J. and Burris, T.P. (2014) Nat. Rev. Drug Discov.<br />
13, 197−216. • Kurakula, K., Koenis, D.S., van Tiel, C.M., and de Vries, C.J. (2014) Biochim. Biophys. Acta. 1843, 2543–2555. • Manolagas, S.C., O’Brien, C.A., and<br />
Almeida, M. (2013) Nat. Rev. Endocrinol. 9, 699−712. • Zhou, W. and Slingerland, J.M. (2014) Nat. Rev. Cancer 14, 26−38.<br />
Nuclear Receptors Signaling<br />
HSP90<br />
Type I Steroid Receptors (Homodimers)<br />
NR<br />
NR<br />
NR<br />
NR<br />
HRE<br />
SBP<br />
HSP90<br />
Homodimerization<br />
SRC1/2 PRMT/<br />
CARM<br />
CBP/<br />
p300 PCAF<br />
RNA<br />
TBP TFIIB POLII<br />
TATA<br />
Plasma Membrane<br />
Cytoplasm<br />
Nucleus<br />
Transcriptional<br />
Activation<br />
Type IIa Non-steroid Receptors (RXR Heterodimers)<br />
Heterodimerization<br />
NcoR1<br />
SMRT<br />
RXR<br />
NR<br />
Ligand<br />
Plasma Membrane<br />
Cytoplasm<br />
Nucleus<br />
Type IIb Orphan Receptors (Monomers and Homodimers)<br />
NcoR1<br />
SMRT<br />
NR<br />
NR<br />
RXR<br />
NR<br />
HRE<br />
HDAC<br />
Complex<br />
No Ligand<br />
Transcriptional Repression<br />
NR<br />
NR<br />
HRE<br />
HDAC<br />
Complex<br />
SRC1/2<br />
PRMT/<br />
CARM<br />
CBP/<br />
p300 PCAF<br />
RNA<br />
TBP TFIIB POLII<br />
SRC1/2<br />
PRMT/<br />
CARM<br />
CBP/<br />
p300 PCAF<br />
RNA<br />
TBP TFIIB POLII<br />
Constitutive<br />
Transcriptional<br />
Repression<br />
Transcriptional<br />
Activation<br />
Nucleus<br />
Constitutive<br />
Transcriptional<br />
Activation<br />
Nur77, an orphan<br />
nuclear receptor<br />
involved in cell<br />
proliferation,<br />
differentiation,<br />
and apoptosis<br />
Nur77 (D63C5) XP ® Rabbit mAb #3960:<br />
Confocal IF analysis of Jurkat cells, untreated<br />
(left) or treated with TPA #4174 and A23187<br />
(right), using #3960 (green). Actin filaments<br />
were labeled with DY-554 phalloidin (red).<br />
© 2012–2015 Cell Signaling Technology, Inc.<br />
40 For Research Use Only. Not For Use in Diagnostic Procedures. See pages 302 & 303 for Pathway Diagrams, Application, and Reactivity keys.<br />
www.cellsignal.com/cstpathways 41
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