Characterization of the proximal estrogen-responsive element of human cathepsin D gene

1994 ◽  
Vol 8 (6) ◽  
pp. 693-703 ◽  
Author(s):  
P. Augereau
Keyword(s):  
Cathepsin D ◽  
Estrogen Responsive Element ◽  
Human Cathepsin ◽  
Responsive Element

scholarly journals Characterization of the proximal estrogen-responsive element of human cathepsin D gene.

1994 ◽  
Vol 8 (6) ◽  
pp. 693-703 ◽  
Author(s):  
P Augereau ◽  
F Miralles ◽  
V Cavaillès ◽  
C Gaudelet ◽  
M Parker ◽  
...  
Keyword(s):  
Cathepsin D ◽  
Estrogen Responsive Element ◽  
Human Cathepsin ◽  
Responsive Element

scholarly journals Real-Time Challenging of ERα Y537S Mutant Transcriptional Activity in Living Cells

Endocrines ◽  
2021 ◽  
Vol 2 (1) ◽  
pp. 54-64
Author(s):  
Manuela Cipolletti ◽  
Sara Pescatori ◽  
Filippo Acconcia
Keyword(s):  
Cell Line ◽  
Transcriptional Activity ◽  
Estrogen Receptor Α ◽  
Living Cells ◽  
Patient Treatment ◽  
Estrogen Responsive Element ◽  
Specific Proteins ◽  
Responsive Element ◽  
Mcf 7

Metastatic estrogen receptor α (ERα)-expressing breast cancer (BC) occurs after prolonged patient treatment with endocrine therapy (ET) (e.g., aromatase inhibitors—AI; 4OH-tamoxifen—4OH-Tam). Often these metastatic BCs express a mutated ERα variant (e.g., Y537S), which is transcriptionally hyperactive, sustains uncontrolled proliferation, and renders tumor cells insensitive to ET drugs. Therefore, new molecules blocking hyperactive Y537S ERα mutation transcriptional activity are requested. Here we generated an MCF-7 cell line expressing the Y537S ERα mutation stably expressing an estrogen-responsive element (ERE) promoter, which activity can be monitored in living cells. Characterization of this cell line shows both hyperactive basal transcriptional activity with respect to normal MCF-7 cells, which stably express the same ERE-based promoter and a decreased effect of selective ER downregulators (SERDs) in reducing Y537S ERα mutant transcriptional activity with respect to wild type ERα transcriptional activity. Kinetic profiles of Y537S ERα mutant-based transcription produced by both drugs inducing receptor degradation and siRNA-mediated depletion of specific proteins (e.g., FOXA1 and caveolin1) reveals biphasic dynamics of the inhibition of the receptor-regulated transcriptional effects. Overall, we report a new model where to study the behavior of the Y537S ERα mutant that can be used for the identification of new targets and pathways regulating the Y537S ERα transcriptional activity.

scholarly journals Production, Characterization, and Epitope Mapping of a Monoclonal Antibody against Aspartic Proteinase ofCandida albicans

1999 ◽  
Vol 6 (3) ◽  
pp. 429-433 ◽  
Author(s):  
Byoung-Kuk Na ◽  
Gyung-Tae Chung ◽  
Chul-Yong Song
Keyword(s):  
Monoclonal Antibody ◽  
Candida Albicans ◽  
Candida Tropicalis ◽  
Cathepsin D ◽  
Epitope Mapping ◽  
Candida Parapsilosis ◽  
Aspartic Proteinase ◽  
Ofcandida Albicans ◽  
Human Cathepsin

ABSTRACT A monoclonal antibody (MAb; MAb CAP1) that was reactive with extracellular aspartic proteinase of Candida albicans (CAP) was produced. The MAb showed strong sensitivity and reactivity to CAP but not to the aspartic proteinases of Candida parapsilosis, Candida tropicalis, andAspergillus fumigatus or to human cathepsin D or porcine pepsin. The epitope of the CAP recognized by the MAb was the proteinaseous part of CAP and the putative epitope of the MAb was located in the Asp77 to Gly103 sequence. This antibody could be useful for the characterization of CAP and would be a valuable probe for the detection of CAP antigen in the sera of patients with invasive candidiasis.

Chemical characterization of cathepsin D inhibitor from potatoes

1977 ◽  
Vol 42 (7) ◽  
pp. 2279-2286 ◽  
Author(s):  
L. Rupova ◽  
H. Keilová ◽  
V. Tomášek
Keyword(s):  
Cathepsin D ◽  
Chemical Characterization
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