+ |
11-deoxycorticosterone | up-regulates activity
chemical activation
|
NR3C1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258713 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
8282004 |
The sex steroid progesterone bound with an affinity (ki < 0.01 nM) even higher than that of aldosterone to the human mineralocorticoid receptor and effectively antagonized the effect of aldosterone via the human mineralocorticoid receptor in functional co-transfection assays. This indicates that progesterone has potent antimineralocorticoid properties, while its antiglucocorticoid effects were less pronounced. The partial agonistic activities of antihormones in this assay suggest a direct interaction of antihormone-receptor complexes with the response elements on the DNA. aldosterone shows a higher functional sensitivity for the human mineralocorticoid receptor than deoxycorticosterone (higher affinity) or cortisol (similar affinity). Moreover, the very high binding affinity of the human mineralocorticoid receptor for progesterone (k i < 0.0l nM) in combination with the very low agonistic activity indicates that progesterone may act as a potent human mineralocorticoid receptor antagonist that is even more effective than spironolactone (k~ = 5.7 nM), which displays no partial agonistic activity (fig. 4). |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
progesterone | up-regulates quantity
precursor of
|
11-deoxycorticosterone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268631 |
|
|
Homo sapiens |
|
pmid |
sentence |
25855791 |
Cytochrome P450 (P450)4 21A2 is the major steroid 21-hydroxylase, which catalyzes the 21-hydroxylation of progesterone and 17alpha-hydroxyprogesterone (17alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
11-deoxycorticosterone | up-regulates activity
chemical activation
|
NR3C2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258714 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
8282004 |
The sex steroid progesterone bound with an affinity (ki < 0.01 nM) even higher than that of aldosterone to the human mineralocorticoid receptor and effectively antagonized the effect of aldosterone via the human mineralocorticoid receptor in functional co-transfection assays. This indicates that progesterone has potent antimineralocorticoid properties, while its antiglucocorticoid effects were less pronounced. The partial agonistic activities of antihormones in this assay suggest a direct interaction of antihormone-receptor complexes with the response elements on the DNA. aldosterone shows a higher functional sensitivity for the human mineralocorticoid receptor than deoxycorticosterone (higher affinity) or cortisol (similar affinity). Moreover, the very high binding affinity of the human mineralocorticoid receptor for progesterone (k i < 0.0l nM) in combination with the very low agonistic activity indicates that progesterone may act as a potent human mineralocorticoid receptor antagonist that is even more effective than spironolactone (k~ = 5.7 nM), which displays no partial agonistic activity (fig. 4). |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
CYP21A2 | up-regulates quantity
chemical modification
|
11-deoxycorticosterone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268645 |
|
|
Homo sapiens |
|
pmid |
sentence |
25855791 |
Cytochrome P450 (P450)4 21A2 is the major steroid 21-hydroxylase, which catalyzes the 21-hydroxylation of progesterone and 17alpha-hydroxyprogesterone (17alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
CYP11B1 | down-regulates quantity
chemical modification
|
11-deoxycorticosterone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268683 |
|
|
Homo sapiens |
|
pmid |
sentence |
33117906 |
The zona glomerulosa lacks the 17alpha-hydroxylase enzyme, committing pregnenolone to the exclusive production of aldosterone.|In the adrenal steroidogenic pathway, 21-hydroxylase (P450c21) catalyzes the conversion of 17-hydroxyprogesterone (17OHP) to 11-deoxycortisol to form cortisol and the conversion of progesterone to 11-deoxycorticosterone to form aldosterone |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
CYP11B2 | down-regulates quantity
chemical modification
|
11-deoxycorticosterone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268681 |
|
|
Homo sapiens |
|
pmid |
sentence |
33117906 |
The zona glomerulosa lacks the 17alpha-hydroxylase enzyme, committing pregnenolone to the exclusive production of aldosterone.|In the adrenal steroidogenic pathway, 21-hydroxylase (P450c21) catalyzes the conversion of 17-hydroxyprogesterone (17OHP) to 11-deoxycortisol to form cortisol and the conversion of progesterone to 11-deoxycorticosterone to form aldosterone |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |
+ |
11-deoxycorticosterone | up-regulates quantity
precursor of
|
corticosterone |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268673 |
|
|
Homo sapiens |
|
pmid |
sentence |
33117906 |
The zona glomerulosa lacks the 17alpha-hydroxylase enzyme, committing pregnenolone to the exclusive production of aldosterone.|In the adrenal steroidogenic pathway, 21-hydroxylase (P450c21) catalyzes the conversion of 17-hydroxyprogesterone (17OHP) to 11-deoxycortisol to form cortisol and the conversion of progesterone to 11-deoxycorticosterone to form aldosterone |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Zona Glomerulosa |
Pathways: | Sex Hormone Biosynthesis |