| + |
11-deoxycortisol | up-regulates quantity
precursor of
|
cortisol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268675 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9814482 |
Recombinant CYP11B genes encode enzymes that can catalyze conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol, and 18-oxocortisol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Fasciculata |
| Pathways: | Steroid Hormone Biosynthesis |
| + |
CYP11B2 | up-regulates quantity
chemical modification
|
cortisol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268676 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9814482 |
Recombinant CYP11B genes encode enzymes that can catalyze conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol, and 18-oxocortisol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Fasciculata |
| Pathways: | Steroid Hormone Biosynthesis |
| + |
cortisol | up-regulates activity
chemical activation
|
NR3C2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258707 |
|
|
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 |
| + |
MC2R | up-regulates quantity
|
cortisol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268621 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20371771 |
Here, we show that, whereas MRAP was essential for activation of MC2R signaling, MRAP2 was an endogenous inhibitor that competed with MRAP for binding to MC2R and decreased the potency of adrenocorticotropic hormone (ACTH), the endogenous agonist for MC2Rs, in stimulating the production of adenosine 3',5'-monophosphate (cAMP). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Adrenal Gland |
| + |
CYP11B1 | up-regulates quantity
chemical modification
|
cortisol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268678 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9814482 |
Recombinant CYP11B genes encode enzymes that can catalyze conversion of 11-deoxycortisol to cortisol, 18-hydroxycortisol, and 18-oxocortisol. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Fasciculata |
| Pathways: | Steroid Hormone Biosynthesis |
| + |
cortisol | up-regulates activity
chemical activation
|
NR3C1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258708 |
|
|
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 |