Lipid signaling
From Proteopedia
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*Microsomal [[Prostaglandin E synthase]] (PGES) converts cyclooxygenase (COX)-derived prostaglandin to PGE2. It is membrane-associated and belongs to the microsomal glutathione S-transferase family. PGES is preferentially linked with the inducible COX-2<ref>PMID:12432931</ref> . PGES is induced by proinflammatory stimuli and down-regulated by anti-inflammatory '''glucocorticoids'''<ref>PMID:16336776</ref>. | *Microsomal [[Prostaglandin E synthase]] (PGES) converts cyclooxygenase (COX)-derived prostaglandin to PGE2. It is membrane-associated and belongs to the microsomal glutathione S-transferase family. PGES is preferentially linked with the inducible COX-2<ref>PMID:12432931</ref> . PGES is induced by proinflammatory stimuli and down-regulated by anti-inflammatory '''glucocorticoids'''<ref>PMID:16336776</ref>. | ||
| - | + | ''Mineralocorticoids'' | |
*[[Mineralocorticoid receptor]] | *[[Mineralocorticoid receptor]] | ||
| - | + | ''Androgens'' | |
*[[Androgen receptor]] | *[[Androgen receptor]] | ||
*[[Heat shock factor]] (HSF) are transcriptional activators of heat shock genes. HSF bind to heat shock sequence elements throughout the genome with a consensus array of three oppositely oriented sequence AGGAN and activate transcription. Each HSF monomer contains one C-terminal and 3 N-terminal leucine zippers. Two sequences flanking the N-terminal leucine zippers contain the consensus nuclear localization signal (NLS). The DNA-binding domain (DBD residues 193-281) of HSF lies in the N-terminal of the first NLS region<ref>PMID:8441385</ref>. Depletion of HSF-1 is associated with accumulation of pathogenic [[androgen receptor]] in neurodegenerative diseases<ref>PMID:23360996</ref>. | *[[Heat shock factor]] (HSF) are transcriptional activators of heat shock genes. HSF bind to heat shock sequence elements throughout the genome with a consensus array of three oppositely oriented sequence AGGAN and activate transcription. Each HSF monomer contains one C-terminal and 3 N-terminal leucine zippers. Two sequences flanking the N-terminal leucine zippers contain the consensus nuclear localization signal (NLS). The DNA-binding domain (DBD residues 193-281) of HSF lies in the N-terminal of the first NLS region<ref>PMID:8441385</ref>. Depletion of HSF-1 is associated with accumulation of pathogenic [[androgen receptor]] in neurodegenerative diseases<ref>PMID:23360996</ref>. | ||
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*[[Zolinza (Vorinostat)]] | *[[Zolinza (Vorinostat)]] | ||
| - | + | ''Estrogens'' | |
*[[Estrogen receptor]] | *[[Estrogen receptor]] | ||
*[[Ivan Koutsopatriy estrogen receptor]] | *[[Ivan Koutsopatriy estrogen receptor]] | ||
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*[[Finasteride]] | *[[Finasteride]] | ||
| - | + | ''Progestogens'' | |
| - | + | Progesterone | |
*[[Progesterone receptor]] | *[[Progesterone receptor]] | ||
Progesterone is a negative allosteric modulator of [[nicotinic acetylcholine receptors]], and a potent antagonist of the [[mineralocorticoid receptor]]. | Progesterone is a negative allosteric modulator of [[nicotinic acetylcholine receptors]], and a potent antagonist of the [[mineralocorticoid receptor]]. | ||
Revision as of 14:32, 2 November 2021
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See also:
References
- ↑ Chatterjee S. Neutral sphingomyelinase: past, present and future. Chem Phys Lipids. 1999 Nov;102(1-2):79-96. PMID:11001563
- ↑ Tuteja G, Kaestner KH. SnapShot: forkhead transcription factors I. Cell. 2007 Sep 21;130(6):1160. PMID:17889656 doi:http://dx.doi.org/10.1016/j.cell.2007.09.005
- ↑ Kaiser G, Gerst F, Michael D, Berchtold S, Friedrich B, Strutz-Seebohm N, Lang F, Haring HU, Ullrich S. Regulation of forkhead box O1 (FOXO1) by protein kinase B and glucocorticoids: different mechanisms of induction of beta cell death in vitro. Diabetologia. 2013 Jul;56(7):1587-95. doi: 10.1007/s00125-013-2863-7. Epub 2013, Feb 23. PMID:23435785 doi:http://dx.doi.org/10.1007/s00125-013-2863-7
- ↑ Horwitz KB, Jackson TA, Bain DL, Richer JK, Takimoto GS, Tung L. Nuclear receptor coactivators and corepressors. Mol Endocrinol. 1996 Oct;10(10):1167-77. PMID:9121485 doi:http://dx.doi.org/10.1210/mend.10.10.9121485
- ↑ Arner ES, Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem. 2000 Oct;267(20):6102-9. PMID:11012661
- ↑ Prasad R, Chan LF, Hughes CR, Kaski JP, Kowalczyk JC, Savage MO, Peters CJ, Nathwani N, Clark AJ, Storr HL, Metherell LA. Thioredoxin Reductase 2 (TXNRD2) mutation associated with familial glucocorticoid deficiency (FGD). J Clin Endocrinol Metab. 2014 Aug;99(8):E1556-63. doi: 10.1210/jc.2013-3844. Epub, 2014 Mar 6. PMID:24601690 doi:http://dx.doi.org/10.1210/jc.2013-3844
- ↑ Murakami M, Nakatani Y, Tanioka T, Kudo I. Prostaglandin E synthase. Prostaglandins Other Lipid Mediat. 2002 Aug;68-69:383-99. PMID:12432931
- ↑ Kudo I, Murakami M. Prostaglandin E synthase, a terminal enzyme for prostaglandin E2 biosynthesis. J Biochem Mol Biol. 2005 Nov 30;38(6):633-8. PMID:16336776
- ↑ Sarge KD, Murphy SP, Morimoto RI. Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol Cell Biol. 1993 Mar;13(3):1392-407. PMID:8441385
- ↑ Kondo N, Katsuno M, Adachi H, Minamiyama M, Doi H, Matsumoto S, Miyazaki Y, Iida M, Tohnai G, Nakatsuji H, Ishigaki S, Fujioka Y, Watanabe H, Tanaka F, Nakai A, Sobue G. Heat shock factor-1 influences pathological lesion distribution of polyglutamine-induced neurodegeneration. Nat Commun. 2013;4:1405. doi: 10.1038/ncomms2417. PMID:23360996 doi:http://dx.doi.org/10.1038/ncomms2417
- ↑ Ghosh, D., Griswold, J., Erman, M., Pangborn, W. " X-ray Structure of Human Aromatase Reveals An Androgen-Specific Active Site" Journal of Steroid Biochemistry and Molecular Biology. [Online] 2010,Vol. 118, Issue 4-5, p197-202[1]
