Drugbank Logo

Showing drug card for Methylprednisolone (DB00959)

Legend: drug field target field enzyme field

for drugs
Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:33
Primary Accession Number DB00959
Secondary Accession Number
  • APRD00342
Name Methylprednisolone
Drug Type
  • Approved
  • Small Molecule
Description A prednisolone derivative with similar anti-inflammatory action. [PubChem]
Synonyms
  1. 6alpha-Methylprednisolone
  2. Methyleneprednisolone
  3. Methylprednisolon
  4. Methylprednisolonum [INN-Latin]
  5. Metilprednisolona [INN-Spanish]
  6. Metilprednisolone [Dcit]
Brand Names
  1. Artisone-Wyeth
  2. Besonia
  3. Dopomedrol
  4. Esametone
  5. Firmacort
  6. Lemod
  7. Medesone
  8. Medixon
  9. Medlone 21
  10. Medrate
  11. Medrol Adt Pak
  12. Medrol Dosepak
  13. Medrone
  14. Mesopren
  15. Metastab
  16. Metilbetasone
  17. Metrisone
  18. Metrocort
  19. Metysolon
  20. Moderin
  21. Nirypan
  22. Noretona
  23. Predni N Tablinen
  24. Promacortine
  25. Reactenol
  26. Sieropresol
  27. Solomet
  28. Summicort
  29. Suprametil
  30. Urbason
  31. Urbasone
  32. Wyacort
Brand Mixtures
  1. Depo-Medrol with Lidocaine (Lidocaine Hydrochloride + Methylprednisolone Acetate)
  2. Medrol Acne Lotion (Aluminum Chlorohydrate + Methylprednisolone Acetate + Sulfur)
  3. Methylprednisolone Sodium Succinate for Injection (Methylprednisolone + Water)
  4. Neo-Medrol (Methylprednisolone Acetate + Neomycin Sulfate)
  5. Neo-Medrol Acne Lotion (Aluminum Chlorohydrate + Methylprednisolone Acetate + Neomycin Sulfate + Sulfur)
Chemical IUPAC Name (6S,8S,9S,10R,11S,13S,14S,17R)-11,17-dihydroxy-17-(2-hydroxyacetyl)-6,10,13-trimethyl-7,8,9,11,12,14,15,16-octahydro-6H-cyclopenta[a]phenanthren-3-one
Chemical Formula C22H30O5
Chemical Structure Structure
CAS Registry Number 83-43-2
InChI Identifier InChI=1/C22H30O5/c1-12-8-14-15-5-7-22(27,18(26)11-23)21(15,3)10-17(25)19(14)20(2)6-4-13(24)9-16(12)20/h4,6,9,12,14-15,17,19,23,25,27H,5,7-8,10-11H2,1-3H3/t12-,14-,15-,17-,19+,20-,21-,22-/m0/s1
InChI Key VHRSUDSXCMQTMA-PJHHCJLFBP
KEGG Drug D00407 Link Image
KEGG Compound Not Available
PubChem Compound 6741 Link Image
PubChem Substance 149724 Link Image
ChEBI ID Not Available
PharmGKB ID PA450466 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02245406 Link Image
RxList Link http://www.rxlist.com/cgi/generic/methprd.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Methylprednisolone Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Sebek, Spero, U.S. Pat. 2,897,218 (1959)
Average Molecular Weight 374.4706
Monoisotopic Molecular Weight 374.2093
State Solid
Melting Point 232.5 oC
Experimental Water Solubility 120 mg/L Source: PhysProp
Predicted Water Solubility 1.09e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 1.5 Source: PhysProp
Predicted LogP 2.06 Calculated using ALOGPS
Experimental LogS -2.99 [ADME Research, USCD]
Predicted LogS -3.54 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES C[C@H]1C[C@H]2[C@@H]3CC[C@](O)(C(=O)CO)[C@@]3(C)C[C@H](O)[C@@H]2[C@@]2(C)C=CC(=O)C=C12
Canonical SMILES CC1CC2C3CCC(O)(C(=O)CO)C3(C)CC(O)C2C2(C)C=CC(=O)C=C12
Drug Category
  • Adrenergic Agents
  • Anti-inflammatory Agents
  • Antiemetics
  • Glucocorticoids
  • Neuroprotective Agents
ATC Codes
AHFS Codes
  • 68:04.00
Indication Adjunctive therapy for short-term administration in rheumatoid arthritis.
Pharmacology Methylprednisolone and its derivatives, methylprednisolone sodium succinate and methylprednisolone acetate, are synthetic glucocorticoids used as antiinflammatory or immunosuppressive agents.
Mechanism of Action Unbound glucocorticoids cross cell membranes and bind with high affinity to specific cytoplasmic receptors, modifying transcription and protein synthesis. By this mechanism, glucocorticoids can inhibit leukocyte infiltration at the site of inflammation, interfere with mediators of inflammatory response, and suppress humoral immune responses. The antiinflammatory actions of corticosteroids are thought to involve phospholipase A2 inhibitory proteins, lipocortins, which control the biosynthesis of potent mediators of inflammation such as prostaglandins and leukotrienes.
Absorption Oral bioavailability 80-99%
Toxicity LD50=2000 mg/kg (orally in rat)
Protein Binding 78%
Biotransformation Hepatic
Half Life 1-3 hours
Dosage Forms
Form Route
Powder Intramuscular
Powder Intravenous
Powder, for solution Intravenous
Suspension Intramuscular
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Annexin A1
  2. Glucocorticoid receptor
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Drug Target 1 [top]
Target 1 ID 469
Target 1 Name Annexin A1
Target 1 Synonyms
  1. Annexin I
  2. Calpactin II
  3. Chromobindin-9
  4. Lipocortin I
  5. Phospholipase A2 inhibitory protein
  6. p35
Target 1 Gene Name ANXA1
Target 1 Protein Sequence >Annexin A1 
AMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVD
EATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDAD
ELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALL
SLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYT
KYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMV
SRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
Target 1 Number of Residues 350
Target 1 Molecular Weight 38583
Target 1 Theoretical pI 7.04
Target 1 GO Classification
Function
enzyme regulator activity
enzyme inhibitor activity
phospholipase inhibitor activity
lipid binding
phospholipid binding
calcium-dependent phospholipid binding
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 1 General Function Involved in calcium ion binding
Target 1 Specific Function Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 12654863 Link Image
Target 1 UniProtKB/Swiss-Prot ID P04083 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ANXA1_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >1041 bp 
ATGGCAATGGTATCAGAATTCCTCAAGCAGGCCTGGTTTATTGAAAATGAAGAGCAGGAA
TATGTTCAAACTGTGAAGTCATCCAAAGGTGGTCCCGGATCAGCGGTGAGCCCCTATCCT
ACCTTCAATCCATCCTCGGATGTCGCTGCCTTGCATAAGGCCATAATGGTTAAAGGTGTG
GATGAAGCAACCATCATTGACATTCTAACTAAGCGAAACAATGCACAGCGTCAACAGATC
AAAGCAGCATATCTCCAGGAAACAGGAAAGCCCCTGGATGAAACACTTAAGAAAGCCCTT
ACAGGTCACCTTGAGGAGGTTGTTTTAGCTCTGCTAAAAACTCCAGCGCAATTTGATGCT
GATGAACTTCGTGCTGCCATGAAGGGCCTTGGAACTGATGAAGATACTCTAATTGAGATT
TTGGCATCAAGAACTAACAAAGAAATCAGAGACATTAACAGGGTCTACAGAGAGGAACTG
AAGAGAGATCTGGCCAAAGACATAACCTCAGACACATCTGGAGATTTTCGGAACGCTTTG
CTTTCTCTTGCTAAGGGTGACCGATCTGAGGACTTTGGTGTGAATGAAGACTTGGCTGAT
TCAGATGCCAGGGCCTTGTATGAAGCAGGAGAAAGGAGAAAGGGGACAGACGTAAACGTG
TTCAATACCATCCTTACCACCAGAAGCTATCCACAACTTCGCAGAGTGTTTCAGAAATAC
ACCAAGTACAGTAAGCATGACATGAACAAAGTTCTGGACCTGGAGTTGAAAGGTGACATT
GAGAAATGCCTCACAGCTATCGTGAAGTGCGCCACAAGCAAACCAGCTTTCTTTGCAGAG
AAGCTTCATCAAGCCATGAAAGGTGTTGGAACTCGCCATAAGGCATTGATCAGGATTATG
GTTTCCCGTTCTGAAATTGACATGAATGATATCAAAGCATTCTATCAGAAGATGTATGGT
ATCTCCCTTTGCCAAGCCATCCTGGATGAAACCAAAGGAGATTATGAGAAAATCCTGGTG
GCTCTTTGTGGAGGAAACTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ANXA1 Link Image
Target 1 GenAtlas ID ANXA1 Link Image
Target 1 HGNC ID HGNC:533 Link Image
Target 1 Chromosome Location 9
Target 1 Locus 9q12-q21.2|9q12-q21.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Kovacic RT, Tizard R, Cate RL, Frey AZ, Wallner BP: Correlation of gene and protein structure of rat and human lipocortin I. Biochemistry. 1991 Sep 17;30(37):9015-21. [PubMed Link Image]
  2. Varticovski L, Chahwala SB, Whitman M, Cantley L, Schindler D, Chow EP, Sinclair LK, Pepinsky RB: Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C. Biochemistry. 1988 May 17;27(10):3682-90. [PubMed Link Image]
  3. Pepinsky RB, Sinclair LK, Chow EP, O'Brine-Greco B: A dimeric form of lipocortin-1 in human placenta. Biochem J. 1989 Oct 1;263(1):97-103. [PubMed Link Image]
  4. Wallner BP, Mattaliano RJ, Hession C, Cate RL, Tizard R, Sinclair LK, Foeller C, Chow EP, Browing JL, Ramachandran KL, et al.: Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity. Nature. 1986 Mar 6-12;320(6057):77-81. [PubMed Link Image]
  5. Biemann K, Scoble HA: Characterization by tandem mass spectrometry of structural modifications in proteins. Science. 1987 Aug 28;237(4818):992-8. [PubMed Link Image]
  6. Arcone R, Arpaia G, Ruoppolo M, Malorni A, Pucci P, Marino G, Ialenti A, Di Rosa M, Ciliberto G: Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli. Eur J Biochem. 1993 Jan 15;211(1-2):347-55. [PubMed Link Image]
  7. Weng X, Luecke H, Song IS, Kang DS, Kim SH, Huber R: Crystal structure of human annexin I at 2.5 A resolution. Protein Sci. 1993 Mar;2(3):448-58. [PubMed Link Image]
  8. Gao J, Li Y, Yan H: NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit. J Biol Chem. 1999 Jan 29;274(5):2971-7. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 871
Target 2 Name Glucocorticoid receptor
Target 2 Synonyms
  1. GR
Target 2 Gene Name NR3C1
Target 2 Protein Sequence >Glucocorticoid receptor 
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRR
LLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLK
LLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGN
VKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGN
SNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTV
YCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVG
SENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKL
CLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRK
CLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIE
PEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSW
MFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSY
EEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTK
LLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
Target 2 Number of Residues 789
Target 2 Molecular Weight 85660
Target 2 Theoretical pI 6.31
Target 2 GO Classification
Function
transcription factor activity
steroid binding
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
glucocorticoid receptor activity
binding
nucleic acid binding
DNA binding
Process
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus
Target 2 General Function Involved in DNA binding
Target 2 Specific Function Receptor for glucocorticoids (GC). Has a dual mode of action:as a transcription factor that binds to glucocorticoid response elements (GRE) and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 31680 Link Image
Target 2 UniProtKB/Swiss-Prot ID P04150 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name GCR_HUMAN Link Image
Target 2 PDB ID 1NHZ Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm. Nucleus. Cytoplasmic in the absence of ligand
  • nuclear after ligand-binding
Target 2 Gene Sequence >2334 bp 
ATGGACTCCAAAGAATCATTAACTCCTGGTAGAGAAGAAAACCCCAGCAGTGTGCTTGCT
CAGGAGAGGGGAGATGTGATGGACTTCTATAAAACCCTAAGAGGAGGAGCTACTGTGAAG
GTTTCTGCGTCTTCACCCTCACTGGCTGTCGCTTCTCAATCAGACTCCAAGCAGCGAAGA
CTTTTGGTTGATTTTCCAAAAGGCTCAGTAAGCAATGCGCAGCAGCCAGATCTGTCCAAA
GCAGTTTCACTCTCAATGGGACTGTATATGGGAGAGACAGAAACAAAAGTGATGGGAAAT
GACCTGGGATTCCCACAGCAGGGCCAAATCAGCCTTTCCTCGGGGGAAACAGACTTAAAG
CTTTTGGAAGAAAGCATTGCAAACCTCAATAGGTCGACCAGTGTTCCAGAGAACCCCAAG
AGTTCAGCATCCACTGCTGTGTCTGCTGCCCCCACAGAGAAGGAGTTTCCAAAAACTCAC
TCTGATGTATCTTCAGAACAGCAACATTTGAAGGGCCAGACTGGCACCAACGGTGGCAAT
GTGAAATTGTATACCACAGACCAAAGCACCTTTGACATTTTGCAGGATTTGGAGTTTTCT
TCTGGGTCCCCAGGTAAAGAGACGAATGAGAGTCCTTGGAGATCAGACCTGTTGATAGAT
GAAAACTGTTTGCTTTCTCCTCTGGCGGGAGAAGACGATTCATTCCTTTTGGAAGGAAAC
TCGAATGAGGACTGCAAGCCTCTCATTTTACCGGACACTAAACCCAAAATTAAGGATAAT
GGAGATCTGGTTTTGTCAAGCCCCAGTAATGTAACACTGCCCCAAGTGAAAACAGAAAAA
GAAGATTTCATCGAACTCTGCACCCCTGGGGTAATTAAGCAAGAGAAACTGGGCACAGTT
TACTGTCAGGCAAGCTTTCCTGGAGCAAATATAATTGGTAATAAAATGTCTGCCATTTCT
GTTCATGGTGTGAGTACCTCTGGAGGACAGATGTACCACTATGACATGAATACAGCATCC
CTTTCTCAACAGCAGGATCAGAAGCCTATTTTTAATGTCATTCCACCAATTCCCGTTGGT
TCCGAAAATTGGAATAGGTGCCAAGGATCTGGAGATGACAACTTGACTTCTCTGGGGACT
CTGAACTTCCCTGGTCGAACAGTTTTTTCTAATGGCTATTCAAGCCCCAGCATGAGACCA
GATGTAAGCTCTCCTCCATCCAGCTCCTCAACAGCAACAACAGGACCACCTCCCAAACTC
TGCCTGGTGTGCTCTGATGAAGCTTCAGGATGTCATTATGGAGTCTTAACTTGTGGAAGC
TGTAAAGTTTTCTTCAAAAGAGCAGTGGAAGGACAGCACAATTACCTATGTGCTGGAAGG
AATGATTGCATCATCGATAAAATTCGAAGAAAAAACTGCCCAGCATGCCGCTATCGAAAA
TGTCTTCAGGCTGGAATGAACCTGGAAGCTCGAAAAACAAAGAAAAAAATAAAAGGAATT
CAGCAGGCCACTACAGGAGTCTCACAAGAAACCTCTGAAAATCCTGGTAACAAAACAATA
GTTCCTGCAACGTTACCACAACTCACCCCTACCCTGGTGTCACTGTTGGAGGTTATTGAA
CCTGAAGTGTTATATGCAGGATATGATAGCTCTGTTCCAGACTCAACTTGGAGGATCATG
ACTACGCTCAACATGTTAGGAGGGCGGCAAGTGATTGCAGCAGTGAAATGGGCAAAGGCA
ATACCAGGTTTCAGGAACTTACACCTGGATGACCAAATGACCCTACTGCAGTACTCCTGG
ATGTTTCTTATGGCATTTGCTCTGGGGTGGAGATCATATAGACAATCAAGTGCAAACCTG
CTGTGTTTTGCTCCTGATCTGATTATTAATGAGCAGAGAATGACTCTACCCTGCATGTAC
GACCAATGTAAACACATGCTGTATGTTTCCTCTGAGTTACACAGGCTTCAGGTATCTTAT
GAAGAGTATCTCTGTATGAAAACCTTACTGCTTCTCTCTTCAGTTCCTAAGGACGGTCTG
AAGAGCCAAGAGCTATTTGATGAAATTAGAATGACCTACATCAAAGAGCTAGGAAAAGCC
ATTGTCAAGAGGGAAGGAAACTCCAGCCAGAACTGGCAGCGGTTTTATCAACTGACAAAA
CTCTTGGATTCTATGCATGAAGTGGTTGAAAATCTCCTTAACTATTGCTTCCAAACATTT
TTGGATAAGACCATGAGTATTGAATTCCCCGAGATGTTAGCTGAAATCATCACCAATCAG
ATACCAAAATATTCAAATGGAAATATCAAAAAACTTCTGTTTCATCAAAAGTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID NR3C1 Link Image
Target 2 GenAtlas ID NR3C1 Link Image
Target 2 HGNC ID HGNC:7978 Link Image
Target 2 Chromosome Location 5
Target 2 Locus 5q31.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  2. Schneikert J, Hubner S, Martin E, Cato AC: A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J Cell Biol. 1999 Sep 6;146(5):929-40. [PubMed Link Image]
  3. Rivers C, Levy A, Hancock J, Lightman S, Norman M: Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing. J Clin Endocrinol Metab. 1999 Nov;84(11):4283-6. [PubMed Link Image]
  4. Diamond MI, Robinson MR, Yamamoto KR: Regulation of expanded polyglutamine protein aggregation and nuclear localization by the glucocorticoid receptor. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):657-61. [PubMed Link Image]
  5. Mahajan MA, Samuels HH: A new family of nuclear receptor coregulators that integrate nuclear receptor signaling through CREB-binding protein. Mol Cell Biol. 2000 Jul;20(14):5048-63. [PubMed Link Image]
  6. Feng J, Zheng J, Bennett WP, Heston LL, Jones IR, Craddock N, Sommer SS: Five missense variants in the amino-terminal domain of the glucocorticoid receptor: no association with puerperal psychosis or schizophrenia. Am J Med Genet. 2000 Jun 12;96(3):412-7. [PubMed Link Image]
  7. Kayes-Wandover KM, White PC: Steroidogenic enzyme gene expression in the human heart. J Clin Endocrinol Metab. 2000 Jul;85(7):2519-25. [PubMed Link Image]
  8. Strickland I, Kisich K, Hauk PJ, Vottero A, Chrousos GP, Klemm DJ, Leung DY: High constitutive glucocorticoid receptor beta in human neutrophils enables them to reduce their spontaneous rate of cell death in response to corticosteroids. J Exp Med. 2001 Mar 5;193(5):585-93. [PubMed Link Image]
  9. Dobson MG, Redfern CP, Unwin N, Weaver JU: The N363S polymorphism of the glucocorticoid receptor: potential contribution to central obesity in men and lack of association with other risk factors for coronary heart disease and diabetes mellitus. J Clin Endocrinol Metab. 2001 May;86(5):2270-4. [PubMed Link Image]
  10. Yudt MR, Cidlowski JA: Molecular identification and characterization of a and b forms of the glucocorticoid receptor. Mol Endocrinol. 2001 Jul;15(7):1093-103. [PubMed Link Image]
  11. 11555652 Wallace AD, Cidlowski JA: Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem. 2001 Nov 16;276(46):42714-21. Epub 2001 Sep 12.
  12. 11589680 Ruiz M, Lind U, Gafvels M, Eggertsen G, Carlstedt-Duke J, Nilsson L, Holtmann M, Stierna P, Wikstrom AC, Werner S: Characterization of two novel mutations in the glucocorticoid receptor gene in patients with primary cortisol resistance. Clin Endocrinol (Oxf). 2001 Sep;55(3):363-71.
  13. 11701741 Kino T, Stauber RH, Resau JH, Pavlakis GN, Chrousos GP: Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking. J Clin Endocrinol Metab. 2001 Nov;86(11):5600-8.
  14. 11932321 Mendonca BB, Leite MV, de Castro M, Kino T, Elias LL, Bachega TA, Arnhold IJ, Chrousos GP, Latronico AC: Female pseudohermaphroditism caused by a novel homozygous missense mutation of the GR gene. J Clin Endocrinol Metab. 2002 Apr;87(4):1805-9.
  15. 12000743 Wang Z, Frederick J, Garabedian MJ: Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo. J Biol Chem. 2002 Jul 19;277(29):26573-80. Epub 2002 May 8.
  16. 12050230 Vottero A, Kino T, Combe H, Lecomte P, Chrousos GP: A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators. J Clin Endocrinol Metab. 2002 Jun;87(6):2658-67.
  17. 12144530 Tian S, Poukka H, Palvimo JJ, Janne OA: Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Biochem J. 2002 Nov 1;367(Pt 3):907-11.
  18. 12151000 Bledsoe RK, Montana VG, Stanley TB, Delves CJ, Apolito CJ, McKee DD, Consler TG, Parks DJ, Stewart EL, Willson TM, Lambert MH, Moore JT, Pearce KH, Xu HE: Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell. 2002 Jul 12;110(1):93-105.
  19. 12415108 Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1.
  20. 12686538 Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, Calles K, Engstrom O, Harlan J, Muchmore S, Ramqvist AK, Thorell S, Ohman L, Greer J, Gustafsson JA, Carlstedt-Duke J, Carlquist M: The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem. 2003 Jun 20;278(25):22748-54. Epub 2003 Apr 9.
  21. 1704018 Hurley DM, Accili D, Stratakis CA, Karl M, Vamvakopoulos N, Rorer E, Constantine K, Taylor SI, Chrousos GP: Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance. J Clin Invest. 1991 Feb;87(2):680-6.
  22. 1707881 Encio IJ, Detera-Wadleigh SD: The genomic structure of the human glucocorticoid receptor. J Biol Chem. 1991 Apr 15;266(11):7182-8.
  23. 1958537 Govindan MV, Pothier F, Leclerc S, Palaniswami R, Xie B: Human glucocorticoid receptor gene promotor-homologous down regulation. J Steroid Biochem Mol Biol. 1991;40(1-3):317-23.
  24. 2026589 Leclerc S, Xie BX, Roy R, Govindan MV: Purification of a human glucocorticoid receptor gene promoter-binding protein. Production of polyclonal antibodies against the purified factor. J Biol Chem. 1991 May 15;266(14):8711-9.
  25. 2867473 Hollenberg SM, Weinberger C, Ong ES, Cerelli G, Oro A, Lebo R, Thompson EB, Rosenfeld MG, Evans RM: Primary structure and expression of a functional human glucocorticoid receptor cDNA. Nature. 1985 Dec 19-1986 Jan 1;318(6047):635-41.
  26. 3841189 Weinberger C, Hollenberg SM, Rosenfeld MG, Evans RM: Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product. Nature. 1985 Dec 19-1986 Jan 1;318(6047):670-2.
  27. 7683692 Malchoff DM, Brufsky A, Reardon G, McDermott P, Javier EC, Bergh CH, Rowe D, Malchoff CD: A mutation of the glucocorticoid receptor in primary cortisol resistance. J Clin Invest. 1993 May;91(5):1918-25.
  28. 8316249 Ashraf J, Thompson EB: Identification of the activation-labile gene: a single point mutation in the human glucocorticoid receptor presents as two distinct receptor phenotypes. Mol Endocrinol. 1993 May;7(5):631-42.
  29. 8358712 Moalli PA, Pillay S, Krett NL, Rosen ST: Alternatively spliced glucocorticoid receptor messenger RNAs in glucocorticoid-resistant human multiple myeloma cells. Cancer Res. 1993 Sep 1;53(17):3877-9.
  30. 8358735 Powers JH, Hillmann AG, Tang DC, Harmon JM: Cloning and expression of mutant glucocorticoid receptors from glucocorticoid-sensitive and -resistant human leukemic cells. Cancer Res. 1993 Sep 1;53(17):4059-65.
  31. 8445027 Karl M, Lamberts SW, Detera-Wadleigh SD, Encio IJ, Stratakis CA, Hurley DM, Accili D, Chrousos GP: Familial glucocorticoid resistance caused by a splice site deletion in the human glucocorticoid receptor gene. J Clin Endocrinol Metab. 1993 Mar;76(3):683-9.
  32. 9150737 Koper JW, Stolk RP, de Lange P, Huizenga NA, Molijn GJ, Pols HA, Grobbee DE, Karl M, de Jong FH, Brinkmann AO, Lamberts SW: Lack of association between five polymorphisms in the human glucocorticoid receptor gene and glucocorticoid resistance. Hum Genet. 1997 May;99(5):663-8.
  33. 9154805 Henriksson A, Almlof T, Ford J, McEwan IJ, Gustafsson JA, Wright AP: Role of the Ada adaptor complex in gene activation by the glucocorticoid receptor. Mol Cell Biol. 1997 Jun;17(6):3065-73.
  34. 9590696 Fryer CJ, Archer TK: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature. 1998 May 7;393(6680):88-91.
Target 2 Drug References
  1. Juruena MF, Cleare AJ, Papadopoulos AS, Poon L, Lightman S, Pariante CM: Different responses to dexamethasone and prednisolone in the same depressed patients. Psychopharmacology (Berl). 2006 Dec;189(2):225-35. Epub 2006 Oct 3. [PubMed Link Image]
  2. Boivin MA, Ye D, Kennedy JC, Al-Sadi R, Shepela C, Ma TY: Mechanism of glucocorticoid regulation of the intestinal tight junction barrier. Am J Physiol Gastrointest Liver Physiol. 2007 Feb;292(2):G590-8. Epub 2006 Oct 26. [PubMed Link Image]
  3. Hirose Y, Tabuchi K, Oikawa K, Murashita H, Sakai S, Hara A: The effects of the glucocorticoid receptor antagonist RU486 and phospholipase A2 inhibitor quinacrine on acoustic injury of the mouse cochlea. Neurosci Lett. 2007 Feb 8;413(1):63-7. Epub 2006 Dec 4. [PubMed Link Image]
  4. Owen HC, Miner JN, Ahmed SF, Farquharson C: The growth plate sparing effects of the selective glucocorticoid receptor modulator, AL-438. Mol Cell Endocrinol. 2007 Jan 29;264(1-2):164-70. Epub 2006 Dec 19. [PubMed Link Image]
  5. Quesnell RR, Han X, Schultz BD: Glucocorticoids stimulate ENaC upregulation in bovine mammary epithelium. Am J Physiol Cell Physiol. 2007 May;292(5):C1739-45. Epub 2007 Jan 24. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.