You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on DrugBank.
Identification
NameFollitropin beta
Accession NumberDB00066  (BIOD00064, BIOD00099, BTD00064, BTD00099)
Typebiotech
Groupsapproved
Description

Follitropin beta is a human follicle stimulating hormone (FSH) preparation of recombinant DNA origin, which consists of two non-covalently linked, non-identical glycoproteins designated as the alpha- and beta- subunits. The alpha- and beta- subunits have 92 and 111 amino acids. The alpha subunit is glycosylated at Asn 51 and Asn 78 while the beta subunit is glycosylated at Asn 7 and Asn 24. Follitropin beta is produced in genetically engineered Chinese hamster cell lines (CHO). The nomenclature “beta” differentiates it from another recombinant human FSH product that was marketed earlier as follitropin alpha. Follitropin is important in the development of follicles produced by the ovaries. Given by subcutaneous injection, it is used in combination with human chorionic gonadotropin (hCG) to assist in ovulation and fertility. Follitropin may also be used to cause the ovary to produce several follicles, which can then be harvested for use in gamete intrafallopian transfer (GIFT) or in vitro fertilization (IVF). Numerous physio-chemical tests and bioassays indicate that follitropin beta and follitropin alpha are indistinguishable. However, a more recent study showed there is may be a slight clinical difference, with the alpha form tending towards a higher pregnancy rate and the beta form tending towards a lower pregnancy rate, but with significantly higher estradiol (E2) levels. Structural analysis shows that the amino acid sequence of follitropin beta is identical to that of natural human follicle stimulating hormone (FSH). Further, the ogliosaccharide side chains are very similar, but not completely identical to that of natural FSH. However, these small differences do not affect the bioactivity compared to natural FSH.

Protein structureDb00066
Protein chemical formulaC975H1513N267O304S26
Protein average weight22672.9000
Sequences
>Alpha chain
APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCC
VAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
>Beta chain
NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYET
VRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE
Download FASTA Format
Synonyms
SynonymLanguageCode
Follicle stimulating hormone betaNot AvailableNot Available
Follicle-stimulating hormone beta subunitNot AvailableNot Available
Follitrophin betaNot AvailableNot Available
Follitropin betaNot AvailableNot Available
Follitropin beta chain precursorNot AvailableNot Available
FSH-bNot AvailableNot Available
FSH-BNot AvailableNot Available
FSH-betaNot AvailableNot Available
SaltsNot Available
Brand names
NameCompany
FollistimOrganon
PuregonMerck & Co., Inc.
Brand mixturesNot Available
Categories
CAS number9002-68-0
Taxonomy
KingdomOrganic Compounds
SuperclassOrganic Acids
ClassCarboxylic Acids and Derivatives
SubclassAmino Acids, Peptides, and Analogues
Direct parentPeptides
Alternative parentsNot Available
SubstituentsNot Available
Classification descriptionNot Available
Pharmacology
IndicationFor treatment of female infertility
PharmacodynamicsUsed for the treatment of female infertility, Follitropin beta or follicle stimulating hormone (FSH) stimulates ovarian follicular growth in women who do not have primary ovarian failure. FSH, the active component of Follitropin beta is the primary hormone responsible for follicular recruitment and development.
Mechanism of actionFollitropin alpha is a recombinant form of endogenous follicle stimulating hormone (FSH). FSH binds to the follicle stimulating hormone receptor which is a G-coupled transmembrane receptor. Binding of the FSH to its receptor seems to induce phosphorylation and activation of the PI3K (Phosphatidylinositol-3-kinase) and Akt signaling pathway, which is known to regulate many other metabolic and related survival/maturation functions in cells.
Absorption74%
Volume of distribution
  • 8 L [female subjects following intravenous administration of a 300 IU dose]
Protein bindingNot Available
Metabolism
Route of eliminationVia liver and kidneys
Half lifeCirculation half life of 3-4 hours, elimination half life of 35-40 hours
Clearance
  • 0.01 1*h-1kg-1 [European women with a single intramuscular dose of 300 IU]
  • 0.01 1*h-1kg-1 [Japanese women with a single intramuscular dose of 300 IU]
ToxicityNot Available
Affected organisms
  • Humans and other mammals
PathwaysNot Available
SNP Mediated EffectsNot Available
SNP Mediated Adverse Drug ReactionsNot Available
Pharmacoeconomics
Manufacturers
  • Organon usa inc
  • Emd serono inc
Packagers
Dosage forms
FormRouteStrength
Injection, powder, lyophilized, for solutionIntramuscular
Injection, powder, lyophilized, for solutionSubcutaneous
Prices
Unit descriptionCostUnit
Gonal-f rff 900 unit pen1409.62USDml
Follistim AQ 900unt/1.08ml Solution 1 Cartridge = 1.17ml1366.71USDcartridge
Follistim AQ 600unt/0.72ml Solution 0.78ml Cartridge911.14USDcartridge
Gonal-f 450 unit Solution Vial733.0USDvial
Gonal-f rff 450 unit pen704.81USDpen
Gonal-f rff 300 unit pen469.87USDpen
Follistim AQ 300unt/0.36ml Solution 0.42ml Cartridge455.57USDcartridge
Follistim aq 300 unit cartridge438.05USDcartridge
Follistim aq 150 unit vial219.02USDvial
Gonal-f rff 75 unit vial117.47USDvial
Follistim aq 75 unit vial109.51USDvial
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
CountryPatent NumberApprovedExpires (estimated)
United States77412682004-04-022024-04-02
United States52700571994-03-202011-03-20
Canada20378842003-10-212011-03-08
Properties
Stateliquid
Experimental Properties
PropertyValueSource
melting point55 °CForastieri, H., Ingham, K.C. J. Biol. Chem. 257:7976-7981 (1982)
hydrophobicity-0.330Not Available
isoelectric point7.50Not Available
References
Synthesis ReferenceNot Available
General Reference
  1. Goa KL, Wagstaff AJ: Follitropin alpha in infertility: a review. BioDrugs. 1998 Mar;9(3):235-60. Pubmed
External Links
ResourceLink
UniProtP01225
GenbankM16647
PharmGKBPA449693
Drug Product Database2243949
RxListhttp://www.rxlist.com/cgi/generic3/follitrop.htm
Drugs.comhttp://www.drugs.com/cdi/follitropin-alfa-powder.html
WikipediaFollicle-stimulating_hormone
ATC CodesG03GA06
AHFS CodesNot Available
PDB Entries
FDA labelshow(468 KB)
MSDSNot Available
Interactions
Drug InteractionsSearched, but no interactions found.
Food InteractionsNot Available

Targets

1. Follicle-stimulating hormone receptor

Kind: protein

Organism: Human

Pharmacological action: yes

Actions: agonist

Components

Name UniProt ID Details
Follicle-stimulating hormone receptor P23945 Details

References:

  1. Layman LC: Mutations in the follicle-stimulating hormone-beta (FSH beta) and FSH receptor genes in mice and humans. Semin Reprod Med. 2000;18(1):5-10. Pubmed
  2. Leng N, Dattatreyamurty B, Reichert LE Jr: Identification of amino acid residues 300-315 of the rat FSH receptor as a hormone binding domain: evidence for its interaction with specific regions of FSH beta-subunit. Biochem Biophys Res Commun. 1995 May 16;210(2):392-9. Pubmed
  3. Santa Coloma TA, Dattatreyamurty B, Reichert LE Jr: A synthetic peptide corresponding to human FSH beta-subunit 33-53 binds to FSH receptor, stimulates basal estradiol biosynthesis, and is a partial antagonist of FSH. Biochemistry. 1990 Feb 6;29(5):1194-200. Pubmed
  4. Dattatreyamurty B, Reichert LE Jr: Identification of regions of the follitropin (FSH) beta-subunit that interact with the N-terminus region (residues 9-30) of the FSH receptor. Mol Cell Endocrinol. 1993 May;93(1):39-46. Pubmed
  5. Lindau-Shepard B, Roth KE, Dias JA: Identification of amino acids in the C-terminal region of human follicle-stimulating hormone (FSH) beta-subunit involved in binding to human FSH receptor. Endocrinology. 1994 Sep;135(3):1235-40. Pubmed
  6. Goa KL, Wagstaff AJ: Follitropin alpha in infertility: a review. BioDrugs. 1998 Mar;9(3):235-60. Pubmed
  7. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. Pubmed

Comments
comments powered by Disqus
Drug created on June 13, 2005 07:24 / Updated on July 29, 2014 11:18