NAV

Moroctocog alfa

Identification

Summary

Moroctocog alfa is a recombinant Factor VIII used to treat hemophilia A to control bleeding.

Brand Names
Refacto AF, Xyntha
Generic Name
Moroctocog alfa
DrugBank Accession Number
DB13999
Background

Moroctocog alfa, also known as BDDrFVIII (B domain deleted recombinant factor VIII), is a recombinant DNA-based drug with functional characteristics comparable to those of endogenous coagulation Factor VIII, the essential human blood clotting protein that is impaired in Hemophilia A. Moroctocog alfa is identical in sequence to endogenously produced Factor VIII, but does not contain the B-domain, which has no known biological function. Moroctocog alfa is produced through recombinant DNA technology and purification, resulting in a 1438 amino acid, 170 kDa protein Label. Clinical evaluation has shown that BDDrFVIII is pharmacokinetically equivalent to full-length recombinant FVIII 5,Label.

Also known as Anti-Hemophilic Factor (AHF), endogenous Factor VIII is essential to the clotting process in the body due to its involvement in the clotting cascade where it is responsible for acting as a co-factor to Factor IX. Activation of Factor IX leads to a cascade of signals that results in activation of Factor X, which then results in the conversion of prothrombin to thrombin, and as a result, leads to the conversion of fibrinogen to fibrin, the fibrous protein that creates the scaffold of the clot. Replacement of Factor VIII is essential for the treatment of Hemophilia A, which is caused by mutations in the Factor VIII gene, leading to a functional deficiency or complete loss of protein. Congenital loss or deficiency of Factor VIII results in the physiologic impairment of the coagulation clotting cascade, and as a result, leads to easy bruising and bleeding. Bleeding can range in severity from minor concerns, such as nosebleeds, to more serious events such as hemorrhaging in the joints, brain, or digestive tract 4.

Exogenous replacement of Factor VIII is currently the cornerstone of Hemophilia treatment and is used for the prophylaxis and control of bleeding episodes. Treatment has drastically improved since the 1960s when Factor VIII protein was primarily purified from human plasma, rather than being produced through recombinant DNA technology. Unfortunately, purification of protein from human plasma carries an increased risk of transmission of blood-borne diseases such as HIV and Hepatitis, which in part contributed to the Tainted Blood Scandal in the 1980s 3,2,6. Use of recombinant DNA-derived clotting factor treatments, such as Moroctocog alfa, has reduced this risk.

Other drug products with similar structure and function to Moroctocog alfa include Antihemophilic factor human, which is purified Factor VIII from human pooled blood and contains both A- and B-subunits, and Efmoroctocog alfa, which is a fully recombinant factor VIII-Fc fusion protein which has an extended half-life compared with conventional factor VIII due to conjugation to the dimeric Fc domain of human immunoglobulin G1, a long-lived plasma protein 3.

Moroctocog alfa is approved by Health Canada and by the European Medicines Agency for the control and prevention of hemorrhagic episodes and for routine and surgical prophylaxis in patients with hemophilia A (congenital factor VIII deficiency or classic hemophilia). As it does not contain von Willebrand factor it is not indicated in von Willebrand’s disease Label.

Type
Biotech
Groups
Approved
Biologic Classification
Protein Based Therapies
Blood factors
Protein Chemical Formula
Not Available
Protein Average Weight
173000.0 Da (glycosylated)
Sequences
Not Available
Synonyms
  • Antihemophilic factor (recombinant, B-domain deleted), plasma/albumin free
  • Antihemophilic factor recombinant plasma/albumin free
  • Antihemphilic factor, recombinant human B-domain deleted
  • B-domain deleted recombinant factor VIII
  • BDDrFVIII
  • Human factor VIII, recombinant B-domain deleted
  • Moroctocog alfa
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Pharmacology

Indication

Moroctocog alfa is indicated for use in adults and children with hemophilia A (congenital factor VIII deficiency) for on-demand treatment and control of bleeding episodes, perioperative management, and routine prophylaxis to reduce the frequency of bleeding episodes.7,8,9

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Associated Conditions
Indication TypeIndicationCombined Product DetailsApproval LevelAge GroupPatient CharacteristicsDose Form
Prophylaxis ofBleeding caused by hemophilia a••••••••••••
Management ofBleeding caused by hemophilia a••••••••••••
Management ofBleeding caused by hemophilia a••••••••••••
Associated Therapies
Contraindications & Blackbox Warnings
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Pharmacodynamics

Antihemophilic Factor binds factor IXa along with calcium and phospholipid, which converts factor X to factor Xa to facilitate the clotting cascade.

Mechanism of action

Antihemophilic factor (AHF) is a protein found in normal plasma which is necessary for clot formation. The administration of AHF provides an increase in plasma levels of AHF and can temporarily correct the coagulation defect of patients with hemophilia A (classical hemophilia). As factor VIII is the specific clotting factor deficient in patients with hemophilia A, replacement of clotting factor with Moroctocog alfa, also known as BDDrFVIII (B domain deleted recombinant factor VIII), is the cornerstone of the prevention and treatment of bleeding for this disorder.

TargetActionsOrganism
ACoagulation factor X
activator
Humans
ACoagulation factor IX
cofactor
Humans
Avon Willebrand factor
binder
Humans
UPhytanoyl-CoA dioxygenase, peroxisomal
antagonist
Humans
UAsialoglycoprotein receptor 2
binder
Humans
U78 kDa glucose-regulated protein
chaperone
Humans
UCalreticulin
chaperone
Humans
UCalnexin
chaperone
Humans
UProtein ERGIC-53
chaperone
Humans
UProlow-density lipoprotein receptor-related protein 1
modulator
Humans
UMultiple coagulation factor deficiency protein 2
modulator
Humans
Absorption

Cmax = 1.08±0.22 IU⋅hr/mL 5 Cmax = 1.12 (±0.19) IU/mL Label

Volume of distribution

Mean steady-state volume of distribution = 65.1 (± 35.1) mL/kg Label

Protein binding

Not Available

Metabolism
Not Available
Route of elimination

Not Available

Half-life

Mean terminal elimination half-life = 11.8 (± 5.1) hours Label Half-life = 11.2 ± 5.0 hours 5

Clearance

Mean clearance = 4.21 (± 2.08) mL/h•kg Label Clearance = 4.51 ± 2.23 mL/h•kg 5

Adverse Effects
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Toxicity

Not Available

Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
DrugInteraction
Integrate drug-drug
interactions in your software
AbciximabThe therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Abciximab.
AcenocoumarolThe therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Acenocoumarol.
Alpha-1-proteinase inhibitorAlpha-1-proteinase inhibitor may increase the thrombogenic activities of Moroctocog alfa.
AlteplaseThe therapeutic efficacy of Moroctocog alfa can be decreased when used in combination with Alteplase.
Aminocaproic acidThe risk or severity of adverse effects can be increased when Aminocaproic acid is combined with Moroctocog alfa.
Food Interactions
No interactions found.

Products

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Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
RefactoPowder, for solution1000 unit / vialIntravenousWyeth Ltd.2003-02-112009-01-23Canada flag
Refacto AFInjection, powder, for solution250 IUIntravenousPfizer Europe Ma Eeig2016-09-08Not applicableEU flag
Refacto AFInjection, powder, for solution500 IUIntravenousPfizer Europe Ma Eeig2016-09-08Not applicableEU flag
Refacto AFInjection, powder, for solution2000 IUIntravenousPfizer Europe Ma Eeig2016-09-08Not applicableEU flag
Refacto AFInjection, powder, for solution2000 IUIntravenousPfizer Europe Ma Eeig2016-09-08Not applicableEU flag
Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
XynthaMoroctocog alfa (2000 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2008-08-01Not applicableUS flag
XynthaMoroctocog alfa (500 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2011-12-01Not applicableUS flag
XynthaMoroctocog alfa (250 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2008-08-01Not applicableUS flag
XynthaMoroctocog alfa (1000 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2008-08-01Not applicableUS flag
XynthaMoroctocog alfa (250 [iU]/4mL) + Isopropyl alcohol (70 mL/100mL)Injection, powder, lyophilized, for solution; KitIntravenous; TopicalWyeth BioPharma Division of Wyeth Pharmaceuticals LLC2011-12-01Not applicableUS flag

Categories

Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
Not Available
Kingdom
Organic Compounds
Super Class
Organic Acids
Class
Carboxylic Acids and Derivatives
Sub Class
Amino Acids, Peptides, and Analogues
Direct Parent
Peptides
Alternative Parents
Not Available
Substituents
Not Available
Molecular Framework
Not Available
External Descriptors
Not Available
Affected organisms
Not Available

Chemical Identifiers

UNII
113E3Z3CJJ
CAS number
284036-24-4

References

General References
  1. Titheradge MA, Coore HG: Initial rates of pyruvate transport in mitochondria determined by an "inhibitor-stop" technique. Biochem J. 1975 Sep;150(3):553-6. [Article]
  2. Santagostino E: A new recombinant factor VIII: from genetics to clinical use. Drug Des Devel Ther. 2014 Dec 12;8:2507-15. doi: 10.2147/DDDT.S73241. eCollection 2014. [Article]
  3. Frampton JE: Efmoroctocog Alfa: A Review in Haemophilia A. Drugs. 2016 Sep;76(13):1281-1291. doi: 10.1007/s40265-016-0622-z. [Article]
  4. Franchini M, Mannucci PM: Hemophilia A in the third millennium. Blood Rev. 2013 Jul;27(4):179-84. doi: 10.1016/j.blre.2013.06.002. Epub 2013 Jun 28. [Article]
  5. Recht M, Nemes L, Matysiak M, Manco-Johnson M, Lusher J, Smith M, Mannucci P, Hay C, Abshire T, O'Brien A, Hayward B, Udata C, Roth DA, Arkin S: Clinical evaluation of moroctocog alfa (AF-CC), a new generation of B-domain deleted recombinant factor VIII (BDDrFVIII) for treatment of haemophilia A: demonstration of safety, efficacy, and pharmacokinetic equivalence to full-length recombinant factor VIII. Haemophilia. 2009 Jul;15(4):869-80. doi: 10.1111/j.1365-2516.2009.02027.x. Epub 2009 Apr 9. [Article]
  6. Have we forgotten the lessons of the tainted blood scandal? - The Globe and Mail [Link]
  7. DailyMed Label: XYNTHA SOLOFUSE (antihemophilic factor [recombinant]) for intravenous injection [Link]
  8. Summary of Product Characteristics: ReFacto AF (moroctocog alfa) Intravenous Injection [Link]
  9. Health Canada Product Monograph: Xyntha [Antihemophilic Factor (Recombinant)] For Intravenous Injection [Link]
KEGG Drug
D08232
ChEMBL
CHEMBL2109137
RxList
RxList Drug Page
Drugs.com
Drugs.com Drug Page
Wikipedia
Moroctocog_alfa
FDA label
Download (985 KB)

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
4CompletedTreatmentHemophilia A3
4TerminatedTreatmentHemophilia A2
3CompletedTreatmentHemophilia A5
3TerminatedTreatmentHemophilia A1
1CompletedNot AvailableHemophilia A1

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage Forms
FormRouteStrength
Powder, for solutionIntravenous1000 unit / vial
Injection, powder, for solutionIntravenous3000 IU
Injection, solutionIntravenous1000 iu
Injection, solutionIntravenous2000 iu
Injection, solutionIntravenous250 iu
Injection, solutionIntravenous500 iu
Injection, powder, lyophilized, for solution; kitIntravenous; Topical
Kit; powder, for solutionIntravenous1000 unit / vial
Kit; powder, for solutionIntravenous2000 unit / vial
Kit; powder, for solutionIntravenous250 unit / vial
Kit; powder, for solutionIntravenous500 unit / vial
Injection, powder, lyophilized, for solutionIntravenous1000 IU
Injection, powder, lyophilized, for solutionIntravenous500 IU
Injection, powder, for solutionIntravenous
Injection, powder, for solutionIntravenous1000 IU
Injection, powder, for solutionIntravenous2000 IU
Injection, powder, for solutionIntravenous250 IU
Injection, powder, for solutionIntravenous500 IU
Powder, for solutionIntravenous1000 unit / syr
Powder, for solutionIntravenous2000 unit / syr
Powder, for solutionIntravenous250 unit / syr
Powder, for solutionIntravenous3000 unit / syr
Powder, for solutionIntravenous500 unit / syr
Injection, powder, lyophilized, for solutionIntravenous2000 IU
Injection, powder, lyophilized, for solutionIntravenous250 IU
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
Not Available

Targets

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Details1. Coagulation factor X
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Activator
General Function
Serine-type endopeptidase activity
Specific Function
Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Gene Name
F10
Uniprot ID
P00742
Uniprot Name
Coagulation factor X
Molecular Weight
54731.255 Da
References
  1. BLATRIX C, SOULIER JP: [Preparation of a fraction rich in prothrombin, proconvertin, Stuart factor and antihemophilic factor B (P.P.B. fraction)]. Pathol Biol (Paris). 1959 Dec;7:2477-86. [Article]
  2. LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF STUART FACTOR (FACTOR X) BY ACTIVATED ANTIHEMOPHILIC FACTOR (ACTIVATED FACTOR 8). Biochemistry. 1965 Jan;4:113-20. [Article]
  3. Radnoff OD, Saito H: Inhibition of Hageman factor, plasma thromboplastin antecedent, thrombin and other clotting factors by phenylglyoxal hydrate (38500). Proc Soc Exp Biol Med. 1975 Jan;148(1):177-82. [Article]
  4. Orthner CL: Characterization of proteases in AHF concentrates: effect on factor VIII:von Willebrand protein as assessed by high-pressure gel permeation chromatography. J Lab Clin Med. 1984 Nov;104(5):816-28. [Article]
  5. Freedman J, Mody M, Lazarus AH, Dewar L, Song S, Blanchette VS, Garvey MB, Ofosu FA: Platelet activation and hypercoagulability following treatment with porcine factor VIII (HYATE:C). Am J Hematol. 2002 Mar;69(3):192-9. [Article]
Details2. Coagulation factor IX
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Cofactor
General Function
Serine-type endopeptidase activity
Specific Function
Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholi...
Gene Name
F9
Uniprot ID
P00740
Uniprot Name
Coagulation factor IX
Molecular Weight
51778.11 Da
References
  1. Hule V: [Factor IX inhibitor (antihemophilic factor B, PTC) in a woman]. Vnitr Lek. 1975 Mar;21(3):274-7. [Article]
  2. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry. 1985 Jul 2;24(14):3736-50. [Article]
  3. LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF ANTIHEMOPHILIC FACTOR (FACTOR 8) BY ACTIVATED CHRISTMAS FACTOR (ACTIVATED FACTOR9 9). Biochemistry. 1964 Nov;3:1720-5. [Article]
  4. Hoofnagle JH, Gerety RJ, Thiel J, Barker LF: The prevalence of hepatitis B surface antigen in commercially prepared plasma products. J Lab Clin Med. 1976 Jul;88(1):102-13. [Article]
  5. Prince AM, Horowitz B, Brotman B, Huima T, Richardson L, van den Ende MC: Inactivation of hepatitis B and Hutchinson strain non-A, non-B hepatitis viruses by exposure to Tween 80 and ether. Vox Sang. 1984;46(1):36-43. [Article]
Details3. von Willebrand factor
Kind
Protein
Organism
Humans
Pharmacological action
Yes
Actions
Binder
General Function
Protein n-terminus binding
Specific Function
Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surf...
Gene Name
VWF
Uniprot ID
P04275
Uniprot Name
von Willebrand factor
Molecular Weight
309261.83 Da
References
  1. Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [Article]
  2. Lillicrap D, Poon MC, Walker I, Xie F, Schwartz BA: Efficacy and safety of the factor VIII/von Willebrand factor concentrate, haemate-P/humate-P: ristocetin cofactor unit dosing in patients with von Willebrand disease. Thromb Haemost. 2002 Feb;87(2):224-30. [Article]
  3. Gill JC, Ewenstein BM, Thompson AR, Mueller-Velten G, Schwartz BA: Successful treatment of urgent bleeding in von Willebrand disease with factor VIII/VWF concentrate (Humate-P): use of the ristocetin cofactor assay (VWF:RCo) to measure potency and to guide therapy. Haemophilia. 2003 Nov;9(6):688-95. [Article]
  4. Smith KJ, Lusher JM, Cohen AR, Salzman P: Initial clinical experience with a new pasteurized monoclonal antibody purified factor VIIIC. Semin Hematol. 1990 Apr;27(2 Suppl 2):25-9. [Article]
  5. Altieri DC, Capitanio AM, Mannucci PM: von Willebrand factor contaminating porcine factor VIII concentrate (Hyate:C) causes platelet aggregation. Br J Haematol. 1986 Aug;63(4):703-11. [Article]
Details4. Phytanoyl-CoA dioxygenase, peroxisomal
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Antagonist
General Function
Phytanoyl-coa dioxygenase activity
Specific Function
Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Gene Name
PHYH
Uniprot ID
O14832
Uniprot Name
Phytanoyl-CoA dioxygenase, peroxisomal
Molecular Weight
38538.065 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Chen C, Wang Q, Fang X, Xu Q, Chi C, Gu J: Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII. J Biol Chem. 2001 Dec 7;276(49):46340-6. [Article]
Details5. Asialoglycoprotein receptor 2
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Binder
General Function
Carbohydrate binding
Specific Function
Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-...
Gene Name
ASGR2
Uniprot ID
P07307
Uniprot Name
Asialoglycoprotein receptor 2
Molecular Weight
35092.04 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Bovenschen N, Rijken DC, Havekes LM, van Vlijmen BJ, Mertens K: The B domain of coagulation factor VIII interacts with the asialoglycoprotein receptor. J Thromb Haemost. 2005 Jun;3(6):1257-65. [Article]
Details6. 78 kDa glucose-regulated protein
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Chaperone
General Function
Unfolded protein binding
Specific Function
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded protein...
Gene Name
HSPA5
Uniprot ID
P11021
Uniprot Name
78 kDa glucose-regulated protein
Molecular Weight
72332.425 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
Details7. Calreticulin
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Chaperone
General Function
Zinc ion binding
Specific Function
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently wit...
Gene Name
CALR
Uniprot ID
P27797
Uniprot Name
Calreticulin
Molecular Weight
48141.2 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [Article]
  4. Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2008 Feb;87(2):107-12. Epub 2007 Sep 26. [Article]
  5. Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
Details8. Calnexin
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Chaperone
General Function
Poly(a) rna binding
Specific Function
Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembl...
Gene Name
CANX
Uniprot ID
P27824
Uniprot Name
Calnexin
Molecular Weight
67567.695 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [Article]
  4. Becker S, Simpson JC, Pepperkok R, Heinz S, Herder C, Grez M, Seifried E, Tonn T: Confocal microscopy analysis of native, full length and B-domain deleted coagulation factor VIII trafficking in mammalian cells. Thromb Haemost. 2004 Jul;92(1):23-35. [Article]
  5. Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2008 Feb;87(2):107-12. Epub 2007 Sep 26. [Article]
  6. Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [Article]
Details9. Protein ERGIC-53
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Chaperone
General Function
Unfolded protein binding
Specific Function
Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or...
Gene Name
LMAN1
Uniprot ID
P49257
Uniprot Name
Protein ERGIC-53
Molecular Weight
57548.665 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Cunningham MA, Pipe SW, Zhang B, Hauri HP, Ginsburg D, Kaufman RJ: LMAN1 is a molecular chaperone for the secretion of coagulation factor VIII. J Thromb Haemost. 2003 Nov;1(11):2360-7. [Article]
  4. Miao HZ, Sirachainan N, Palmer L, Kucab P, Cunningham MA, Kaufman RJ, Pipe SW: Bioengineering of coagulation factor VIII for improved secretion. Blood. 2004 May 1;103(9):3412-9. Epub 2004 Jan 15. [Article]
Details10. Prolow-density lipoprotein receptor-related protein 1
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Modulator
General Function
Receptor activity
Specific Function
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance...
Gene Name
LRP1
Uniprot ID
Q07954
Uniprot Name
Prolow-density lipoprotein receptor-related protein 1
Molecular Weight
504601.695 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Franchini M, Montagnana M: Low-density lipoprotein receptor-related protein 1: new functions for an old molecule. Clin Chem Lab Med. 2011 Jun;49(6):967-70. doi: 10.1515/CCLM.2011.154. Epub 2011 Mar 11. [Article]
Details11. Multiple coagulation factor deficiency protein 2
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Modulator
General Function
Calcium ion binding
Specific Function
The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.
Gene Name
MCFD2
Uniprot ID
Q8NI22
Uniprot Name
Multiple coagulation factor deficiency protein 2
Molecular Weight
16390.175 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Zhang B, Kaufman RJ, Ginsburg D: LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J Biol Chem. 2005 Jul 8;280(27):25881-6. Epub 2005 May 10. [Article]

Enzymes

Details1. Prothrombin
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Activator
General Function
Thrombospondin receptor activity
Specific Function
Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostas...
Gene Name
F2
Uniprot ID
P00734
Uniprot Name
Prothrombin
Molecular Weight
70036.295 Da
References
  1. Alberio L, Safa O, Clemetson KJ, Esmon CT, Dale GL: Surface expression and functional characterization of alpha-granule factor V in human platelets: effects of ionophore A23187, thrombin, collagen, and convulxin. Blood. 2000 Mar 1;95(5):1694-702. [Article]
  2. Ratnoff OD, Lewis JH: Heckathorn's disease: variable functional dificiency of antihemophilic factor (factor VIII). Blood. 1975 Aug;46(2):161-73. [Article]
  3. Anderson DM, Shelley S, Crick N, Buraglio M: No effect of the novel antidiabetic agent nateglinide on the pharmacokinetics and anticoagulant properties of warfarin in healthy volunteers. J Clin Pharmacol. 2002 Dec;42(12):1358-65. [Article]
  4. Piet MP, Chin S, Prince AM, Brotman B, Cundell AM, Horowitz B: The use of tri(n-butyl)phosphate detergent mixtures to inactivate hepatitis viruses and human immunodeficiency virus in plasma and plasma's subsequent fractionation. Transfusion. 1990 Sep;30(7):591-8. [Article]
  5. Lazarchick J, Ashby MA, Lazarchick JJ, Sens DA: Mechanism of factor VIII inactivation by human antibodies. IV. Antibody binding prevents factor VIII proteolysis by thrombin. Ann Clin Lab Sci. 1986 Nov-Dec;16(6):497-501. [Article]
Details2. Vitamin K-dependent protein C
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Inactivator
General Function
Serine-type endopeptidase activity
Specific Function
Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts ...
Gene Name
PROC
Uniprot ID
P04070
Uniprot Name
Vitamin K-dependent protein C
Molecular Weight
52070.82 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
  2. 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. [Article]
  3. Bereczky Z, Kovacs KB, Muszbek L: Protein C and protein S deficiencies: similarities and differences between two brothers playing in the same game. Clin Chem Lab Med. 2010 Dec;48 Suppl 1:S53-66. doi: 10.1515/CCLM.2010.369. Epub 2010 Nov 5. [Article]

Drug created at March 20, 2018 17:53 / Updated at April 17, 2024 06:33