Recombinant alpha 1-antitrypsin

Identification

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Name
Recombinant alpha 1-antitrypsin
Accession Number
DB05481
Type
Biotech
Groups
Investigational
Biologic Classification
Protein Based Therapies
Other protein based therapies
Description

Alpha 1-antitrypsin is a glycoprotein primarily produced by hepatocytes, and to a lesser extent, immune system cells. Recombinant alpha 1-antitrypsin (rAAT) is produced from yeast, which unlike commercially available forms of plasma-derived AAT, eliminates the risk associated with blood-borne infectious agents and allows for a increased manufacturing. rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase. The proteinase/antiproteinase balance is believed to be important for maintaining healthy skin. The rAAT topical gel (Dermolastin™) is indicated for patients with atopic dermatitis and psoriasis. The company has indicated that other formulations for gastroenterological and urological indications will also be developed.

Protein chemical formula
Not Available
Protein average weight
Not Available
Sequences
Not Available
Synonyms
  • Recombinant alpha 1-antitrypsin
International/Other Brands
Dermolastin
Categories
Not Available
UNII
Not Available
CAS number
Not Available

Pharmacology

Indication

Investigated for use/treatment in alpha 1 antitrypsin deficiency, atopic dermatitis, and chronic obstructive pulmonary disease (COPD).

Pharmacodynamics

Alpha 1-antitrypsin is a glycoprotein primarily produced by hepatocytes, and to a lesser extent, immune system cells. Recombinant alpha 1-antitrypsin (rAAT) is produced from yeast, which unlike commercially available forms of plasma-derived AAT, eliminates the risk associated with blood-borne infectious agents and allows for a increased manufacturing. rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase. The proteinase/antiproteinase balance is believed to be important for maintaining healthy skin.

Mechanism of action

rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase.

TargetActionsOrganism
UAlpha-1-antitrypsinNot AvailableHumans
Absorption
Not Available
Volume of distribution
Not Available
Protein binding
Not Available
Metabolism
Not Available
Route of elimination
Not Available
Half life
Not Available
Clearance
Not Available
Toxicity

Well tolerated in clinical trials.

Affected organisms
Not Available
Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
Not Available
Food Interactions
Not Available

References

General References
  1. Brown WM: rAAt (dermatological) Arriva/ProMetic. Curr Opin Mol Ther. 2006 Feb;8(1):69-75. [PubMed:16506528]
  2. Brown WM: rAAt (inhaled) Arriva/Hyland Immuno. Curr Opin Mol Ther. 2006 Feb;8(1):76-82. [PubMed:16506529]
External Links
PubChem Substance
347910164

Clinical Trials

Clinical Trials
Not Available

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage forms
Not Available
Prices
Not Available
Patents
Not Available

Properties

State
Solid
Experimental Properties
Not Available

Taxonomy

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

Targets

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Serine-type endopeptidase inhibitor activity
Specific Function
Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. T...
Gene Name
SERPINA1
Uniprot ID
P01009
Uniprot Name
Alpha-1-antitrypsin
Molecular Weight
46736.195 Da

Drug created on November 18, 2007 11:25 / Updated on June 04, 2019 06:17