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Title: Elastase  
Author: World Heritage Encyclopedia
Language: English
Subject: Protease, Digestive enzyme, Neutrophil elastase, Alpha 1-antitrypsin deficiency, Proteolysis
Publisher: World Heritage Encyclopedia


Space-filling model of elastase.
Crystals of porcine elastase.

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins.[1]


  • Forms and classification 1
  • Function 2
  • The role of human elastase in disease 3
    • A1AT 3.1
    • Cyclic hematopoeiesis 3.2
    • Other diseases 3.3
  • The role of bacterial elastase in disease 4
  • References 5
  • External links 6

Forms and classification

Eight human genes exist for elastase:

Family Gene symbol Protein name EC number
Approved Previous Approved Previous
CELA1 ELA1 chymotrypsin-like elastase family, member 1 elastase 1, pancreatic EC
CELA2A ELA2A chymotrypsin-like elastase family, member 2A elastase 2A, pancreatic EC
CELA2B ELA2B chymotrypsin-like elastase family, member 2B elastase 2B, pancreatic EC
CELA3A ELA3A chymotrypsin-like elastase family, member 3A elastase 3A, pancreatic EC
CELA3B ELA3B chymotrypsin-like elastase family, member 3B elastase 3B, pancreatic EC
chymotrypsin CTRC ELA4 chymotrypsin C (caldecrin) elastase 4 EC
neutrophil ELANE ELA2 neutrophil elastase elastase 2 EC
macrophage MMP12 HME macrophage metalloelastase macrophage elastase EC

Some bacteria (including Pseudomonas aeruginosa) also produce elastase. In bacteria, elastase is considered a virulence factor.


Elastase breaks down elastin, an elastic fibre that, together with collagen, determines the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. Elastase also has the important immunological role of breaking down Shigella virulence factors. This is accomplished through the cleavage of peptide bonds in the target proteins. The specific peptide bonds cleaved are those on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine. For more on how this is accomplished, see serine protease.

The role of human elastase in disease


Elastase is inhibited by the acute-phase protein α1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin. A1AT is normally secreted by the liver cells into the serum. α1-antitryspin deficiency (A1AD) leads to uninhibited destruction of elastic fibre by elastase; the main result is pulmonary emphysema.

Cyclic hematopoeiesis

The rare disease cyclic hematopoeiesis (also called "cyclic neutropenia") is an autosomal dominant genetic disorder characterised by fluctuating neutrophil granulocyte counts over 21-day periods. During neutropenia, patients are at risk for infections. In 1999, this disease was linked to disorders in the ELA-2 / ELANE gene.[2] Other forms of congenital neutropenia also appear to be linked to ELA-2 mutations.

Other diseases

Neutrophil elastase is responsible for the blistering in bullous pemphigoid, a skin condition, in the presence of antibodies.

The role of bacterial elastase in disease

Elastase has been shown to disrupt tight junctions, cause proteolytic damage to tissue, break down cytokines and alpha proteinase inhibitor, cleave immunoglobulin A and G (IgA, IgG), and cleave both C3bi, a component of the complement system, and CR1, a receptor on neutrophils for another complement molecule involved in phagocytosis. The cleavage of IgA, IgG, C3bi, and CR1 contributes to a decrease of the ability of neutrophils to kill bacteria by phagocytosis. Together, all these factors contribute to human pathology.


  1. ^ Bieth JG (2001). "[The elastases]". J. Soc. Biol. (in French) 195 (2): 173–9.  
  2. ^ Horwitz M, Benson KF, Person RE, Aprikyan AG, Dale DC (1999). "Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis". Nat. Genet. 23 (4): 433–6.  

External links

  • GeneReviews/NCBI/NIH/UW entry on ELANE-Related Neutropenias including cyclic neutropenia
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