Elastase

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Space-filling model of elastase
Crystals of porcine elastase

In

substrate specificity (i.e. what proteins it can digest), not to any kind of evolutionary grouping.[2]

Forms and classification

Eight human genes exist for elastase:

Family Gene symbol Protein name EC number
Approved Previous Approved Previous
chymotrypsin-
like 		CELA1 ELA1 chymotrypsin-like elastase family, member 1 elastase 1, pancreatic EC 3.4.21.36
CELA2A ELA2A chymotrypsin-like elastase family, member 2A elastase 2A, pancreatic EC 3.4.21.71
CELA2B ELA2B chymotrypsin-like elastase family, member 2B elastase 2B, pancreatic EC 3.4.21.71
CELA3A ELA3A chymotrypsin-like elastase family, member 3A elastase 3A, pancreatic EC 3.4.21.70
CELA3B ELA3B chymotrypsin-like elastase family, member 3B elastase 3B, pancreatic EC 3.4.21.70
chymotrypsin CTRC ELA4 chymotrypsin C (caldecrin) elastase 4 EC 3.4.21.2
neutrophil ELANE ELA2 neutrophil elastase elastase 2 EC 3.4.21.37
macrophage MMP12 HME macrophage metalloelastase macrophage elastase EC 3.4.24.65

The four "pancreatic elastases",

matrix metallopeptidase
.

Chymotrypsin is weaker at digesting elastin than the architypical pancreatic elastase.[4]

Some

metalloenzymes.[2]

Function

The fact that elastase can break down elastin in test tubes (while other proteases cannot) does not imply that there is a unifying function for all elastases in the living body. Instead, they each have their own role:

Elastases of the serine protease type preferentially break down peptide bonds on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine.

Role of human elastase in disease

A1AT

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. Alpha-1 antitrypsin deficiency (A1AD) leads to uninhibited destruction of elastic fibre by elastase; the main result is emphysema.

Cyclic neutropenia

The

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.[10] Other forms of congenital neutropenia also appear to be linked to ELA-2 mutations.[citation needed
]

Other diseases

Neutrophil elastase is responsible for the blistering in bullous pemphigoid, a skin condition, in the presence of antibodies. It may also play a role in the formation of abdominal aortic aneurysms (AAAs) and chronic obstructive pulmonary disease (COPD).

Role of bacterial elastase in disease

Elastase has been shown to disrupt

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
.

References

  1. PMID 11723830
    .
  2. ^
    PMID 36913358
    .
  3. OCLC 887605755.{{cite book}}: CS1 maint: location missing publisher (link
    )
  4. PMID 3161694
    .
  5. PMID 819031
    .
  6. PMID 10620133
    .
  7. PMID 10947984
    .
  8. PMID 12018205
    .
  9. PMID 37648735
    .
  10. S2CID 6951666
    .
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