Elastases

from Wikipedia, the free encyclopedia

Elastases are enzymes in mammals that can break peptide bonds, called proteases . Within the serine proteases , they form a subfamily that is closely related to chymotrypsin . Several, but not all, elastases are able to digest elastin , an endogenous structural protein , from which the name of the group arose. In humans, nine enzymes are currently known that are counted among the elastases.

Elastases are proteins with 250-270 amino acid residues .

In humans, elastases are an important part of the immune response to pathological gram-negative germs in the lungs, in the gastrointestinal tract, but also on wounds. They split peptide bonds on the carboxy side of small hydrophobic amino acids, such as. B. glycine, alanine and valine. Their effect is so unspecific that it also endangers the body's own tissue and plays a pathological role in pneumonia and arthritis. There are several elastase inhibiting proteins in the body, including α1-antitrypsin , SLPI, elafin and alpha-2-macroglobulin. So far only a few inhibitors of the protein for use in severe lung diseases have been synthetically produced. Many plant constituents, in particular from the sunflower family (Asteraceae), show an inhibitory effect on elastase, including flavonoids and their metabolites , caffeic acid derivatives , triterpene derivatives and sesquiterpene lactones . Up to 500 mg of elastase are converted in the body every day.

Human elastases

Surname Gene name UniProt EC number pathology
Skin elastase, (incorrectly: elastase-1) CELA1 Q9UNI1 EC  3.4.21.36
Neutrophil elastase , (elastase-2) ELANE P08246 EC  3.4.21.37 congenital neutropenia (SCN1)
Pancreatic elastase , elastase-1 CELA2A P08217 EC  3.4.21.71
Elastase-2B CELA2B P08218 EC  3.4.21.71
Elastase-3A CELA3A P09093 EC  3.4.21.70
Elastase-3B CELA3B P08861 EC  3.4.21.70
Myeloblastin PRTN3 P24158 EC  3.4.21.76 Antigen in Wegener's granulomatosis
Chymotrypsin C. CTRC Q99895 EC  3.4.21.2 chronic pancreatitis
Azurocidin AZU1 P20160 -

literature

  • Bettina Siedle: Phytochemical and pharmacological-biological studies of traditional medicinal plants from Costa Rica and of sesquiterpene lactones ... (Diss. Freiburg, 2003) urn : nbn: de: bsz: 25-opus-10335