elastasa

Elastases are serine proteases that cleave peptide bonds in elastin and other proteins of the extracellular matrix. They are important in normal tissue remodeling and in defense against pathogens, but their activity must be tightly regulated to prevent damage to host tissues. In humans, the best known elastases are neutrophil elastase, produced by neutrophils, and pancreatic elastases, secreted by the pancreas as digestive enzymes.

Neutrophil elastase is stored in azurophilic granules of neutrophils and released during inflammatory responses. It degrades elastin and several other matrix proteins, contributing to tissue remodeling and antimicrobial defense. Pancreatic elastases are secreted into the small intestine as part of the digestive enzyme mix and primarily participate in the breakdown of dietary proteins, including elastin-containing proteins, during digestion. Other elastase-like enzymes exist in various tissues and cell types, contributing to remodeling in development and disease.

Regulation of elastase activity is essential. A key inhibitor is alpha-1 antitrypsin, which helps limit elastase activity in the lungs and other tissues. Deficiency of this inhibitor can lead to excessive elastase activity, resulting in tissue destruction and diseases such as emphysema and COPD. Conversely, excessive elastase activity has been implicated in inflammatory lung diseases, cystic fibrosis, and chronic wounds. Therapeutic approaches include inhibitors of elastase activity and strategies to restore inhibitor balance.

In summary, elastases are proteases with important physiological roles in defense and remodeling but can contribute to tissue damage when not properly regulated. They are studied in fields ranging from digestion to immunology and respiratory medicine.