Endopeptidase inhibitor
Endopeptidase Inhibitor
Endopeptidase inhibitors (pronunciation: en-doh-pep-ti-dase in-hi-bi-tors) are a class of enzyme inhibitors that reduce the activity of endopeptidase enzymes.
Etymology
The term "endopeptidase inhibitor" is derived from the Greek words "endon" meaning within, "peptos" meaning digested, and the Latin word "inhibitor" meaning hinderer.
Function
Endopeptidase inhibitors play a crucial role in the regulation of peptide degradation in the body. They bind to the active site of endopeptidases, preventing them from breaking down peptides. This can have a significant impact on various physiological processes, including blood pressure regulation, inflammation, and pain perception.
Types
There are several types of endopeptidase inhibitors, including:
- Aprotinin: A potent inhibitor of serine endopeptidases.
- Leupeptin: A naturally occurring inhibitor of serine and cysteine endopeptidases.
- E-64: A specific inhibitor of cysteine endopeptidases.
Clinical Significance
Endopeptidase inhibitors have been used in the treatment of various medical conditions. For example, aprotinin has been used to reduce bleeding during surgery, while E-64 has been investigated for its potential use in the treatment of neurodegenerative diseases.
See Also
External links
- Medical encyclopedia article on Endopeptidase inhibitor
- Wikipedia's article - Endopeptidase inhibitor
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