TY  - GEN
T1  - Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in Drosophila melanogaster
AU  - Meyer, Heiko
AU  - Buhr, Annika
AU  - Callaerts, Patrick
AU  - Schiemann, Ronja
AU  - Wolfner, Mariana F.
AU  - Marygold, Steven J.
DO  - 10.17912/micropub.biology.000410
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000410/
AB  - Neprilysins belong to the family of M13 metalloendopeptidases and constitute highly conserved ectoenzymes that cleave and thereby inactivate numerous physiologically relevant peptides in the extracellular space. While the vast majority of these enzymes appear to be membrane-bound, some family members have been identified as soluble secreted proteins (Turner et al., 2001). In humans, seven members of the M13 family are known, namely Neprilysin (NEP), endothelin-converting enzymes (ECE1, ECE2), ECEL1, MMEL1, the KELL blood-group protein and PHEX (Turner and Tanzawa 1997). Among these, NEP is characterized best, with identified substrates including endothelins, angiotensins I and II, enkephalins, bradykinin, atrial natriuretic peptide, substance P and the amyloid-beta peptide (Turner et al., 2001, Nalivaeva et al., 2020). NEP-mediated hydrolysis is critical to maintain the physiological homeostasis of these peptides, and thus represents a prerequisite for proper endocrine signal transmission. Accordingly, impaired neprilysin activity in humans is involved in the pathogenesis of numerous diseases, including hypertension (Molinaro et al., 2002), analgesia (Whitworth 2003), cancer (Turner et al., 2001) and Alzheimer’s disease (Iwata et al., 2000, Belyaev et al., 2009). Clinical trials have confirmed the therapeutic potential of modulating neprilysin activity (Jessup 2014).
PY  - 2021
JO  - microPublication Biology
ER  -