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NLN encodes a member of the metallopeptidase M3 protein family that cleaves neurotensin at the Pro10-Tyr11 bond, leading to the formation of neurotensin(1-10) and neurotensin(11-13).
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Mutations at only two residues (Arg-470 and Arg-498) are required to swap specificity with thimet oligopeptidase (show THOP1 Proteins), a result that is confirmed by testing the two-mutant constructs.
These results confirm the identity of neurolysin as a novel Ang II binding site, suggesting that neurolysin may play a significant role in opposing the pathophysiological actions of the brain RAS and influencing brain morphology.
These results suggest the exciting new possibility that Nln is a key enzyme for energy metabolism and could be a novel therapeutic target to improve glucose uptake and insulin (show INS Proteins) sensitivity.
Neurolysin plays a role in modulating the brain's response to stroke and recovery after stroke.
Melanoma cells secrete neurolysin which may have an important role in tumor proliferation/angiogenesis in vitro and in vivo.
Cyclic strain putatively regulates both the mRNA expression and enzymatic function of EP24.15 (show THOP1 Proteins) and EP24.16.
Ciliary epithelium expresses neurolysin.
This gene encodes a member of the metallopeptidase M3 protein family that cleaves neurotensin at the Pro10-Tyr11 bond, leading to the formation of neurotensin(1-10) and neurotensin(11-13). The encoded protein is likely involved in the termination of the neurotensinergic signal in the central nervous system and in the gastrointestinal tract.
angiotensin binding protein
, angiotensin-binding protein
, endopeptidase 24.16
, microsomal endopeptidase
, mitochondrial oligopeptidase M
, neurolysin, mitochondrial
, neurotensin endopeptidase
, endopeptidase EC220.127.116.11
, soluble angiotensin-binding protein
, soluble angiotesin-binding protein