Neurolysin (NLN, EC 3.4.24.16) is a member of the thermolysin-like mammalian zinc endopeptidase family (Dauch et al. 1995). It is maximally active at neutral pH and responsible for hydrolytic processing of bioactive peptides in the extracellular environment (Shrimpton et al. 2002). It cleaves 3 residues from the C-teminal end of Neurotensin (Dauch et al. 1995). Other endogenous substrates of NLN include bradykinin, angiotensins I and II, substance P, hemopressin, dynorphin A(1–8), metorphamide, and somatostatin (Wangler et al. 2016). The functional significance of NLN is poorly understood (Checler 2014). In vivo studies have linked it to neurotensin-dependent nociception (Vincent et al. 1997), bradykinin-mediated hypotension, microvascular permeability and hyperalgesia (Gomez et al. 2011), and pathogenesis of stroke (Rashid et al. 2014).
Bickel, U, Jayaraman, S, Abbruscato, TJ, Mechref, Y, Karamyan, VT, Zhu, R, Wangler, NJ
Kitabgi, P, Vincent, JP, Checler, F
metalloendopeptidase activity of NLN [extracellular region]
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