Oxytocinase is a type of enzyme that metabolizes the endogenous neuropeptide, oxytocin.[1] The most well-characterized oxytocinase is leucyl/cystinyl aminopeptidase,[1][2] which is also an enkephalinase. Other oxytocinases are also known.[1][3] During pregnancy, oxytocinase plays a role in balancing concentration of oxytocin by degrading the oxytocin produced by the fetus, as production of oxytocin increases with growth of fetus.[2] One study found that concentration level of oxytocinase increased progressively with gestational age until labor, which indicates that pregnancy development can be statistically evaluated by comparing oxytocinase levels.[4]
Inhibitors edit
Amastatin, bestatin (ubenimex), and puromycin have been found to inhibit the enzymatic degradation of oxytocin, though they also inhibit the degradation of various other peptides, such as vasopressin, met-enkephalin, and dynorphin A.[5][3][6] EDTA, L-methionine, o-phenanthroline, and phosphoramidon have also been found to inhibit the enzymatic degradation of oxytocin.[7]
See also edit
References edit
- ^ a b c Tsujimoto M, Hattori A (2005). "The oxytocinase subfamily of M1 aminopeptidases". Biochim. Biophys. Acta. 1751 (1): 9–18. doi:10.1016/j.bbapap.2004.09.011. PMID 16054015.
- ^ a b Nomura S, Ito T, Yamamoto E, Sumigama S, Iwase A, Okada M, Shibata K, Ando H, Ino K, Kikkawa F, Mizutani S (2005). "Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy". Biochim. Biophys. Acta. 1751 (1): 19–25. doi:10.1016/j.bbapap.2005.04.006. PMID 15894523.
- ^ a b Mizutani S, Yokosawa H, Tomoda Y (1992). "Degradation of oxytocin by the human placenta: effect of selective inhibitors". Acta Endocrinol. 127 (1): 76–80. doi:10.1530/acta.0.1270076. PMID 1355623.
- ^ Klimek, Marek (August 2005). "Comparative analysis of ACTH and oxytocinase plasma concentration during pregnancy". Neuro Endocrinology Letters. 26 (4): 337–341. ISSN 0172-780X. PMID 16136013.
- ^ Meisenberg G, Simmons WH (1984). "Amastatin potentiates the behavioral effects of vasopressin and oxytocin in mice". Peptides. 5 (3): 535–9. doi:10.1016/0196-9781(84)90083-4. PMID 6540873. S2CID 3881661.
- ^ Stancampiano R, Melis MR, Argiolas A (1991). "Proteolytic conversion of oxytocin by brain synaptic membranes: role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119–25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950. S2CID 36706540.
- ^ Itoh C, Watanabe M, Nagamatsu A, Soeda S, Kawarabayashi T, Shimeno H (1997). "Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization". Biol. Pharm. Bull. 20 (1): 20–4. doi:10.1248/bpb.20.20. PMID 9013800.
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