Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy.
Biochim Biophys Acta
; 1751(1): 19-25, 2005 Aug 01.
Article
de En
| MEDLINE
| ID: mdl-15894523
ABSTRACT
Human pregnancy serum and placenta have the ability to degrade uterotonic peptide oxytocin (OT). Placental leucine aminopeptidase (P-LAP), which is also called cystine aminopeptidase, is the only membrane aminopeptidase known to functionally degrade OT as oxytocinase (OTase). P-LAP/OTase hydrolyzes several peptides other than OT including vasopressin and angiotensin III. P-LAP/OTase predicted from cDNA sequence is a type II integral membrane protein, which is converted to a soluble form existing in maternal serum by metalloproteases, possibly ADAM (a disintegrin and metalloproteinase) members. P-LAP/OTase activity increases with normal gestation, while decreases in the patients with preterm delivery and severe preeclampsia. In placenta, P-LAP/OTase is predominantly expressed in differentiated trophoblasts, syncytiotrophoblasts. Activator protein-2 (AP-2) and Ikaros transcription factors play significant roles in exerting high promoter activity of P-LAP/OTase in the trophoblastic cells. Moreover, P-LAP/OTase is transcriptionally regulated in a trophoblast-differentiation-dependent fashion via up-regulation of AP-2, putatively AP-2alpha. P-LAP/OTase may be involved in maintaining pregnancy homeostasis via metabolizing peptides such as OT and vasopressin.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Cystinyl aminopeptidase
/
Placenta
/
Grossesse
/
Ocytocine
Type d'étude:
Prognostic_studies
Limites:
Female
/
Humans
Langue:
En
Journal:
Biochim Biophys Acta
Année:
2005
Type de document:
Article
Pays d'affiliation:
Japon