[Complication with paraaortic lymphadenectomy in gynecological cancer patients].

Although paraaortic lymphadenectomy is one of the standard treatments for gynecological cancer in Japan, it is very invasive so one must examine its safety for patients. Paraaortic lymphadenectomy was performed in 215. Two hundred and fifteen gynecologic cancer patients at our hospital between January 1991 and August 2005.

Impaired insulin-regulated membrane aminopeptidase translocation to the plasma membrane in adipocytes of Otsuka Long Evans Tokushima Fatty rats.

Insulin-regulated membrane aminopeptidase (IRAP) translocates to the plasma membrane with glucose transporter-4 (GLUT4) on insulin stimulation. However, this may be impaired in patients at risk of diabetes. Recently a novel technique has been developed to assess cell surface IRAP activity dynamically using a fluorogenic membrane impermeable substrate.

Placental leucine aminopeptidase might regulate the effects of oxytocin with resolution in endothelial cells.

Background: Oxytocin (OT) is known to cause vascular relaxation via nitric oxide (NO) production and proliferation of endothelial cells. Previously we revealed that human umbilical vascular endothelial cells (HUVECs) expresses placental leucine aminopeptidase (P-LAP)/insulin regulated aminopeptidase (IRAP), which becomes translocation to the cell surface on activation of oxytocin receptor (OTR). However, the physiological roles of P-LAP in HUVECs have not been elucidated.

Effects of estradiol administration on feto-placental growth in rat.

Background: To clarify the effect of estradiol benzoate on placental structure and its consequences for fetal survival and fetoplacental growth.

Study Design: Estradiol benzoate (0, 0.1, 1, 10, 100 microg/day) was infused intraperitoneally into pregnant Wistar rats from 12 to 19 days' gestation.

Enhancement of aminopeptidase A expression during angiotensin II-induced choriocarcinoma cell proliferation through AT1 receptor involving protein kinase C- and mitogen-activated protein kinase-dependent signaling pathway.

Angiotensin II (Ang II) is a bioactive peptide of the renin-angiotensin system, exerting its actions not only as a vasoconstrictor, but also as a growth promoter. In human placenta, type 1 Ang II receptors (AT(1)R) are predominantly expressed in trophoblasts, and we previously reported that aminopeptidase A (APA), a cell surface peptidase that converts Ang II to Ang III, is also expressed in both normal and neoplastic trophoblasts. However, the roles of Ang II and APA in trophoblast function remain to be clarified.

Hypertension and angiotensin II hypersensitivity in aminopeptidase A-deficient mice.

Local concentrations of the vasopressor peptide, angiotensin II (AngII), depend upon the balance between synthesis and degradation. Previous studies of blood pressure (BP) regulation have focused primarily on the generation of AngII and its receptors, and less attention has been devoted to angiotensin degradation. Aminopeptidase A (APA, EC 3.

Possible involvement of aminopeptidase A in hypertension in spontaneously hypertensive rats (SHRs) and change of refractoriness in response to angiotensin II in pregnant SHRs.

Background: Hypertension complicated with pregnancy is a major cause of maternal and fetal mortality, but its pathophysiology is unclear.

Objective: To investigate the pressor response to angiotensin II (Ang II) and the involvement of the Ang II degrading protease, aminopeptidase A, in spontaneously hypertensive rats (SHRs).

Design: Pregnant SHRs and Wistar-Kyoto (WKY) rats were studied.