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Mona Nystad, Vasilis Sitras, Cecilie Valborg Nordbakken, Mona Irene Pedersen, Ganesh Acharya
INTRODUCTION: Laeverin is a placenta-specific protein that is normally expressed in the plasma membrane of human trophoblasts. In previous studies, we showed higher expression levels of laeverin gene in preeclamptic compared with normal placentas and found that laeverin protein was ectopically expressed in the cytoplasm of the preeclamptic placentas. Our objective was to investigate laeverin protein expression in normal and preeclamptic placentas combining immunohistochemistry and immunofluorescence...
May 2018: Acta Obstetricia et Gynecologica Scandinavica
Mona Nystad, Vasilis Sitras, Kari Flo, Christian Widnes, Åse Vårtun, Tom Wilsgaard, Ganesh Acharya
BACKGROUND: Laeverin is a placenta-specific membrane-bound aminopeptidase. In this study we wanted to: 1) serially measure plasma levels of laeverin in healthy women during the second half of pregnancy and postpartum, 2) determine whether laeverin is differently expressed at 22-24 weeks in women who later develop preeclampsia compared to controls, 3) compare laeverin protein expression in placenta and umbilical vein serum in healthy and preeclamptic pregnancies at birth. METHODS: Plasma was obtained serially, approximately every 4-weeks, from 53 healthy women with uncomplicated pregnancies during 22+0 to 39+6 weeks of gestation, and at 22-24 weeks from 15 women who later developed preeclampsia...
November 25, 2016: BMC Pregnancy and Childbirth
Mona Nystad, Vasilis Sitras, Merethe Larsen, Ganesh Acharya
OBJECTIVE: The purpose of this study was to investigate the expression and subcellular localization of laeverin, a placenta-specific membrane-bound aminopeptidase, in preeclamptic placentas and its role in trophoblast cell migration and invasion. STUDY DESIGN: Expression of laeverin was investigated in 6 normal and 6 preeclamptic placentas with the use of immunofluorescence, sodium dodecylsulfate-polyacrylamide gel electrophoresis with Western blot analysis and immunoelectron microscopy...
December 2014: American Journal of Obstetrics and Gynecology
Akihito Horie, Hiroshi Fujiwara, Yukiyasu Sato, Koh Suginami, Hisanori Matsumoto, Masato Maruyama, Ikuo Konishi, Akira Hattori
BACKGROUND: In primate placenta, extravillous trophoblast (EVT) invades maternal tissue in temporally- and spatially-regulated fashions. We previously identified a novel placenta-specific cell-surface aminopeptidase, laeverin/aminopeptidase Q, which is expressed on EVT-lineage cells in the fetal membrane. Laeverin possesses a peptide-binding site that is evolutionally unique to primates, suggesting possible involvement of laeverin in a primate-specific phenomenon during placentation. Thus, this study was designed to elucidate the molecular characteristics and physiological roles of laeverin in human EVT...
May 2012: Human Reproduction
Yoshikuni Goto, Rina Yoshioka, Naomi Arisaka, Akira Hattori, Masafumi Tsujimoto
Human laeverin/aminopeptidase Q (APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of extravillous trophoblasts. In this study, we examined the significance of Gln-238 of laeverin/APQ, a putative S1 site residue, by site-directed mutagenesis for its enzymatic activity and substrate specificity. Replacement of Gln-238 with Ala caused a significant change in substrate specificity rather than a decrease in enzymatic activity. These results indicate that Gln-238 is important for the substrate specificity of laeverin/APQ...
2011: Biological & Pharmaceutical Bulletin
Masato Maruyama, Naomi Arisaka, Yoshikuni Goto, Yosuke Ohsawa, Hideshi Inoue, Hiroshi Fujiwara, Akira Hattori, Masafumi Tsujimoto
Human laeverin/aminopeptidase Q (LVRN/APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of human extravillous trophoblasts. Multiple sequence alignment of human M1 aminopeptidase revealed that the first Gly residue within the conserved exopeptidase motif of the M1 family, GXMEN motif, is uniquely substituted for His in human LVRN/APQ. In this study, we evaluated the roles of nonconserved His(379), comprising the exopeptidase motif in the enzymatic properties of human LVRN/APQ...
December 11, 2009: Journal of Biological Chemistry
V Sitras, R H Paulssen, H Grønaas, J Leirvik, T A Hanssen, A Vårtun, G Acharya
We investigated the global placental gene expression profile in severe preeclampsia. Twenty-one women were randomly selected from 50 participants with uncomplicated pregnancies to match 21 patients with severe preeclampsia. A 30K Human Genome Survey Microarray v.2.0 (Applied Biosystems) was used to evaluate the gene expression profile. After RNA isolation, five preeclamptic placentas were excluded due to poor RNA quality. The series composed of 37 hybridizations in a one-channel detection system of chemiluminescence emitted by the microarrays...
May 2009: Placenta
Masato Maruyama, Akira Hattori, Yoshikuni Goto, Masamichi Ueda, Michiyuki Maeda, Hiroshi Fujiwara, Masafumi Tsujimoto
Laeverin/aminopeptidase Q (APQ) is a cell surface protein specifically expressed on human embryo-derived extravillous trophoblasts that invades the uterus during placentation. The cDNA cloning of Laeverin/APQ revealed that the sequence encodes a protein with 990 amino acid residues, and Laeverin/APQ contains the HEXXHX(18)E gluzincin motif, which is characteristic of the M1 family of aminopeptidases, although the exopeptidase motif of the family, GAMEN, is uniquely substituted for the HAMEN sequence. In this study, we expressed a recombinant human Laeverin/APQ using a baculovirus expression system, purified to homogeneity, and characterized its enzymatic properties...
July 13, 2007: Journal of Biological Chemistry
H Fujiwara
During human placentation, the extravillous trophoblast (EVT) invades maternal decidua and spiral arteries. However, the precise regulatory mechanisms by which EVT invasion is induced toward maternal arteries or limited within the uterus have not been well characterized. Recently, we found that dipeptidyl peptidase IV, a membrane-bound cell surface peptidase that can degrade chemokines, including RANTES, was expressed on EVT that had already ceased invasion. Another cell surface peptidase, carboxypeptidase-M, was also detected on EVT including the endovascular trophoblast in the maternal arteries...
April 2007: Placenta
Christian S Haas, Chad J Creighton, Xiujun Pi, Ira Maine, Alisa E Koch, G Kenneth Haines, Song Ling, Arul M Chinnaiyan, Joseph Holoshitz
OBJECTIVE: To identify disease-specific gene expression profiles in patients with rheumatoid arthritis (RA), using complementary DNA (cDNA) microarray analyses on lymphoblastoid B cell lines (LCLs) derived from RA-discordant monozygotic (MZ) twins. METHODS: The cDNA was prepared from LCLs derived from the peripheral blood of 11 pairs of RA-discordant MZ twins. The RA twin cDNA was labeled with cy5 fluorescent dye, and the cDNA of the healthy co-twin was labeled with cy3...
July 2006: Arthritis and Rheumatism
Hiroshi Fujiwara, Toshihiro Higuchi, Yukiyasu Sato, Yoshihiro Nishioka, Bin-Xiang Zeng, Shinya Yoshioka, Keiji Tatsumi, Masamichi Ueda, Michiyuki Maeda
During human placentation, the invasion of extravillous trophoblasts (EVTs) into maternal decidual tissues, especially toward maternal spiral arteries, is considered an essential process for subsequent normal fetal development. However, the precise regulatory mechanisms to induce EVT invasion toward arteries and/or to protect EVTs from further invasion have not been well understood. Recently, we found that two cell surface peptidases, dipeptidyl peptidase IV (DPPIV) and carboxypeptidase-M (CP-M,) are differentially expressed on EVTs...
August 1, 2005: Biochimica et Biophysica Acta
Hiroshi Fujiwara, Toshihiro Higuchi, Shigetoshi Yamada, Takeshi Hirano, Yukiyasu Sato, Yoshihiro Nishioka, Shinya Yoshioka, Keiji Tatsumi, Masamichi Ueda, Michiyuki Maeda, Shingo Fujii
Human extravillous trophoblasts (EVTs) invade the maternal decidua. To identify the molecules involved in EVT invasion, we raised a murine monoclonal antibody (CHL2) that reacts with human EVTs. The molecular mass of CHL2 antigen purified from placental tissues was 160 kDa. Although the N-terminal partial amino acid sequence and one internal sequence are still unreported, the other three internal sequences matched those deduced from the coding region of the estimated sequence tag (1672 bp, AK075131). Based on this information, the full-length of the coding cDNA sequence of CHL2 antigen (2970 bp), which has not been reported elsewhere, was determined by 5' RACE...
January 23, 2004: Biochemical and Biophysical Research Communications
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