scholarly journals Lack of significant differences in the corrected activity of lysophospholipase D, producer of phospholipid mediator lysophosphatidic acid, in incubated serum from women with and without ovarian tumors

Cancer ◽  
2001 ◽  
Vol 94 (1) ◽  
pp. 141-151 ◽  
Author(s):  
Akira Tokumura ◽  
Kyoko Tominaga ◽  
Katsuhiko Yasuda ◽  
Hideharu Kanzaki ◽  
Kentaro Kogure ◽  
...  
Author(s):  
J MORISHIGE ◽  
K TOUCHIKA ◽  
T TANAKA ◽  
K SATOUCHI ◽  
K FUKUZAWA ◽  
...  

2006 ◽  
Vol 26 (13) ◽  
pp. 5015-5022 ◽  
Author(s):  
Laurens A. van Meeteren ◽  
Paula Ruurs ◽  
Catelijne Stortelers ◽  
Peter Bouwman ◽  
Marga A. van Rooijen ◽  
...  

ABSTRACT Autotaxin (ATX), or nucleotide pyrophosphatase-phosphodiesterase 2, is a secreted lysophospholipase D that promotes cell migration, metastasis, and angiogenesis. ATX generates lysophosphatidic acid (LPA), a lipid mitogen and motility factor that acts on several G protein-coupled receptors. Here we report that ATX-deficient mice die at embryonic day 9.5 (E9.5) with profound vascular defects in yolk sac and embryo resembling the Gα13 knockout phenotype. Furthermore, at E8.5, ATX-deficient embryos showed allantois malformation, neural tube defects, and asymmetric headfolds. The onset of these abnormalities coincided with increased expression of ATX and LPA receptors in normal embryos. ATX heterozygous mice appear healthy but show half-normal ATX activity and plasma LPA levels. Our results reveal a critical role for ATX in vascular development, indicate that ATX is the major LPA-producing enzyme in vivo, and suggest that the vascular defects in ATX-deficient embryos may be explained by loss of LPA signaling through Gα13.


2005 ◽  
Vol 125 (3) ◽  
pp. 421-427 ◽  
Author(s):  
Juliette Mazereeuw-Hautier ◽  
Sandra Gres ◽  
Madie Fanguin ◽  
Clotilde Cariven ◽  
Josette Fauvel ◽  
...  

2002 ◽  
Vol 43 (6) ◽  
pp. 904-910 ◽  
Author(s):  
Stéphane Gesta ◽  
Marie-Françoise Simon ◽  
Astrid Rey ◽  
David Sibrac ◽  
Alexia Girard ◽  
...  

2002 ◽  
Vol 67 (5) ◽  
pp. 1386-1392 ◽  
Author(s):  
Akira Tokumura ◽  
Yumi Kanaya ◽  
Maki Miyake ◽  
Shuji Yamano ◽  
Minoru Irahara ◽  
...  

2006 ◽  
Vol 21 (12) ◽  
pp. 3612-3613 ◽  
Author(s):  
R. Ohkawa ◽  
N. Hisano ◽  
K. Nakamura ◽  
S. Okubo ◽  
H. Yokota ◽  
...  

2002 ◽  
Vol 158 (2) ◽  
pp. 227-233 ◽  
Author(s):  
Makiko Umezu-Goto ◽  
Yasuhiro Kishi ◽  
Akitsu Taira ◽  
Kotaro Hama ◽  
Naoshi Dohmae ◽  
...  

Autotaxin (ATX) is a tumor cell motility–stimulating factor, originally isolated from melanoma cell supernatants. ATX had been proposed to mediate its effects through 5′-nucleotide pyrophosphatase and phosphodiesterase activities. However, the ATX substrate mediating the increase in cellular motility remains to be identified. Here, we demonstrated that lysophospholipase D (lysoPLD) purified from fetal bovine serum, which catalyzes the production of the bioactive phospholipid mediator, lysophosphatidic acid (LPA), from lysophosphatidylcholine (LPC), is identical to ATX. The Km value of ATX for LPC was 25-fold lower than that for the synthetic nucleoside substrate, p-nitrophenyl-tri-monophosphate. LPA mediates multiple biological functions including cytoskeletal reorganization, chemotaxis, and cell growth through activation of specific G protein–coupled receptors. Recombinant ATX, particularly in the presence of LPC, dramatically increased chemotaxis and proliferation of multiple different cell lines. Moreover, we demonstrate that several cancer cell lines release significant amounts of LPC, a substrate for ATX, into the culture medium. The demonstration that ATX and lysoPLD are identical suggests that autocrine or paracrine production of LPA contributes to tumor cell motility, survival, and proliferation. It also provides potential novel targets for therapy of pathophysiological states including cancer.


2002 ◽  
Vol 277 (42) ◽  
pp. 39436-39442 ◽  
Author(s):  
Akira Tokumura ◽  
Eiji Majima ◽  
Yuko Kariya ◽  
Kyoko Tominaga ◽  
Kentaro Kogure ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document