Mammalian Glycerophosphodiester Phosphodiesterases
-
- YANAKA Noriyuki
- Department of Molecular and Applied Bioscience, Graduate School of Biosphere Science, Hiroshima University
Bibliographic Information
- Other Title
-
- Award review: Mammalian glycerophosphodiester phosphodiesterases
Search this article
Abstract
Bacterial glycerophosphodiester phosphodiesterases (GP-PDEs), GlpQ and UgpQ, are well-characterized periplasmic and cytosolic proteins that play critical roles in the hydrolysis of deacylated glycerophospholipids to glycerol phosphate and alcohol, which are utilized as major sources of carbon and phosphate. In contrast, two novel mammalian GP-PDEs, GDE1/MIR16 and GDE3, were recently identified, and were shown to be involved in several physiological functions. GDE1/MIR16 was identified as a membrane protein interacting with RGS16, a regulator of G protein signaling, and found to hydrolyze glycerophosphoinositol preferentially. We have found that expression of GDE3 is significantly up-regulated during osteoblast differentiation and is involved in morphological changes of cells. Furthermore, five mammalian GP-PDEs were virtually identified, and very recent studies indicate that retinoic acid-induced expression of GDE2 plays essential roles in neuronal differentiation and neurite outgrowth. Thus mammalian GP-PDEs are likely to be important in controlling numerous cellular events, indicating that the GP-PDE superfamily in mammals might be a pharmacological target in the future.
Journal
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 71 (8), 1811-1818, 2007
Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Tweet
Details 詳細情報について
-
- CRID
- 1390001206480287872
-
- NII Article ID
- 10027517101
-
- NII Book ID
- AA10824164
-
- ISSN
- 13476947
- 09168451
-
- NDL BIB ID
- 8887103
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
-
- Abstract License Flag
- Disallowed