A unique biosynthetic pathway for gangliosides exists in <i>Xenopus laevis</i> oocytes

Hidari, Kazuya I.P.J.; Nagai, Yoshitaka; Sanai, Yutaka

doi:10.1016/0014-5793(94)01005-6

Cited by 7 publications

(3 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Glucosylceramide synthase catalyzes the first step in the ganglioside biosynthetic pathway (Fig. 1); as other ganglioside glucosyltransferases, this enzyme is associated with the ER/Golgi membranes in Xenopus oocytes [19]. Therefore, the main effect of its inhibition by PDMP in whole oocyte should be an increase in the level of ceramide and sphingomyelin in the inner leaflet of membrane vesicles trafficking from the ER through the Golgi apparatus to the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte

Smedt¹,

Rime

Jessus

et al. 1995

FEBS Letters

View full text Add to dashboard Cite

In Xenopus prophase-blocked oocytes, it is assumed that progesterone interacts with the plasma membrane to initiate a signalling cascade that ultimately leads to MPF activation. Progesterone regulates negatively the cAMP pathway through an inhibition of adenylate cyclase. However, the mechanisms linking the initial action of the hormone with adenylate cyclase activity remain to be elucidated. Here, we demonstrate that PDMP, an inhibitor of glucosphingolipid synthesis, triggers oocyte meiotic maturation in a cAMP- and cycloheximide-dependent manner, whereas exogenous ceramide is unefficient. We propose that sphingolipid metabolism and targeting represent an important regulatory process of oocyte meiosis.

show abstract

Section: Discussionmentioning

confidence: 99%

“…The possibility that metabolism between sphingolipids and glycosphingolipids ( Fig. l), which have been characterized in Xenopus oocyte membranes [19], is involved in MPF activation was then investigated.…”

Section: Exogenous Ceramide Does Not Promote Gvbd In Oocytes From Unsmentioning

confidence: 99%

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte

Smedt¹,

Rime

Jessus

et al. 1995

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…We have been investigating a biosynthesis of gangliosides during normal neuronal development and oncogenic transformation (12)(13)(14)(15)(16)(17)(18)(19)(20). Ganglioside biosynthesis takes place in the Golgi apparatus, where glucosylceramide is glycosylated by sequential addition of galactose, sialic acid, and N-acetylgalactosamine.…”

mentioning

confidence: 99%

Association of Src Family Tyrosine Kinase Lyn with Ganglioside GD3 in Rat Brain

Kasahara

Watanabe

Yamamoto

et al. 1997

Journal of Biological Chemistry

Self Cite

174

View full text Add to dashboard Cite

Association of gangliosides with specific proteins in the central nervous system was examined by co-immunoprecipitation with anti-ganglioside antibody. Protein kinase activity was detected in precipitates with monoclonal antibody to ganglioside G D3 (R24) from membranal fraction of rat brain. Using in vitro kinase assay, several phosphorylated proteins of 40, 53, 56, and 80 kDa were isolated by gel electrophoresis. Of these proteins, the proteins of 53 and 56 kDa (p53/56) were identified as two isoforms of Src family tyrosine kinase Lyn, based on co-migration during gel electrophoresis, comparative peptide mapping, and sequential immunoprecipitation with anti-Lyn antibody. The identification was confirmed using a cDNA expression system in Chinese hamster ovary (CHO) cells, which express solely ganglioside G M3 , the enzymatic substrate of G D3 synthase. In cotransfection with G D3 synthase and Lyn expression plasmids, R24 immunoprecipitated Lyn and anti-Lyn antibody immunoprecipitated G D3 . R24 treatment of rat primary cerebellar cultures induced Lyn activation and rapid tyrosine phosphorylation of several substrates including mitogen-activated protein kinases. Furthermore, sucrose density gradient analysis showed that Lyn of cerebellum and CHO transfectants were detected in a low density light-scattering band, i.e. the caveolae membrane fraction. R24 immunoprecipitated caveolin from Triton X-100 extract of CHO transfectants. These observations suggest that G D3 may regulate Lyn in a caveolae-like domain on brain cell membranes.

show abstract

Glycosylated and Phosphorylated Proteins—Expression in Yeast and Oocytes of Xenopus: Prospects and Challenges—Relevance to Expression of Thermostable Proteins

Gao

Arellano

et al. 2001

Protein Expression and Purification

View full text Add to dashboard Cite

A unique biosynthetic pathway for gangliosides exists in Xenopus laevis oocytes

Cited by 7 publications

References 22 publications

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte

Association of Src Family Tyrosine Kinase Lyn with Ganglioside GD3 in Rat Brain

Glycosylated and Phosphorylated Proteins—Expression in Yeast and Oocytes of Xenopus: Prospects and Challenges—Relevance to Expression of Thermostable Proteins

Contact Info

Product

Resources

About

A unique biosynthetic pathway for gangliosides exists in Xenopus laevis oocytes

Cited by 7 publications

References 22 publications

Inhibition of glycosphingolipid synthesis induces p34cdc2 activation in Xenopus oocyte

Inhibition of glycosphingolipid synthesis induces p34cdc2 activation in Xenopus oocyte

Association of Src Family Tyrosine Kinase Lyn with Ganglioside GD3 in Rat Brain

Glycosylated and Phosphorylated Proteins—Expression in Yeast and Oocytes of Xenopus: Prospects and Challenges—Relevance to Expression of Thermostable Proteins

Contact Info

Product

Resources

About

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte

Inhibition of glycosphingolipid synthesis induces p34^cdc2 activation in Xenopus oocyte