|
C18H40NO5P
|
M.W. 381.49
|
Stability 1 year
|
Storage -20°C
|
|
Catalog
Number: 860536
|
|
|
| |
| Sphingosine-1-phosphate (SPP) is a lipid second
messenger that also acts as a first messenger through the G
protein-coupled receptor Edg-1. Here we show that SPP also binds
to the related receptors H218 and Edg3 with high affinity and
specificity. SPP and sphinganine-1-phosphate bind to these receptors,
whereas neither sphingosylphosphorylcholine nor lysophosphatidic
acid compete with SPP for binding to either receptor. 1 |
The activity of sphinganine kinase, the enzyme catalyzing the
first step in the breakdown of the sphingoid longchain base
sphinganine by converting it to sphinganine-1-phosphate, was
characterized in microsomes isolated from corn shoots using
Derythrosphinganine and ATP as substrates. Maximum product formation
required the presence of Mg2+. The apparent Km for ATP was 0.81
mM. GTP also served as a source of phosphate, whereas CTP and
UTP were not effective substrates in this assay. Fumonisin,
a mycotoxin that disrupts sphingolipid metabolism, did not alter
sphinganine kinase activity in vivo or in vitro. The results
of this study demonstrate, for the first time, the presence
of sphinganine kinase activity in plant tissue and suggest that
the properties of the kinase from corn microsomes are distinct
from those of the mammalian and protistan enzymes in some respects.
2
|
|
References:
- Van Brocklyn JR; Tu Z; Edsall LC; Schmidt RR; Spiegel
S., (1999), Sphingosine-1-phosphate induced cell rounding
and neurite retraction are mediated by the G protein-coupled
receptor H218., J Biol Chem, 274:8, 462632
- Crowther GJ; Lynch DV., (1997), Characterization of sphinganine
kinase activity in corn shoot microsomes. Arch Biochem
Biophys, 337:2, 28490
|
|
|
