Biosynthesis and localization of phosphatidyl-scyllo-inositol in barley aleurone cells
Document Type
Article
Publication Date
1-1-1999
Department
Department of Chemistry
Abstract
A novel isomer of phosphatidylinositol (PI), phosphatidyl-scyllo- inositol, was characterized in the aleurone cells of barley seeds. In this investigation, the subcellular localization of scyllo-PI and the relative rates of biosynthesis and accumulation of [32P]phosphoric acid ([32Pi])- labeled scyllo- and myo-phosphoinositides in the plasma membrane and intracellular membrane pools were investigated. About 25% of the [32Pi]- labeled phospholipids were present in plasma membrane and 75% in intracellular membranes. Incorporation of [32Pi] into scyllo-PI was greater than into myo-PI in both the plasma membranes and intracellular membranes at all time points investigated, thus suggesting a higher rate of biosynthesis; however, the data do not preclude reduced breakdown of labeled scyllo-PI as a contributing factor. In vitro studies were conducted to investigate the presence of cytidinediphosphate diacylglycerol (CDP-DG):scyllo-inositol 3- phosphatidyltransferase (scyllo-PI synthase) and to optimize enzymatic activity. The inclusion of nonionic detergents (Brij 58 and Triton X-100) effected significant enhancement in the biosynthesis of scyllo-PI, whereas anionic, cationic, and zwitterionic detergents had little or no effect. This is the first evidence for CDP-DG:scyllo-inositol 3-phosphatidyltransferase activity.
Publication Title
Lipids
Recommended Citation
Carstensen, S.,
Pliska-Matyshak, G.,
Bhuvarahamurthy, N.,
Robbins, K.,
&
Murthy, P.
(1999).
Biosynthesis and localization of phosphatidyl-scyllo-inositol in barley aleurone cells.
Lipids,
34(1), 67-73.
http://doi.org/10.1007/s11745-999-339-y
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/5091