Practical divergent synthesis of all possible regioisomers of myo-inositol trisphosphates

Chung, Sung‐Kee; Chang, Young‐Tae; Sohn, Kwang-Hoon

doi:10.1039/cc9960000163

Cited by 27 publications

(3 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Non-radiolabeled Ins(3,4,5,6)P 4 , Ins(1,4,5,6)P 4 and Ins(1,3,4)P 3 were purchased from CellSignals Inc (Lexington, KY). Ins(3,5,6)P 3 and Ins(4,5,6)P 3 were synthesized as previously described [23,24] and their identities were confirmed by 1 H, 13 C and 31 P NMR spectroscopy [23][24][25]. Previously unpublished 1 H, and 13 C NMR data for Ins(4,5,6)P 3 are as follows: 1 The purity of Ins(3,5,6)P 3 and Ins(4,5,6)P 3 was determined by HPLC separation followed by metal dye detection [26] using two complementary HPLC procedures that employ either an acidic or an alkaline gradient [27].…”

Section: Methodsmentioning

confidence: 99%

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate

Riley¹,

Deleu²,

Qian³

et al. 2005

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Ins(1,4,5,6)P4, a biologically active cell constituent, was recently advocated as a substrate of human Ins(3,4,5,6)P4 1-kinase (hITPK1), because stereochemical factors were believed relatively unimportant to specificity [Miller, G.J., Wilson, M.P., Majerus, P.W. and Hurley, J.H. (2005) Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-triphosphate 5/6-kinase. Mol. Cell. 18, 201-212]. Contrarily, we provide three examples of hITPK1 stereospecificity. hITPK1 phosphorylates only the 1-hydroxyl of both Ins(3,5,6)P3 and the meso-compound, Ins(4,5,6)P3. Moreover, hITPK1 has >13,000-fold preference for Ins(3,4,5,6)P4 over its enantiomer, Ins(1,4,5,6)P4. The biological significance of hITPK1 being stereospecific, and not physiologically phosphorylating Ins(1,4,5,6)P4, is reinforced by our demonstrating that Ins(1,4,5,6)P4 is phosphorylated (K(m) = 0.18 microM) by inositolphosphate-multikinase.

show abstract

Section: Methodsmentioning

confidence: 99%

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate

Riley¹,

Deleu²,

Qian³

et al. 2005

FEBS Letters

Self Cite

View full text Add to dashboard Cite

show abstract

“…-Ins(2,4,5)P $ , purified from bovine brain [19], was used for the experiments shown in Figure 3 and Table 2. ,-Ins(2,4,5)P $ was synthesized as previously reported [20] and used for the experiments shown in Figures 1 and 2. The substantial amounts of Ins(2,4,5)P $ needed to establish concentration-effect relationships by superfusion necessitated the use of synthetic enantiomeric ,-Ins(2,4,5)P $ (Figures 1 and 2).…”

Section: Methodsmentioning

confidence: 99%

Rapid kinetic measurements of 45Ca2+ mobilization reveal that Ins(2,4,5)P3 is a partial agonist at hepatic InsP3 receptors

Marchant¹,

Chang

Chung

et al. 1997

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

Ins(2,4,5)P3, a metabolically stable analogue of Ins(1,4,5)P3, is widely used in analyses of Ca2+ signalling pathways, but its utility depends upon it faithfully mimicking the effects of the natural messenger, Ins(1,4,5)P3, at InsP3 receptors. To compare the kinetics of InsP3-evoked 45Ca2+ mobilization, Ins(1,4,5)P3- and Ins(2,4,5)P3-stimulated 45Ca2+ release from the intracellular stores of permeabilized rat hepatocytes was measured using rapid superfusion. Both Ins(1,4,5)P3 and Ins(2,4,5)P3 caused concentration-dependent increases in the rate of 45Ca2+ efflux, which accelerated towards a peak and then abruptly switched to a bi-exponentially decaying release rate. However, the peak rate of 45Ca2+ mobilization evoked by maximal concentrations of Ins(2,4,5)P3 was only 65+/-3% (n = 3) of that evoked by Ins(1,4,5)P3. Furthermore, Ins(2,4,5)P3 inhibited the peak rate of 45Ca2+ efflux evoked by Ins(1,4,5)P3. These results indicate that Ins(2,4,5)P3 is a partial agonist at hepatic Ins(1,4,5)P3 receptors. Additionally, responses to Ins(2,4,5)P3 were less positively cooperative [Hill coefficient (h) = 1.9+/-0.3] than were those to Ins(1,4,5)P3 (h = 3.0+/-0.2) and the kinetics of termination of 45Ca2+ mobilization were slower. The lesser efficacy of Ins(2,4,5)P3 may account for the lower cooperativity in the responses it evokes, the slower inactivation of InsP3 receptors and the characteristic patterns of Ca2+ spiking it evokes in intact cells.

show abstract

“…All synthetic isomers of InsP 1 s (Chung and Chang, 1996a), InsP 2 s (Chung et al, 1998), InsP 3 s (Chung et al, 1996), InsP 4 s (Chung and Chang, 1995), and InsP 5 s (Chung and Chang, 1996b) were synthesized, and their structures and purities were confirmed in Dr. Sung-Kee Chung's laboratory (Pohang University of Science and Technology, Korea).…”

Section: Reagentsmentioning

confidence: 98%

Phytic Acid Synthesis and Vacuolar Accumulation in Suspension-Cultured Cells of Catharanthus roseus Induced by High Concentration of Inorganic Phosphate and Cations

et al. 2005

Self Cite

View full text Add to dashboard Cite

We have established a new system for studying phytic acid, myo-inositol hexakisphosphate (InsP 6 ) synthesis in suspensioncultured cells of Catharanthus. InsP 6 and other intermediates of myo-inositol (Ins) phosphate metabolism were measured using an ion chromatography method. The detection limit for InsP 6 was less than 50 nM, which was sufficient to analyze Ins phosphates in living cells. Synthesis of Ins phosphates was induced by incubation in high inorganic phosphate medium. InsP 6 was mainly accumulated in vacuoles and was enhanced when cells were grown in high concentration of inorganic phosphates with the cations K 1

show abstract

Practical divergent synthesis of all possible regioisomers of myo-inositol trisphosphates

Cited by 27 publications

References 16 publications

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate

Rapid kinetic measurements of 45Ca2+ mobilization reveal that Ins(2,4,5)P3 is a partial agonist at hepatic InsP3 receptors

Phytic Acid Synthesis and Vacuolar Accumulation in Suspension-Cultured Cells of Catharanthus roseus Induced by High Concentration of Inorganic Phosphate and Cations

Contact Info

Product

Resources

About

Practical divergent synthesis of all possible regioisomers of myo-inositol trisphosphates

Cited by 27 publications

References 16 publications

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P4 is not a physiologic substrate

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P4 is not a physiologic substrate

Rapid kinetic measurements of 45Ca2+ mobilization reveal that Ins(2,4,5)P3 is a partial agonist at hepatic InsP3 receptors

Phytic Acid Synthesis and Vacuolar Accumulation in Suspension-Cultured Cells of Catharanthus roseus Induced by High Concentration of Inorganic Phosphate and Cations

Contact Info

Product

Resources

About

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate

On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄ is not a physiologic substrate