Complexation studies on inositol-phosphates: IV. Ca(II) complexes of myo-inositol 1,4,5-trisphosphate

doi:10.1016/0162-0134(92)84036-M

Journal of Inorganic Biochemistry

Volume 45, Issue 1, January 1992, Pages 13-19

https://doi.org/10.1016/0162-0134(92)84036-M Get rights and content

Abstract

The stability constants of the complexes formed between Ca²⁺ and the myo-inositol 1,4,5-trisphosphate (Ins(1,4,5)P₃) were determined by potentiometric titration in two different media and temperature conditions (medium 1: I = 0.1 M But₄NBr, 25°C; medium 2: I = 0.2 M KCl, 37°C). Mainly because of the presence of potassium the results obtained in these media show large differences in both the nature and the stability of the complexes. In medium 1, MH₂L and M₂L species are formed along with the ML and MHL species which also exist in medium 2. In addition, the stability of the latter species decreases by more than one log unit in going from medium 1 to medium 2. In an attempt to assess the biological significance of the metal binding to Ins(1,4,5)P₃, the results were compared to the Ca²⁺-ATP complexes that form in the same media conditions. Taking into account the relative stability of the complexes of both systems, it is likely that the action or metabolism of Ins(1,4,5)P₃ may be influenced by coordination of either alkali or alkali-earth cations.

References (19)

S.R. Nahorski et al.
Trends Pharmacol. Sci.
(1986)
P.F. Worley et al.
J. Biol. Chem.
(1987)
H. Bieth et al.
J. Inorg. Biochem.
(1990)
A. Sabatini et al.
Talanta
(1974)
M.J. Berridge et al.
Nature
(1984)
M.J. Berridge et al.
Nature
(1984)
M.J. Berridge
Biochem. J.
(1984)
M.J. Berridge et al.
Nature
(1989)
M.J. Berridge
JAMA
(1989)

There are more references available in the full text version of this article.

Cited by (15)

Investigation of the ternary D-myo-inositol 1,2,6-tris(phosphate)-spermine-Zn2+ system in solution
2001, Journal of Inorganic Biochemistry
Interactions of Ins(1,2,6)P₃ (IP), with spermine (Spm) and zinc cations have been studied by potentiometric and ³¹P NMR titrations. In the 4–11 pH range, two IPSpmZn₂H₃ and IPSpmZn₂H mixed complexes are formed which are largely predominant with respect to the binary species. According to ³¹P NMR titration it is likely that one of the zinc cations preferably binds phosphates P1 and P6. The adduct formation between Ins(1,2,6)P₃ and spermine seems also favourable to the formation of the mixed complexes. The occurrence of ternary complexes involving inositol-phosphates, biogenic amines, and metallic cations may be of relevance in the regulation of biological processes.
Carbohydrates as ligands: Coordination equilibria and structure of the metal complexes
2000, Coordination Chemistry Reviews
Citation Excerpt :
A polysaccharide–iron complex named ‘Nifrex’ obtained from Fe(III)-chloride and Glc is also being used for treatment of iron deficiency anaemia [85,86]. There are many experiments in progress to develop other sugar type ligands like the l-idopyranosiduronic acid — containing oligosaccharides (Sarkar et al. [16]), or modified inositols (Hegetschweiler et al., [39] and Spiess et al. [87,88]). The Zn(II)–HyA complex has been patented and used as a medicine for the treatment of crural ulcer, decubitus and primarily non-healing wounds [89].
Simple sugars and their derivatives — with oxygen, nitrogen, sulphur or phosphorous anchoring donor groups — form metal ion complexes of various composition and stability. The emergence of new experimental methods allowed the assignment of the metal binding sites in the different isomeric complexes of these multidentate ligands, and also the determination of the most effective chelating isomers of the ligands — being present as a mixture of different conformational and/or configurational isomers in solution. We review the literature on the metal ion complexes of carbohydrate type ligands with the emphasis on the past 20 years, discussing the equilibria and structure in aqueous solution together with the structures determined for the solid state complexes. Stability and structural data are collected for comparison.
Complexation of spermine and spermidine by myo-inositol 1,4,5-tris(phosphate) and related compounds: Biological significance
1996, Biochimica et Biophysica Acta - General Subjects
D myo-inositol 1,4,5-tris(phosphate) (Ins(1,4,5)P₃) displays a multicoordination site arrangement that allows strong interactions with polycationic species such as the naturally occurring polyamines spermine and spermidine. In the present work, the complexation of these polyamines by Ins(1,4,5)P₃ and related compounds was quantitatively investigated. The study was performed in a 0.1 M tetramethylammonium p-toluenesulfonate (Me₄NOTs) solution at 25°C. For purpose of comparison, the complexation of the polyamine-ATP systems were also considered in the same experimental conditions. ³⁴P-NMR experiments showed for Ins(1,4,5)P₃ and its analogues, the formation of complexes of a 1:1 stoichiometry. As expected, the most stable complexes are formed between the most charged partners. In addition, the basicity of the phosphate groups seems to govern the stability of the complexes. If both ATP and Ins(1,4,5)P₃ are present at the same concentration, the latter interacts preferably with the polyamines. Ins(1,4,5)P₃-spermine complex formation provides a possible simple explanation for the inhibition by spermine of Ins(1,4,5)P₃-induced Ca²⁺ release. Spermine will undoubtedly compete with metallic cations such as Ca²⁺ in the intracellular medium and consequently, may play a regulatory role in the signal transduction mediated by Ins(1,4,5)P₃.
Effect of hypothermia on intracellular Ca2+ in rabbit renal tubules suspended in UW-gluconate preservation solution
1996, Cryobiology
Altered cellular calcium (Ca) homeostasis may be important in mediating hypothermic injury in preserved kidneys. In this study the effect of hypothermic (5°C) storage on ionized intracellular Ca concentration ([Ca]_i) in rabbit tubules was examined using Indo-1. Tubules were stored up to 250 min in UW-gluconate solution containing either 0.0, 0.5, 1.5, or 5.0 mMCa (yielding about 3.6, 62, 371, and 1,010 μMionized solution Ca (Ca²⁺) at 5°C, respectively). [Ca]_iincreased to about 1,600 nMwithin 1 min after suspension in UW solution followed by a decrease in [Ca]_iduring the subsequent 60 min in all groups, suggesting mitochondrial Ca sequestration. Thereafter, [Ca]_ieither 1) increased in tubules incubated with 1.5 and 5.0 mMCa to levels greater than 2,500 nM;2) decreased to about 800 nMin tubules incubated with 0.5 mMCa and then remained stable; or 3) continued to decrease in tubules incubated with 0.0 mMadded Ca to reach an apparent steady-state concentration of about 175 nMafter 180 min of incubation. The early spike in [Ca]_iwas unaffected by adding EGTA (solution Ca²⁺= 50 nM). Ryanodine eliminated the [Ca]_ispike, indicating that cooling in UW-gluconate solution caused release of endoplasmic reticulum Ca. This study shows that [Ca]_iinitially increases after exposure to UW-gluconate solution and appears to be transiently buffered through intracellular, probably mitochondrial, sequestration. Saturation of cellular buffer mechanisms resulted in a sustained dependence of [Ca]_ion extracellular Ca²⁺. These results support the hypothesis that the effect of Ca on kidney viability is related to solution-induced alterations in [Ca]_i.
Complexation studies on inositol-phosphates, VI. Al3+ complexes of DL-myo-inositol 1,4,5-triphosphate and D-myo-inositol 1,2,6-triphosphate
1995, Journal of Inorganic Biochemistry
Aluminum complexes of D-myo-inositol 1,2,6-triphosphate (Ins(1,2,6)P₃) and DL-myo-inositol 1,4,5-triphosphate (Ins(1,4,5)P₃) have been studied by potentiometry at 25°C in a 0.1 M tetrabutylammonium bromide medium. Both ligands form AlHL, AlL, and AlOHL species whereas Ins(1,2,6)P₃ forms, in addition, an Al₂L complex and Ins(1,4,5)P₃ an Al(OH)₂L species. In an attempt to assess the biological significance of the Al³⁺ binding to Ins(1,4,5)P₃, the results were compared to the Al³⁺-ATP complexes that have been found in similar medium conditions. Taking into account the relative stability of the complexes of both systems, it appears likely that the intracellular second messenger system involving Ins(1,4,5)P₃ may be disturbed by the presence of the aluminum cation.
Complexation studies on inositol-phosphates. V. Cu2+, Zn2+, Fe2+ and Fe3+ complexes of some myo-inositol triphosphates
1994, Journal of Inorganic Biochemistry
Potentiometry and ³¹P NMR spectroscopy have been used to study the protonation and complexation properties of some myo-inositol triphosphates (Ins(1,2,6)P₃, Ins(1,3,5)P₃, and Ins(2,4,6)P₃) with Cu²⁺, Zn²⁺, Fe²⁺, and Fe³⁺. The study was performed for all the ligands at 25°C in a 0.1 M tetrabutylammonium bromide solution (medium 1) and in addition, for Ins(1,2,6)P₃, at 37°C in a 0.2 M KCl medium (medium 2). The position of the phosphate groups around the inositol ring largely influences the basicity of the ligand. Log β₀₁₁ has the highest value for Ins(1,2,6)P₃ which displays three vicinal phosphates. When no interfering cations such as K⁺ are present, M₂HL, M₂L, MHL, ML, and MOHL complexes were found for most of the systems. Although the stability of the complexes follows the Irving-Williams rule, i.e., Cu(II) > Zn(II) > Fe(II), no real selectivity of complexation is observed. A ³¹P NMR titration was performed for the Zn²⁺-^H+-Ins(1,2,6)P₃ system. The resulting titration curves, compared with those obtained in the absence of metal showed two opposite effects: i) a downfield shift due to the competition of the metal with the proton, ii) an upfield shift corresponding to the binding of Zn²⁺. From these curves it can, in addition, be concluded that the cation in the mononuclear species is mainly coordinated to P1 and P2 whereas the second cation of the homodinuclear complex is stabilized by P6.

View all citing articles on Scopus

View full text

Article preview

Journal of Inorganic Biochemistry

Abstract

References (19)

Trends Pharmacol. Sci.

J. Biol. Chem.

J. Inorg. Biochem.

Talanta

Nature

Nature

Biochem. J.

Nature

JAMA

Cited by (15)

Investigation of the ternary D-myo-inositol 1,2,6-tris(phosphate)-spermine-Zn<sup>2+</sup> system in solution

Carbohydrates as ligands: Coordination equilibria and structure of the metal complexes

Complexation of spermine and spermidine by myo-inositol 1,4,5-tris(phosphate) and related compounds: Biological significance

Effect of hypothermia on intracellular Ca<sup>2+</sup> in rabbit renal tubules suspended in UW-gluconate preservation solution

Complexation studies on inositol-phosphates, VI. Al<sup>3+</sup> complexes of DL-myo-inositol 1,4,5-triphosphate and D-myo-inositol 1,2,6-triphosphate

Complexation studies on inositol-phosphates. V. Cu<sup>2+</sup>, Zn<sup>2+</sup>, Fe<sup>2+</sup> and Fe<sup>3+</sup> complexes of some myo-inositol triphosphates