Characterization of the Ca2+ Binding Sites of Calmodulin from Bovine Testis Using 43Ca and 113Cd NMR

Andersson, Thomas; Drakenberg, Torbjörn; Forsén, Sture; Thulin, Eva

doi:10.1111/j.1432-1033.1982.tb06808.x

Cited by 84 publications

(42 citation statements)

References 24 publications

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“…We suggest that Cd2+ binds with higher afa Unity to one of the four Ca~r-binding sites of CaM for which Mg:+ succesfully competes with Ca2 + . This result is in line with the results of Andersson et al (1982), who showed that Mg:+ decreases the 43Ca-CaM NMR signal (and therefore the binding of Ca2 + to CaM) but not the m Cd-CaM NMR signal. A higher affinity of CaM for Cd2 + was further indicated by the fact that Cd2 + elimi nates Ca2 + from Ca2 + -saturated CaM almost completely at equimolar concentrations of either metal ion.…”

Section: Binding O F Car* and Cd-+ To Calmodulinsupporting

confidence: 82%

Calmodulin-mediated cadmium inhibition of phosphodiesterase activity, in vitro

et al. 1987

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Abstract. Ion-stripped bovine brain calmodulin (CaM) binds 4 moles Cd2 + as well as 4 moles Ca2 + per mole pro tein, with similar affinity; in the presence of 1 mM Mg2 + the molar binding ratio of CaM for Ca2 + decreased to 3, the apparent K05 for Ca2 + nearly doubled, but the binding i characteristics of CaM for Cd" + were not changed. Satu rating concentrations Ca2 + did not affect the molar bind ing ratio of CaM for Cd2 + , but increased the apparent K05 for Cd2+; vice versa, saturating concentrations Cd2+ de creased the molar binding ratio for Ca2+ to 2 without af fecting the apparent K0 5 for Ca2 + .CaM-independent phosphodiesterase (PDE) activity was inhibited at [Cd2 + ] > 10-5 M. Cd2^ -CaM as well as Ca2 + -CaM activated PDE. However, the Cd: + -CaM com plex is less effective than the Ca: + -CaM complex in stimu lating CaM-dependent enzyme activities. Cd2+ inhibits Ca2 + -and CaM-dependent PDE in a competitive way. In troduction of Cd2 + in a medium containing Ca2 1 and CaM may, therefore, result in a reduction of CaM-dependent enzyme stimulation.By its interference with Ca2 + -and CaM-dependent PDE activity, Cd~f could upset the catabolic pathway of cellular cyclic nucleotide metabolism.

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Section: Binding O F Car* and Cd-+ To Calmodulinsupporting

confidence: 82%

Calmodulin-mediated cadmium inhibition of phosphodiesterase activity, in vitro

et al. 1987

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“…However, extensive n.m.r. studies (Forsen et al, 1980Andersson et al, 1982) suggest that the Ca2+-binding sites can be grouped into two sites with high affinity and two with low affinity.…”

Section: Introductionmentioning

confidence: 99%

The effects of Ca2+ and Cd2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study

Martin¹,

Bayley²

1986

Biochemical Journal

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Near-u.v. and far-u.v. c.d. spectra of bovine testis calmodulin and its tryptic fragments (TR1C, N-terminal half, residues 1-77, and TR2C, C-terminal half, residues 78-148) were recorded in metal-ion-free buffer and in the presence of saturating concentrations of Ca2+ or Cd2+ under a range of different solvent conditions. The results show the following: if there is any interaction between the N-terminal and C-terminal halves of calmodulin, it has not apparent effect on the secondary or tertiary structure of either half; the conformational changes induced by Ca2+ or Cd2+ are substantially greater in TR2C than they are in TR1C; the presence of Ca2+ or Cd2+ confers considerable stability with respect to urea-induced denaturation, both for the whole molecule and for either of the tryptic fragments; a thermally induced transition occurs in whole calmodulin at temperatures substantially below the temperature of major thermal unfolding, both in the presence and in the absence of added metal ion; the effects of Cd2+ are identical with those of Ca2+ under all conditions studied.

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“…The binding of ions to the polar groups of amphiphilic compounds is a subject of continuing interest and of great importance in various areas of chemistry and biochemistry (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). Unfortunately, as is often the case with biological systems, studies are hampered by the extreme complexity of the system being studied.…”

Section: Introductionmentioning

confidence: 99%

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

Tracey¹

1984

Can. J. Chem.

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ALAN S . TRACEY. Can. J. Chem. 62, 2161Chem. 62, (1984.The binding interactions of chloride and bromide ions have been studied in nematic lyotropic liquid crystalline materials prepared using the mixed detergent system of potassium dodecanoate/dodecylpyridinium chloride. The results from this study show that a three-site model of binding is sufficient to describe the behaviour of the observed quadrupole splittings. The results clearly reveal that the selectivity of ion binding is a function not only of the counterion but also of the detergent ion to which it is bound. In the cationic mesophase prepared from decylpyridinium, Cl-binds simultaneously to two and Br-to three headgroups. This contrasts with the alkyltrimethylammonium bromide system, where Cl-binds to three cationic amphiphiles while Br-binds to two. Sodium ion appears indifferent to the type of cationic detergent present, a result in accordance with the expectation that its binding is determined only by the headgroup of the anionic detergent. Extension of the three-site theory to take into account the effect of surface charge on ion binding provides information concerning relative strengths of binding. In the dodecylpyridinium system CI-binds only weakly compared to Br-whereas in the alkyltrimethylammonium system Clbinds more strongly than Br-. K' binds most strongly to dodecanoate anion, CsC least strongly, and the other alkali metal ions occupy intermediate positions. IntroductionThe binding of ions to the polar groups of amphiphilic compounds is a subject of continuing interest and of great importance in various areas of chemistry and biochemistry (1-12). Unfortunately, as is often the case with biological systems, studies are hampered by the extreme complexity of the system being studied. For the particular case of ion binding a further impediment often encountered is that the details of the stereochemical requirements which are imposed on a substrate by the ion during binding interactions are not known. A study of simple systems can often provide the background information necessary for understanding the more complex systems.A particularly suitable medium for studying ion interactions is that of lyotropic liquid crystals. Of these materials, those which have the property of spontaneously aligning in the magnetic field of a nuclear magnetic resonance spectrometer provide distinct advantages, the most important one being "sharp" nrnr transitions, which result from the fact that the mesophase directors are aligned homogeneously by the magnetic field of the spectrometer (1 3).Of particular utility in the study of ion binding is the mixed detergent system prepared from potassium dodecanoate (potassium laurate) and alkyltrimethylammonium bromide. This system has the advantage in that, under the appropriate conditions, the potassium dodecanoate can be replaced in a stepwise fashion by alkyltrimethylammonium bromide, thus progressing

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Characterization of the Ca²⁺ Binding Sites of Calmodulin from Bovine Testis Using ⁴³Ca and ¹¹³Cd NMR

Cited by 84 publications

References 24 publications

Calmodulin-mediated cadmium inhibition of phosphodiesterase activity, in vitro

Calmodulin-mediated cadmium inhibition of phosphodiesterase activity, in vitro

The effects of Ca2+ and Cd2+ on the secondary and tertiary structure of bovine testis calmodulin. A circular-dichroism study

The interactions of the chloride and bromide ions in nematic lyotropic liquid crystalline solution

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