Dissociation of Calmodulin-Target Peptide Complexes by the Lipid Mediator Sphingosylphosphorylcholine

Kovács, Erika; Tóth, Judit; Vértessy, Beáta G.; Liliom, Károly

doi:10.1074/jbc.m109.053116

Cited by 20 publications

(29 citation statements)

References 41 publications

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“…3A). This value compares well with the results of peptide binding assays (IC 50 = 19.4 ± 1.4 μM) [18]. S1P and LPA were ineffective, while LPC also decreased [ 35 S]CaM binding to SR vesicles (Fig.s 3B).…”

Section: Resultssupporting

confidence: 88%

“…Displacement of inhibitory Ca 2+ CaM from RyR1 has an activating effect, whereas direct interaction with RyR1 is inhibitory, negating the effects of SPC. [ 35 S]CaM binding studies (see below) and the fact that S1P (which does not interact with CaM [17,18]) further decreased [ 3 H]ryanodine binding in the presence of CaM (Fig. 2D), favour this explanation.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, we demonstrated that the sphingolipid disrupts the complex between CaM and the peptide representing the CaM-binding domain of RyR1 [18]. In this report, we describe the regulation of RyR1 by SPC focusing on the role of CaM.…”

Section: Introductionmentioning

confidence: 97%

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Regulation of ryanodine receptors by sphingosylphosphorylcholine: Involvement of both calmodulin-dependent and -independent mechanisms

Kovács¹,

Xu²,

Pasek³

et al. 2010

Biochemical and Biophysical Research Communications

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Sphingosylphosphorylcholine (SPC), a lipid mediator with putative second messenger functions, has been reported to regulate ryanodine receptors (RyRs), Ca 2+ channels of the sarco/endoplasmic reticulum. RyRs are also regulated by the ubiquitous Ca 2+ sensor calmodulin (CaM), and we have previously shown that SPC disrupts the complex of CaM and the peptide corresponding to the CaM-binding domain of the skeletal muscle Ca 2+ release channel (RyR1). Here we report that SPC also displaces Ca 2+ -bound CaM from the intact RyR1, which we hypothesized might lead to channel activation by relieving the negative feedback Ca 2+ CaM exerts on the channel. We could not demonstrate such channel activation as we have found that SPC has a direct, CaM-independent inhibitory effect on channel activity, confirmed by both single channel measurements and [ 3 H]ryanodine binding assays. In the presence of Ca 2+ CaM, however, the addition of SPC did not reduce [ 3 H]ryanodine binding, which we could explain by assuming that the direct inhibitory action of the sphingolipid was negated by the simultaneous displacement of inhibitory Ca 2+ CaM. Additional experiments revealed that RyRs are unlikely to be responsible for SPC-elicited Ca 2+ release from brain microsomes, and that SPC does not exert detergent-like effects on sarcoplasmic reticulum vesicles. We conclude that regulation of RyRs by SPC involves both CaM-dependent and -independent mechanisms, thus, the sphingolipid might play a pysiological role in RyR regulation, but channel activation previously attributed to SPC is unlikely.

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

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Regulation of ryanodine receptors by sphingosylphosphorylcholine: Involvement of both calmodulin-dependent and -independent mechanisms

Kovács¹,

Xu²,

Pasek³

et al. 2010

Biochemical and Biophysical Research Communications

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“…2 [52]. This model has also been used to investigate the binding and subsequent change in conformation that occurs for the complex between melittin and Ca 2+ -saturated calmodulin [76], as well as the interaction of a transcriptional activator-DNA complex with a coactivator [77], and the interaction of N -phenyl-1-naphthylamine with pheromone-binding proteins [78]. …”

Section: Stopped-flow Analysismentioning

confidence: 99%

“…In addition, this technique can be used to examine either slow or relatively fast events. Rate constants that have been determined by stopped-flow analysis have ranged from 10 −6 to 10 6 s −1 for first-order reactions and from 1 to 10 9 M −1 s −1 for second-order reactions [40,62,71,76]. It is necessary, however, for the observed reaction to have a half-life that is longer than the mixing time and dead time of the stopped-flow instrument, which limits the use of this method in the study of some very fast reactions [80].…”

Section: Stopped-flow Analysismentioning

confidence: 99%

Analytical methods for kinetic studies of biological interactions: A review

Zheng

Zhao

et al. 2015

Journal of Pharmaceutical and Biomedical Analysis

142

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The rates at which biological interactions occur can provide important information concerning the mechanism and behavior of these processes in living systems. This review discusses several analytical methods that can be used to examine the kinetics of biological interactions. These techniques include common or traditional methods such as stopped-flow analysis and surface plasmon resonance spectroscopy, as well as alternative methods based on affinity chromatography and capillary electrophoresis. The general principles and theory behind these approaches are examined, and it is shown how each technique can be utilized to provide information on the kinetics of biological interactions. Examples of applications are also given for each method. In addition, a discussion is provided on the relative advantages or potential limitations of each technique regarding its use in kinetic studies.

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Sphingosylphosphorylcholine alleviates hypoxia-caused apoptosis in cardiac myofibroblasts via CaM/p38/STAT3 pathway

Liu

Yang

et al. 2020

Apoptosis

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Dissociation of Calmodulin-Target Peptide Complexes by the Lipid Mediator Sphingosylphosphorylcholine

Cited by 20 publications

References 41 publications

Regulation of ryanodine receptors by sphingosylphosphorylcholine: Involvement of both calmodulin-dependent and -independent mechanisms

Regulation of ryanodine receptors by sphingosylphosphorylcholine: Involvement of both calmodulin-dependent and -independent mechanisms

Analytical methods for kinetic studies of biological interactions: A review

Sphingosylphosphorylcholine alleviates hypoxia-caused apoptosis in cardiac myofibroblasts via CaM/p38/STAT3 pathway

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