Molecular Cloning of Human Calmitine, a Mitochondrial Calcium Binding Protein, Reveals Identity with Calsequestrine

Bataillé, Nelly; Schmitt, Nelly; Aumercier-Maes, Pierrette; Ollivier, Béatrice; Lucas-Heron, Brigitte; Lestienne, Patrick

doi:10.1006/bbrc.1994.2351

Cited by 9 publications

(6 citation statements)

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“…Sodium (Na) and potassium (K) contribute to osmotic and bioenergetic balance. Calcium is sequestered in mitochondria and participates in cellular calcium signaling; calcium is also a required cofactor in several mitochondrial proteins, including several dehydrogenases and calsequestrin 1 (Nicholls and Scott, 1980;McCormack et al, 1990;Bataille et al, 1994;Brown et al, 1995;Gunter and Gunter, 2001). Several other metals like molybdenum (Mo) and vanadium (V) have been detected in mitochondria, but their functions and specific binding proteins have yet to be identified (Peisach et al, 1971;Sharma et al, 1980).…”

Section: Metals Necessary For Mitochondria Not Used Directly In the Hmentioning

confidence: 99%

Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging

Ames¹,

Atamna²,

Killilea³

2005

Molecular Aspects of Medicine

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Section: Metals Necessary For Mitochondria Not Used Directly In the Hmentioning

confidence: 99%

Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging

Ames¹,

Atamna²,

Killilea³

2005

Molecular Aspects of Medicine

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“…2). These observations, clearly showing that calsequestrin and calmitine, despite certain similarities [2], are not dependent on the same protease, suggest that each has a distinct specificity in addition to a different localization. It may be noted that in all cases Ca 45 binding to specific proteins (Fig.…”

Section: Resultsmentioning

confidence: 78%

“…Calmitine, a mitochondrial calcium-binding protein specific for fast skeletal muscle [1], shows some similarities with calsequestrin [2]. The fact that it has recently been localized more specifically in the mitochondrial matrix [2] suggests that it plays a primordial role in the regulation of mitochondrial bound and free calcium [3] and thus in the cellular functioning and particularly the synthesis of ATE There is increasing evidence that mitochondrial calcium, which influences the activity of various matrical enzymes involved in oxidative phosphorylation and the production of cellular energy, plays a second messenger role triggering mitochondrial response to cytosolic signals [4].…”

Section: Introductionmentioning

confidence: 99%

“…The fact that it has recently been localized more specifically in the mitochondrial matrix [2] suggests that it plays a primordial role in the regulation of mitochondrial bound and free calcium [3] and thus in the cellular functioning and particularly the synthesis of ATE There is increasing evidence that mitochondrial calcium, which influences the activity of various matrical enzymes involved in oxidative phosphorylation and the production of cellular energy, plays a second messenger role triggering mitochondrial response to cytosolic signals [4]. For example, at the time of muscle contraction, when the need for ATP is very great, the concentration of cytosolic calcium (released by sarcoplasmic reticulum) increases, producing an augmentation of mitochondrial calcium serving to stimulate the activity of certain matrical enzymes (dehydrogenases [5 7], ATP synthase [8]) responsible for ATP production.…”

Section: Introductionmentioning

confidence: 99%

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Does calmitine, a protein specific for the mitochondrial matrix of skeletal muscle, play a key role in mitochondrial function?

1995

FEBS Letters

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The effect of the myotoxic drug chlorpromazine was studied in vitro on proteins of sarcoplasmic reticulum and mitochondrial matrix of skeletal muscle in the normal mouse. Our results indicate that the drug is specific for calcium-binding proteins (calcium ATPase, calsequestrin and calmitine). Its proteolytic effect on these proteins, apparently due to the stimulation of specific proteases, could account for its myotoxic action. Moreover, calsequestrin (sarcoplasmic reticulum) and calmitine (mitoehondrial matrix) were not sensitive to the same proteases. Proteases acting on caimitine were inhibited by a2-macroglobulin but not those acting on calsequestrin. Despite some similarities between these two proteins, their characteristics of localization and sensitivity of their proteases indicate that calmitine has a specificity within the mitochondrial matrix and very probably plays a major role in the mitochondrial regulation of free calcium, which controls the activity of various enzymes of the mitochondrial matrix involved in ATP synthesis.Key words: Calmitine; Mitochondrial matrix; Skeletal muscle calcium in response to cellular demand. This could account in part for muscle degeneration in patients with Duchenne's or Becker's muscular dystrophy and in dy/dy mice for which a large calmitine deficit has been observed [9]. Moreover, an experimental calmitine deficit, associated with increased mitochondrial free calcium and muscle degeneration, has been obtained in the normal mouse after a single injection of the myotoxic drug chlorpromazine [10]. According to data in the literature, this drug has an affinity for calcium-binding proteins [11,12] and could act more specifically at the mitochondrial level [13]. We studied the effect of chlorpromazine in vitro on subcellular fractions (sarcoplasmic reticulum and mitochondrial matrix) to determine whether the proteolytic action observed in vivo on calmitine was the same for other calciumbound proteins (calcium ATPase and calsequestrin) or whether calmitine in fact showed particularities differentiating it from calsequestrin and according it a role and a very specific function within the mitochondrial matrix.

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“…Among these genes, we find CALM, the gene encoding for calmodulin, a key regulator of transcription, memory and neuronal survival, PKC, as well as GLUR5 (i.e. : GRIK1) that encodes for a kainate receptor subunit, CASQ encoding for calsequestrin, a mitochondrial calcium-binding protein [16], CREB encoding for the Cyclic AMP Response Element Binding, a key transcriptor factor involved in neuronal plasticity and LTP. We also find CBP that encodes for the CREB-binding protein and is a co-activator interacting with CREB, thereby reinforcing the modulation of LTP.…”

Section: Resultsmentioning

confidence: 99%

Microarray Analysis on Human Neuroblastoma Cells Exposed to Aluminum, β1–42-Amyloid or the β1–42-Amyloid Aluminum Complex

Gatta

Drago

Fincati³

et al. 2011

PLoS ONE

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BackgroundA typical pathological feature of Alzheimer's disease (AD) is the appearance in the brain of senile plaques made up of β-amyloid (Aβ) and neurofibrillary tangles. AD is also associated with an abnormal accumulation of some metal ions, and we have recently shown that one of these, aluminum (Al), plays a relevant role in affecting Aβ aggregation and neurotoxicity.MethodologyIn this study, employing a microarray analysis of 35,129 genes, we investigated the effects induced by the exposure to the Aβ1–42-Al (Aβ-Al) complex on the gene expression profile of the neuronal-like cell line, SH-SY5Y.Principal FindingsThe microarray assay indicated that, compared to Aβ or Al alone, exposure to Aβ-Al complex produced selective changes in gene expression. Some of the genes selectively over or underexpressed are directly related to AD. A further evaluation performed with Ingenuity Pathway analysis revealed that these genes are nodes of networks and pathways that are involved in the modulation of Ca2+ homeostasis as well as in the regulation of glutamatergic transmission and synaptic plasticity.Conclusions and SignificanceAβ-Al appears to be largely involved in the molecular machinery that regulates neuronal as well as synaptic dysfunction and loss. Aβ-Al seems critical in modulating key AD-related pathways such as glutamatergic transmission, Ca2+ homeostasis, oxidative stress, inflammation, and neuronal apoptosis.

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Molecular Cloning of Human Calmitine, a Mitochondrial Calcium Binding Protein, Reveals Identity with Calsequestrine

Cited by 9 publications

References 0 publications

Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging

Mineral and vitamin deficiencies can accelerate the mitochondrial decay of aging

Does calmitine, a protein specific for the mitochondrial matrix of skeletal muscle, play a key role in mitochondrial function?

Microarray Analysis on Human Neuroblastoma Cells Exposed to Aluminum, β1–42-Amyloid or the β1–42-Amyloid Aluminum Complex

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