Characterization of calumenin in mouse heart

Sahoo, Sanjaya Kumar; Kim, Do Han

doi:10.5483/bmbrep.2010.43.3.158

Cited by 36 publications

(24 citation statements)

References 46 publications

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“…Calcium is a universal second messenger that plays important roles in various cellular processes, such as gene expression, signal transduction, and exocytosis (Sahoo and Kim do 2010).…”

Section: Other Proteinsmentioning

confidence: 99%

Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo

et al. 2011

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Toxoplasma gondii is an obligate intracellular protozoan parasite, which can invade and multiply within the macrophages of humans and most warm-blooded animals. Macrophages are important effector cells for the control and killing of intracellular T. gondii, and they may also serve as long-term host cells for the replication and survival of the parasite. In the present study, we explored the proteomic profile of macrophages of the specific pathogen-free Kunming mice at 24 h after infection with tachyzoites of the virulent T. gondii RH strain using two-dimensional gel electrophoresis combined with matrix-assisted laser desorption ionization time-of-flight (TOF)/TOF tandem mass spectrometry. Totally, 60 differentially expressed protein spots were identified. Among them, 52 spots corresponded to 38 proteins matching to proteins of the mouse, including actin, enolase, calumenin, vimentin, plastin 2, annexin A1, cathepsin S, arginase-1, arachidonate 12-lipoxygenase, and aminoacylase-1. Functional prediction using Gene Ontology database showed that these proteins were mainly involved in metabolism, structure, protein fate, and immune responses. The findings provided an insight into the interactive relationship between T. gondii and the host macrophages, and will shed new lights on the understanding of molecular mechanisms of T. gondii pathogenesis.

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“…Calcium is a universal second messenger that plays important roles in various cellular processes, such as gene expression, signal transduction, and exocytosis (Sahoo and Kim do 2010).…”

Section: Other Proteinsmentioning

confidence: 99%

Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo

et al. 2011

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“…Calumenin possibly also interacts directly with proteins involved in Ca 2+ homeostasis, in particular the Sarco(Endoplasmic)Reticulum Ca 2+ -ATPase (SERCA2a) [ 9 ] and the ryanodine receptor [ 10 ], thereby regulating their function. Calumenin can therefore be considered a key player in ER Ca 2+ homeostasis and given its high expression level in myocytes, it is likely to play a fundamental role in the control of muscle contraction/relaxation both in smooth muscle and in heart (reviewed in [ 11 ]).…”

Section: Introductionmentioning

confidence: 99%

Ca-Dependent Folding of Human Calumenin

2016

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Human calumenin (hCALU) is a six EF-hand protein belonging to the CREC family. As other members of the family, it is localized in the secretory pathway and regulates the activity of SERCA2a and of the ryanodine receptor in the endoplasmic reticulum (ER). We have studied the effects of Ca2+ binding to the protein and found it to attain a more compact structure upon ion binding. Circular Dichroism (CD) measurements suggest a major rearrangement of the protein secondary structure, which reversibly switches from disordered at low Ca2+ concentrations to predominantly alpha-helical when Ca2+ is added. SAXS experiments confirm the transition from an unfolded to a compact structure, which matches the structural prediction of a trilobal fold. Overall our experiments suggest that calumenin is a Ca2+ sensor, which folds into a compact structure, capable of interacting with its molecular partners, when Ca2+ concentration within the ER reaches the millimolar range.

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“…The functional properties are steadily emerging with links to malignant cell transformation [ 10 , 19 – 22 ] and stress responses [ 23 , 24 ]. A number of molecular functions have been described especially in connection with calumenin in the endoplasmic reticulum (ER) or sarcoplasmic reticulum (SR) [ 2 , 25 ]. Thus, calumenin interacts with the ryanodine receptor-1 possibly regulating its activity [ 26 ].…”

Section: Introductionmentioning

confidence: 99%

Fibulin-1C, C1 Esterase Inhibitor and Glucose Regulated Protein 75 Interact with the CREC Proteins, Calumenin and Reticulocalbin

et al. 2015

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Affinity purification, immunoprecipitation, gel electrophoresis and mass spectrometry were used to identify fibulin-1C, C1 esterase inhibitor and glucose regulated protein 75, grp75, as binding partners of the CREC proteins, calumenin and reticulocalbin. Surface plasmon resonance was used to verify the interaction of all three proteins with each of the CREC proteins. Fibulin-1C interacts with calumenin and reticulocalbin with an estimated dissociation constant around 50-60 nM. The interaction, at least for reticulocalbin, was not dependent upon the presence of Ca2+. C1 esterase inhibitor interacted with both proteins with an estimated dissociation constant at 1 μM for reticulocalbin and 150 nM for calumenin. The interaction, at least for calumenin, was dependent upon the presence of Ca2+ with strong interaction at 3.5 mM while no detectable interaction could be found at 0.1 mM. Grp75 binds with an affinity of approximately 3-7 nM with reticulocalbin as well as with calumenin. These interactions suggest functional participation of the CREC proteins in chaperone activity, cell proliferation and transformation, cellular aging, haemostasis and thrombosis as well as modulation of the complement system in fighting bacterial infection.

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Characterization of calumenin in mouse heart

Cited by 36 publications

References 46 publications

Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo

Modulation of mouse macrophage proteome induced by Toxoplasma gondii tachyzoites in vivo

Ca-Dependent Folding of Human Calumenin

Fibulin-1C, C1 Esterase Inhibitor and Glucose Regulated Protein 75 Interact with the CREC Proteins, Calumenin and Reticulocalbin

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