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Article: Optimal microscopic systems for long-term imaging of intracellular calcium using a ratiometric genetically-encoded calcium indicator

Miyamoto, Akitoshi / Bannai, Hiroko / Michikawa, Takayuki / Mikoshiba, Katsuhiko

Biochemical and biophysical research communications. 2013 May 3, v. 434, no. 2

2013

Abstract: Monitoring the pattern of intracellular Ca²⁺ signals that control many diverse cellular processes is essential for understanding regulatory mechanisms of cellular functions. Various genetically encoded Ca²⁺ indicators (GECIs) are used for monitoring ... ...

Abstract	Monitoring the pattern of intracellular Ca²⁺ signals that control many diverse cellular processes is essential for understanding regulatory mechanisms of cellular functions. Various genetically encoded Ca²⁺ indicators (GECIs) are used for monitoring intracellular Ca²⁺ changes under several types of microscope systems. However, it has not yet been explored which microscopic system is ideal for long-term imaging of the spatiotemporal patterns of Ca²⁺ signals using GECIs. We here compared the Ca²⁺ signals reported by a fluorescence resonance energy transfer (FRET)-based ratiometric GECI, yellow cameleon 3.60 (YC3.60), stably expressed in DT40 B lymphocytes, using three different imaging systems. These systems included a wide-field fluorescent microscope, a multipoint scanning confocal system, and a single-point scanning confocal system. The degree of photobleaching and the signal-to-noise ratio of YC3.60 in DT40 cells were highly dependent on the fluorescence excitation method, although the total illumination energy was maintained at a constant level within each of the imaging systems. More strikingly, the Ca²⁺ responses evoked by B-cell antigen receptor stimulation in YC3.60-expressing DT40 cells were different among the imaging systems, and markedly affected by the illumination power used. Our results suggest that optimization of the imaging system, including illumination and acquisition conditions, is crucial for accurate visualization of intracellular Ca²⁺ signals.
Keywords	B-lymphocytes ; antigens ; calcium ; calcium signaling ; energy transfer ; fluorescence ; image analysis ; lighting ; monitoring ; photobleaching
Language	English
Dates of publication	2013-0503
Size	p. 252-257.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2013.02.112
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Article ; Online: Distributed sensory coding by cerebellar complex spikes in units of cortical segments.

Michikawa, Takayuki / Yoshida, Takamasa / Kuroki, Satoshi / Ishikawa, Takahiro / Kakei, Shinji / Kimizuka, Ryo / Saito, Atsushi / Yokota, Hideo / Shimizu, Akinobu / Itohara, Shigeyoshi / Miyawaki, Atsushi

Cell reports

2021 Volume 37, Issue 6, Page(s) 109966

Abstract: Sensory processing is essential for motor control. Climbing fibers from the inferior olive transmit sensory signals to Purkinje cells, but how the signals are represented in the cerebellar cortex remains elusive. To examine the olivocerebellar ... ...

Abstract	Sensory processing is essential for motor control. Climbing fibers from the inferior olive transmit sensory signals to Purkinje cells, but how the signals are represented in the cerebellar cortex remains elusive. To examine the olivocerebellar organization of the mouse brain, we perform quantitative Ca
MeSH term(s)	Action Potentials ; Animals ; Bayes Theorem ; Calcium/metabolism ; Cerebellum/cytology ; Cerebellum/physiology ; Female ; Male ; Mice ; Mice, Inbred ICR ; Nerve Net/cytology ; Nerve Net/physiology ; Olivary Nucleus/cytology ; Olivary Nucleus/physiology ; Purkinje Cells/cytology ; Purkinje Cells/physiology ; Sense Organs/cytology ; Sense Organs/physiology
Chemical Substances	Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-11-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.109966
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Article ; Online: Dual-FRET imaging of IP

Matsu-Ura, Toru / Shirakawa, Hideki / Suzuki, Kenichi G N / Miyamoto, Akitoshi / Sugiura, Kotomi / Michikawa, Takayuki / Kusumi, Akihiro / Mikoshiba, Katsuhiko

Scientific reports

2019 Volume 9, Issue 1, Page(s) 4829

Abstract: In most species, fertilization induces ... ...

Abstract	In most species, fertilization induces Ca
MeSH term(s)	Animals ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Calcium/metabolism ; Calcium Signaling/physiology ; Cations, Divalent/metabolism ; Female ; Fertilization/physiology ; Fluorescence Resonance Energy Transfer ; Fluorescent Dyes/chemistry ; Genes, Reporter/genetics ; HeLa Cells ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Intravital Microscopy ; Luminescent Proteins/chemistry ; Luminescent Proteins/genetics ; Male ; Mice ; Microinjections ; Microscopy, Fluorescence ; Sf9 Cells ; Sperm Injections, Intracytoplasmic ; Spodoptera ; Type C Phospholipases/metabolism ; Zygote/metabolism
Chemical Substances	Bacterial Proteins ; Cations, Divalent ; Fluorescent Dyes ; Luminescent Proteins ; yellow fluorescent protein, Bacteria ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; Type C Phospholipases (EC 3.1.4.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2019-03-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-40931-w
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Article ; Online: Optimal microscopic systems for long-term imaging of intracellular calcium using a ratiometric genetically-encoded calcium indicator.

Miyamoto, Akitoshi / Bannai, Hiroko / Michikawa, Takayuki / Mikoshiba, Katsuhiko

Biochemical and biophysical research communications

2013 Volume 434, Issue 2, Page(s) 252–257

Abstract: Monitoring the pattern of intracellular Ca(2+) signals that control many diverse cellular processes is essential for understanding regulatory mechanisms of cellular functions. Various genetically encoded Ca(2+) indicators (GECIs) are used for monitoring ... ...

Abstract	Monitoring the pattern of intracellular Ca(2+) signals that control many diverse cellular processes is essential for understanding regulatory mechanisms of cellular functions. Various genetically encoded Ca(2+) indicators (GECIs) are used for monitoring intracellular Ca(2+) changes under several types of microscope systems. However, it has not yet been explored which microscopic system is ideal for long-term imaging of the spatiotemporal patterns of Ca(2+) signals using GECIs. We here compared the Ca(2+) signals reported by a fluorescence resonance energy transfer (FRET)-based ratiometric GECI, yellow cameleon 3.60 (YC3.60), stably expressed in DT40 B lymphocytes, using three different imaging systems. These systems included a wide-field fluorescent microscope, a multipoint scanning confocal system, and a single-point scanning confocal system. The degree of photobleaching and the signal-to-noise ratio of YC3.60 in DT40 cells were highly dependent on the fluorescence excitation method, although the total illumination energy was maintained at a constant level within each of the imaging systems. More strikingly, the Ca(2+) responses evoked by B-cell antigen receptor stimulation in YC3.60-expressing DT40 cells were different among the imaging systems, and markedly affected by the illumination power used. Our results suggest that optimization of the imaging system, including illumination and acquisition conditions, is crucial for accurate visualization of intracellular Ca(2+) signals.
MeSH term(s)	Animals ; Calcium/metabolism ; Calcium Signaling ; Calcium-Binding Proteins/metabolism ; Cell Line, Tumor ; Fluorescence Resonance Energy Transfer ; Fluorescent Dyes/metabolism ; Image Processing, Computer-Assisted/methods ; Indicators and Reagents/metabolism ; Lymphocytes/metabolism ; Microscopy, Confocal/methods ; Microscopy, Fluorescence/methods ; Photobleaching ; Receptors, Antigen, B-Cell/metabolism ; Reproducibility of Results ; Signal-To-Noise Ratio ; Time Factors
Chemical Substances	Calcium-Binding Proteins ; Fluorescent Dyes ; Indicators and Reagents ; Receptors, Antigen, B-Cell ; yellow cameleon ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-05-03
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2013.02.112
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Article: Apoptosis induction-related cytosolic calcium responses revealed by the dual FRET imaging of calcium signals and caspase-3 activation in a single cell

Miyamoto, Akitoshi / Miyauchi, Hiroshi / Kogure, Takako / Miyawaki, Atsushi / Michikawa, Takayuki / Mikoshiba, Katsuhiko

Biochemical and biophysical research communications. 2015 Apr. 24, v. 460

2015

Abstract: Stimulus-induced changes in the intracellular Ca2+ concentration control cell fate decision, including apoptosis. However, the precise patterns of the cytosolic Ca2+ signals that are associated with apoptotic induction remain unknown. We have developed a ...

Abstract	Stimulus-induced changes in the intracellular Ca2+ concentration control cell fate decision, including apoptosis. However, the precise patterns of the cytosolic Ca2+ signals that are associated with apoptotic induction remain unknown. We have developed a novel genetically encoded sensor of activated caspase-3 that can be applied in combination with a genetically encoded sensor of the Ca2+ concentration and have established a dual imaging system that enables the imaging of both cytosolic Ca2+ signals and caspase-3 activation, which is an indicator of apoptosis, in the same cell. Using this system, we identified differences in the cytosolic Ca2+ signals of apoptotic and surviving DT40 B lymphocytes after B cell receptor (BCR) stimulation. In surviving cells, BCR stimulation evoked larger initial Ca2+ spikes followed by a larger sustained elevation of the Ca2+ concentration than those in apoptotic cells; BCR stimulation also resulted in repetitive transient Ca2+ spikes, which were mediated by the influx of Ca2+ from the extracellular space. Our results indicate that the observation of both Ca2+ signals and cells fate in same cell is crucial to gain an accurate understanding of the function of intracellular Ca2+ signals in apoptotic induction.
Keywords	B-lymphocytes ; apoptosis ; calcium ; calcium signaling ; caspase-3 ; extracellular space ; image analysis
Language	English
Dates of publication	2015-0424
Size	p. 82-87.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2015.02.045
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Article ; Online: Excitatory Neuronal Hubs Configure Multisensory Integration of Slow Waves in Association Cortex.

Kuroki, Satoshi / Yoshida, Takamasa / Tsutsui, Hidekazu / Iwama, Mizuho / Ando, Reiko / Michikawa, Takayuki / Miyawaki, Atsushi / Ohshima, Toshio / Itohara, Shigeyoshi

Cell reports

2018 Volume 22, Issue 11, Page(s) 2873–2885

Abstract: Multisensory integration (MSI) is a fundamental emergent property of the mammalian brain. During MSI, perceptual information encoded in patterned activity is processed in multimodal association cortex. The systems-level neuronal dynamics that coordinate ... ...

Abstract	Multisensory integration (MSI) is a fundamental emergent property of the mammalian brain. During MSI, perceptual information encoded in patterned activity is processed in multimodal association cortex. The systems-level neuronal dynamics that coordinate MSI, however, are unknown. Here, we demonstrate intrinsic hub-like network activity in the association cortex that regulates MSI. We engineered calcium reporter mouse lines based on the fluorescence resonance energy transfer sensor yellow cameleon (YC2.60) expressed in excitatory or inhibitory neurons. In medial and parietal association cortex, we observed spontaneous slow waves that self-organized into hubs defined by long-range excitatory and local inhibitory circuits. Unlike directional source/sink-like flows in sensory areas, medial/parietal excitatory and inhibitory hubs had net-zero balanced inputs. Remarkably, multisensory stimulation triggered rapid phase-locking mainly of excitatory hub activity persisting for seconds after the stimulus offset. Therefore, association cortex tends to form balanced excitatory networks that configure slow-wave phase-locking for MSI. VIDEO ABSTRACT.
MeSH term(s)	Animals ; Cerebral Cortex/cytology ; Cerebral Cortex/physiology ; Mice ; Neurons/physiology
Language	English
Publishing date	2018-03-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.02.056
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Article ; Online: Apoptosis induction-related cytosolic calcium responses revealed by the dual FRET imaging of calcium signals and caspase-3 activation in a single cell.

Miyamoto, Akitoshi / Miyauchi, Hiroshi / Kogure, Takako / Miyawaki, Atsushi / Michikawa, Takayuki / Mikoshiba, Katsuhiko

Biochemical and biophysical research communications

2015 Volume 460, Issue 1, Page(s) 82–87

Abstract: Stimulus-induced changes in the intracellular Ca(2+) concentration control cell fate decision, including apoptosis. However, the precise patterns of the cytosolic Ca(2+) signals that are associated with apoptotic induction remain unknown. We have ... ...

Abstract	Stimulus-induced changes in the intracellular Ca(2+) concentration control cell fate decision, including apoptosis. However, the precise patterns of the cytosolic Ca(2+) signals that are associated with apoptotic induction remain unknown. We have developed a novel genetically encoded sensor of activated caspase-3 that can be applied in combination with a genetically encoded sensor of the Ca(2+) concentration and have established a dual imaging system that enables the imaging of both cytosolic Ca(2+) signals and caspase-3 activation, which is an indicator of apoptosis, in the same cell. Using this system, we identified differences in the cytosolic Ca(2+) signals of apoptotic and surviving DT40 B lymphocytes after B cell receptor (BCR) stimulation. In surviving cells, BCR stimulation evoked larger initial Ca(2+) spikes followed by a larger sustained elevation of the Ca(2+) concentration than those in apoptotic cells; BCR stimulation also resulted in repetitive transient Ca(2+) spikes, which were mediated by the influx of Ca(2+) from the extracellular space. Our results indicate that the observation of both Ca(2+) signals and cells fate in same cell is crucial to gain an accurate understanding of the function of intracellular Ca(2+) signals in apoptotic induction.
MeSH term(s)	Animals ; Apoptosis/physiology ; Apoptosis Regulatory Proteins/metabolism ; Calcium/metabolism ; Calcium Signaling/physiology ; Caspase 3/metabolism ; Cell Line ; Chickens ; Cytoplasm/metabolism ; Fluorescence Resonance Energy Transfer/methods ; Microscopy, Fluorescence, Multiphoton/methods
Chemical Substances	Apoptosis Regulatory Proteins ; Caspase 3 (EC 3.4.22.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2015-04-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2015.02.045
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Article ; Online: Phospholipase C-β1 and β4 contribute to non-genetic cell-to-cell variability in histamine-induced calcium signals in HeLa cells.

Ishida, Sachiko / Matsu-Ura, Toru / Fukami, Kiyoko / Michikawa, Takayuki / Mikoshiba, Katsuhiko

PloS one

2014 Volume 9, Issue 1, Page(s) e86410

Abstract: A uniform extracellular stimulus triggers cell-specific patterns of Ca(2+) signals, even in genetically identical cell populations. However, the underlying mechanism that generates the cell-to-cell variability remains unknown. We monitored cytosolic ... ...

Abstract	A uniform extracellular stimulus triggers cell-specific patterns of Ca(2+) signals, even in genetically identical cell populations. However, the underlying mechanism that generates the cell-to-cell variability remains unknown. We monitored cytosolic inositol 1,4,5-trisphosphate (IP3) concentration changes using a fluorescent IP3 sensor in single HeLa cells showing different patterns of histamine-induced Ca(2+) oscillations in terms of the time constant of Ca(2+) spike amplitude decay and the Ca(2+) oscillation frequency. HeLa cells stimulated with histamine exhibited a considerable variation in the temporal pattern of Ca(2+) signals and we found that there were cell-specific IP3 dynamics depending on the patterns of Ca(2+) signals. RT-PCR and western blot analyses showed that phospholipase C (PLC)-β1, -β3, -β4, -γ1, -δ3 and -ε were expressed at relatively high levels in HeLa cells. Small interfering RNA-mediated silencing of PLC isozymes revealed that PLC-β1 and PLC-β4 were specifically involved in the histamine-induced IP3 increases in HeLa cells. Modulation of IP3 dynamics by knockdown or overexpression of the isozymes PLC-β1 and PLC-β4 resulted in specific changes in the characteristics of Ca(2+) oscillations, such as the time constant of the temporal changes in the Ca(2+) spike amplitude and the Ca(2+) oscillation frequency, within the range of the cell-to-cell variability found in wild-type cell populations. These findings indicate that the heterogeneity in the process of IP3 production, rather than IP3-induced Ca(2+) release, can cause cell-to-cell variability in the patterns of Ca(2+) signals and that PLC-β1 and PLC-β4 contribute to generate cell-specific Ca(2+) signals evoked by G protein-coupled receptor stimulation.
MeSH term(s)	Blotting, Western ; Calcium Signaling/drug effects ; Calcium Signaling/physiology ; Cytosol/metabolism ; DNA Primers/genetics ; HeLa Cells ; Histamine/metabolism ; Histamine/pharmacology ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Isoenzymes/metabolism ; Phospholipase C beta/metabolism ; RNA Interference ; RNA, Small Interfering/genetics ; Receptors, G-Protein-Coupled/metabolism ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	DNA Primers ; Isoenzymes ; RNA, Small Interfering ; Receptors, G-Protein-Coupled ; Histamine (820484N8I3) ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; Phospholipase C beta (EC 3.1.4.11)
Language	English
Publishing date	2014-01-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0086410
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Article ; Online: Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening.

Yamazaki, Haruka / Chan, Jenny / Ikura, Mitsuhiko / Michikawa, Takayuki / Mikoshiba, Katsuhiko

The Journal of biological chemistry

2010 Volume 285, Issue 46, Page(s) 36081–36091

Abstract: The N-terminal ∼220-amino acid region of the inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R)/Ca(2+) release channel has been referred to as the suppressor/coupling domain because it is required for both IP(3) binding suppression and IP(3)-induced ... ...

Abstract	The N-terminal ∼220-amino acid region of the inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R)/Ca(2+) release channel has been referred to as the suppressor/coupling domain because it is required for both IP(3) binding suppression and IP(3)-induced channel gating. Measurements of IP(3)-induced Ca(2+) fluxes of mutagenized mouse type 1 IP(3)R (IP(3)R1) showed that the residues responsible for IP(3) binding suppression in this domain were not essential for channel opening. On the other hand, a single amino acid substitution of Tyr-167 to alanine completely impaired IP(3)-induced Ca(2+) release without reducing the IP(3) binding activity. The corresponding residue in type 3 IP(3)R (IP(3)R3), Trp-168, was also critical for channel opening. Limited trypsin digestion experiments showed that the trypsin sensitivities of the C-terminal gatekeeper domain differed markedly between the wild-type channel and the Tyr-167 mutant under the optimal conditions for channel opening. These results strongly suggest that the Tyr/Trp residue (Tyr-167 in IP(3)R1 and Trp-168 in IP(3)R3) is critical for the functional coupling between IP(3) binding and channel gating by maintaining the structural integrity of the C-terminal gatekeeper domain at least under activation gating.
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites/genetics ; Blotting, Western ; Calcium/metabolism ; Cell Line, Tumor ; Inositol 1,4,5-Trisphosphate/chemistry ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol 1,4,5-Trisphosphate/pharmacology ; Inositol 1,4,5-Trisphosphate Receptors/chemistry ; Inositol 1,4,5-Trisphosphate Receptors/genetics ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Ion Channel Gating/drug effects ; Ion Channel Gating/genetics ; Ion Channel Gating/physiology ; Ligands ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Protein Binding ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Trypsin/metabolism ; Tryptophan/chemistry ; Tryptophan/genetics ; Tryptophan/metabolism ; Tyrosine/chemistry ; Tyrosine/genetics ; Tyrosine/metabolism
Chemical Substances	Inositol 1,4,5-Trisphosphate Receptors ; Ligands ; Protein Isoforms ; Tyrosine (42HK56048U) ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; Tryptophan (8DUH1N11BX) ; Trypsin (EC 3.4.21.4) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2010-09-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M110.140129
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Article: Functional characterization of the P1059L mutation in the inositol 1,4,5-trisphosphate receptor type 1 identified in a Japanese SCA15 family

Yamazaki, Haruka / Nozaki, Hiroaki / Onodera, Osamu / Michikawa, Takayuki / Nishizawa, Masatoyo / Mikoshiba, Katsuhiko

Biochemical and biophysical research communications. 2011 July 15, v. 410, no. 4

2011

Abstract: Spinocerebellar ataxia type 15 (SCA15) is a group of human neurodegenerative disorders characterized by a slowly progressing pure cerebellar ataxia. The inositol 1,4,5-trisphosphate (IP₃) receptor type 1 (IP₃R1) is an intracellular IP₃-induced Ca²⁺ ... ...

Abstract	Spinocerebellar ataxia type 15 (SCA15) is a group of human neurodegenerative disorders characterized by a slowly progressing pure cerebellar ataxia. The inositol 1,4,5-trisphosphate (IP₃) receptor type 1 (IP₃R1) is an intracellular IP₃-induced Ca²⁺ release channel that was recently identified as a causative gene for SCA15. In most case studies, a heterozygous deletion of the IP₃R1 gene was identified. However, one Japanese SCA15 family was found to have a Pro to Leu (P1059L) substitution in IP₃R1. To investigate the effect of the P1059L mutation, we analyzed the channel properties of the mutant human IP₃R1 by expressing it in an IP₃R-deficient B lymphocyte cell line. The P1059L mutant was a functional Ca²⁺ release channel with a twofold higher IP₃ binding affinity compared to wild-type IP₃R1. The cooperative dependence of the Ca²⁺ release activity of the mutant on IP₃ concentration was reduced, but both wild-type and mutant receptors produced similar B cell receptor-induced Ca²⁺ signals. These results demonstrate that the Ca²⁺ release properties of IP₃R1 are largely unaffected by the P1059L mutation.
Keywords	B-lymphocytes ; ataxia (disorder) ; binding capacity ; calcium ; calcium signaling ; case studies ; genes ; heterozygosity ; humans ; mutants ; mutation ; myo-inositol ; neurodegenerative diseases ; receptors
Language	English
Dates of publication	2011-0715
Size	p. 754-758.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2011.06.043
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