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Article: Social Stress-Induced Postsynaptic Hyporesponsiveness in Glutamatergic Synapses Is Mediated by PSD-Zip70-Rap2 Pathway and Relates to Anxiety-Like Behaviors.

Mayanagi, Taira / Sobue, Kenji

2020 Volume 13, Page(s) 564

Abstract: PSD-Zip70 is a postsynaptic protein that regulates glutamatergic synapse formation and maturation by modulation of Rap2 activity. PSD-Zip70 knockout (PSD-Zip70KO) mice exhibit defective glutamatergic synaptic transmission in the prefrontal cortex (PFC) ... ...

Abstract	PSD-Zip70 is a postsynaptic protein that regulates glutamatergic synapse formation and maturation by modulation of Rap2 activity. PSD-Zip70 knockout (PSD-Zip70KO) mice exhibit defective glutamatergic synaptic transmission in the prefrontal cortex (PFC) with aberrant Rap2 activation. As prefrontal dysfunction is implicated in the pathophysiology of stress-induced psychiatric diseases, we examined PSD-Zip70KO mice in a social defeat (SD) stress-induced mouse model of depression to investigate stress-induced alterations in synaptic function. Compared with wild-type (WT) mice, PSD-Zip70KO mice exhibited almost normal responses to SD stress in depression-related behaviors such as social activity, anhedonia, and depressive behavior. However, PSD-Zip70KO mice showed enhanced anxiety-like behavior irrespective of stress conditions. The density and size of dendritic spines of pyramidal neurons were reduced in the medial PFC (mPFC) in mice exposed to SD stress. Phosphorylation levels of the AMPA-type glutamate receptor (AMPA-R) GluA2 subunit at Ser880 were prominently elevated in mice exposed to SD stress, indicating internalization of surface-expressed AMPA-Rs and decreased postsynaptic responsiveness. Structural and functional impairments in postsynaptic responsiveness were associated with Rap2 GTPase activation in response to SD stress. Social stress-induced Rap2 activation was regulated by a PSD-Zip70-dependent pathway via interaction with SPAR/PDZ-GEF1. Notably, features such as Rap2 activation, dendritic spine shrinkage, and increased GluA2 phosphorylation were observed in the mPFC of PSD-Zip70KO mice even without SD stress. Together with our previous results, the present findings suggest that SD stress-induced postsynaptic hyporesponsiveness in glutamatergic synapses is mediated by PSD-Zip70-Rap2 signaling pathway and closely relates to anxiety-like behaviors.
Language	English
Publishing date	2020-01-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452963-1
ISSN	1662-5102
ISSN	1662-5102
DOI	10.3389/fncel.2019.00564
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Article ; Online: NLRP3 Inflammasome Inhibitor OLT1177 Suppresses Onset of Inflammation in Mice with Dextran Sulfate Sodium-Induced Colitis.

Oizumi, Tomofumi / Mayanagi, Taira / Toya, Yosuke / Sugai, Tamotsu / Matsumoto, Takayuki / Sobue, Kenji

Digestive diseases and sciences

2021 Volume 67, Issue 7, Page(s) 2912–2921

Abstract: Background and aims: NLRP3 inflammasomes have been reported to have a key role in the initiation and perpetuation of inflammatory bowel diseases (IBD). Here we investigated the effects of OLT1177, a selective inhibitor of NLRP3 inflammasomes, in mice ... ...

Abstract	Background and aims: NLRP3 inflammasomes have been reported to have a key role in the initiation and perpetuation of inflammatory bowel diseases (IBD). Here we investigated the effects of OLT1177, a selective inhibitor of NLRP3 inflammasomes, in mice with dextran sulfate sodium (DSS)-induced colitis. Methods: C57BL/6J mice were given drinking water containing 3% DSS for 5 days. OLT1177 was administered for 5 days during the induction phase (simultaneously with DSS treatment) or the recovery phase (after the DSS treatment ended). The body weight and disease activity index were monitored daily. The mice were sacrificed 10 days after the start of the experiment, and the severity of inflammation in the colon was determined based on histological and biochemical analyses. Results: Administration of OLT1177 during the induction phase effectively suppressed DSS colitis in terms of weight loss, disease activity index, histological score, and expression of inflammatory cytokines compared to the DSS group. In contrast, OLT1177 administration during the recovery phase did not significantly affect the colitis disease course or the results of histological analyses. Conclusions: OLT1177 was effective in preventing the onset of DSS colitis in mice. These results could guide the use of OLT1177 as a therapy for human IBD.
MeSH term(s)	Animals ; Colitis/chemically induced ; Colitis/drug therapy ; Colitis/prevention & control ; Colon/pathology ; Dextran Sulfate/toxicity ; Disease Models, Animal ; Humans ; Inflammasomes/metabolism ; Inflammation/metabolism ; Inflammatory Bowel Diseases/metabolism ; Mice ; Mice, Inbred C57BL ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Nitriles ; Sulfones
Chemical Substances	Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nitriles ; Nlrp3 protein, mouse ; Sulfones ; dapansutrile (2Z03364G96) ; Dextran Sulfate (9042-14-2)
Language	English
Publishing date	2021-08-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	304250-9
ISSN	1573-2568 ; 0163-2116
ISSN (online)	1573-2568
ISSN	0163-2116
DOI	10.1007/s10620-021-07184-y
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Suzuki, Takashi / Nakamura, Kazuyoshi / Mayanagi, Taira / Sobue, Kenji / Kubokawa, Manabu

Biochemical and biophysical research communications

2017 Volume 489, Issue 2, Page(s) 116–122

Abstract: The ROMK1 ... ...

Abstract	The ROMK1 K
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Cells, Cultured ; Kidney Tubules, Collecting/cytology ; Mice ; Phosphoproteins/metabolism ; Potassium Channels, Inwardly Rectifying/genetics ; Potassium Channels, Inwardly Rectifying/metabolism ; Sodium-Hydrogen Exchangers/metabolism
Chemical Substances	Kcnj1 protein, mouse ; Phosphoproteins ; Potassium Channels, Inwardly Rectifying ; Sodium-Hydrogen Exchangers ; sodium-hydrogen exchanger regulatory factor
Language	English
Publishing date	2017-07-22
Publishing country	United States
Document type	Journal Article
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.2017.05.104
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Article ; Online: PSD-Zip70 Deficiency Causes Prefrontal Hypofunction Associated with Glutamatergic Synapse Maturation Defects by Dysregulation of Rap2 Activity.

Mayanagi, Taira / Yasuda, Hiroki / Sobue, Kenji

The Journal of neuroscience : the official journal of the Society for Neuroscience

2015 Volume 35, Issue 42, Page(s) 14327–14340

Abstract: Dysregulation of synapse formation and plasticity is closely related to the pathophysiology of psychiatric and neurodevelopmental disorders. The prefrontal cortex (PFC) is particularly important for executive functions such as working memory, cognition, ... ...

Abstract	Dysregulation of synapse formation and plasticity is closely related to the pathophysiology of psychiatric and neurodevelopmental disorders. The prefrontal cortex (PFC) is particularly important for executive functions such as working memory, cognition, and emotional control, which are impaired in the disorders. PSD-Zip70 (Lzts1/FEZ1) is a postsynaptic density (PSD) protein predominantly expressed in the frontal cortex, olfactory bulb, striatum, and hippocampus. Here we found that PSD-Zip70 knock-out (PSD-Zip70KO) mice exhibit working memory and cognitive defects, and enhanced anxiety-like behaviors. These abnormal behaviors are caused by impaired glutamatergic synapse transmission accompanied by tiny-headed immature dendritic spines in the PFC, due to aberrant Rap2 activation, which has roles in synapse formation and plasticity. PSD-Zip70 modulates the Rap2 activity by interacting with SPAR (spine-associated RapGAP) and PDZ-GEF1 (RapGEF) in the postsynapse. Furthermore, suppression of the aberrant Rap2 activation in the PFC rescued the behavioral defects in PSD-Zip70KO mice. Our data demonstrate a critical role for PSD-Zip70 in Rap2-dependent spine synapse development in the PFC and underscore the importance of this regulation in PFC-dependent behaviors. Significance statement: PSD-Zip70 deficiency causes behavioral defects in working memory and cognition, and enhanced anxiety due to prefrontal hypofunction. This study revealed that PSD-Zip70 plays essential roles in glutamatergic synapse maturation via modulation of the Rap2 activity in the PFC. PSD-Zip70 interacts with both SPAR (spine-associated RapGAP) and PDZ-GEF1 (RapGEF) and modulates the Rap2 activity in postsynaptic sites. Our results provide a novel Rap2-specific regulatory mechanism in synaptic maturation involving PSD-Zip70.
MeSH term(s)	Animals ; Cells, Cultured ; Cognition Disorders/genetics ; Disease Models, Animal ; Embryo, Mammalian ; Excitatory Postsynaptic Potentials/drug effects ; Excitatory Postsynaptic Potentials/genetics ; Glutamic Acid/metabolism ; Humans ; In Vitro Techniques ; Maze Learning/physiology ; Memory Disorders/genetics ; Memory, Short-Term/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Prefrontal Cortex/metabolism ; Prefrontal Cortex/pathology ; Recognition, Psychology/physiology ; Synapses/pathology ; Tumor Suppressor Proteins/deficiency ; Tumor Suppressor Proteins/genetics ; rap GTP-Binding Proteins/metabolism
Chemical Substances	Lzts1 protein, mouse ; Nerve Tissue Proteins ; Tumor Suppressor Proteins ; Glutamic Acid (3KX376GY7L) ; Rap2a protein, mouse (EC 3.6.1.-) ; rap GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2015-10-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.2349-15.2015
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Article ; Online: Diversification of caldesmon-linked actin cytoskeleton in cell motility.

Mayanagi, Taira / Sobue, Kenji

Cell adhesion & migration

2011 Volume 5, Issue 2, Page(s) 150–159

Abstract: The actin cytoskeleton plays a key role in regulating cell motility. Caldesmon (CaD) is an actin-linked regulatory protein found in smooth muscle and non-muscle cells that is conserved among a variety of vertebrates. It binds and stabilizes actin ... ...

Abstract	The actin cytoskeleton plays a key role in regulating cell motility. Caldesmon (CaD) is an actin-linked regulatory protein found in smooth muscle and non-muscle cells that is conserved among a variety of vertebrates. It binds and stabilizes actin filaments, as well as regulating actin-myosin interaction in a calcium (Ca2+)/calmodulin (CaM)- and/or phosphorylation-dependent manner. CaD function is regulated qualitatively by Ca2+/CaM and by its phosphorylation state and quantitatively at the mRNA level, by three different transcriptional regulation of the CALD1 gene. CaD has numerous functions in cell motility, such as migration, invasion, and proliferation, exerted via the reorganization of the actin cytoskeleton. Here we will outline recent findings regarding CaD's structural features and functions.
MeSH term(s)	Actin Cytoskeleton/physiology ; Actins ; Animals ; Calcium/metabolism ; Calmodulin/genetics ; Calmodulin/metabolism ; Calmodulin-Binding Proteins/genetics ; Calmodulin-Binding Proteins/metabolism ; Cell Movement ; Cell Proliferation ; Cytoskeleton/physiology ; Gene Expression Regulation ; Humans ; Muscle, Smooth/cytology ; Muscle, Smooth/metabolism ; Myosins/metabolism ; Phosphorylation ; Phylogeny ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA, Messenger/biosynthesis ; Transcription, Genetic
Chemical Substances	Actins ; Calmodulin ; Calmodulin-Binding Proteins ; Protein Isoforms ; RNA, Messenger ; Myosins (EC 3.6.4.1) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2011-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2268518-2
ISSN	1933-6926 ; 1933-6918
ISSN (online)	1933-6926
ISSN	1933-6918
DOI	10.4161/cam.5.2.14398
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Article ; Online: Myocardin-related transcription factor A (MRTF-A) activity-dependent cell adhesion is correlated to focal adhesion kinase (FAK) activity.

Kishi, Takayuki / Mayanagi, Taira / Iwabuchi, Sadahiro / Akasaka, Toshihide / Sobue, Kenji

Oncotarget

2016 Volume 7, Issue 44, Page(s) 72113–72130

Abstract: The regulation of cell-substrate adhesion is tightly linked to the malignant phenotype of tumor cells and plays a role in their migration, invasion, and metastasis. Focal adhesions (FAs) are dynamic adhesion structures that anchor the cell to the ... ...

Abstract	The regulation of cell-substrate adhesion is tightly linked to the malignant phenotype of tumor cells and plays a role in their migration, invasion, and metastasis. Focal adhesions (FAs) are dynamic adhesion structures that anchor the cell to the extracellular matrix. Myocardin-related transcription factors (MRTFs), co-regulators of the serum response factor (SRF), regulate expression of a set of genes encoding actin cytoskeletal/FA-related proteins. Here we demonstrated that the forced expression of a constitutively active MRTF-A (CA-MRTF-A) in B16F10 melanoma cells induced the up-regulation of actin cytoskeletal and FA proteins, resulting in FA reorganization and the suppression of cell migration. Expression of CA-MRTF-A markedly increased phosphorylation of focal adhesion kinase (FAK) and paxillin, which are important components for FA dynamics. Notably, FAK activation was triggered by the clustering of up-regulated integrins. Our results revealed that the MRTF-SRF-dependent regulation of cell migration requires both the up-regulation of actin cytoskeletal/FA proteins and the integrin-mediated regulation of FA components via the FAK/Src pathway. We also demonstrated that activation of the MRTF-dependent transcription correlates FAK activation in various tumor cells. The elucidation of the correlation between MRTF and FAK activities would be an effective therapeutic target in focus of tumor cell migration.
MeSH term(s)	Actins/metabolism ; Animals ; Cell Adhesion/genetics ; Cell Line, Tumor ; Cell Movement/genetics ; Focal Adhesion Kinase 1/genetics ; Focal Adhesion Kinase 1/metabolism ; Focal Adhesions/pathology ; Gene Expression Regulation, Neoplastic ; Humans ; Integrins/metabolism ; Mice ; Microscopy, Fluorescence ; Neoplasms/genetics ; Neoplasms/pathology ; Paxillin/metabolism ; Phosphorylation ; RNA Interference ; RNA, Small Interfering/metabolism ; Rats ; Real-Time Polymerase Chain Reaction ; Serum Response Factor/metabolism ; Signal Transduction/genetics ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Up-Regulation ; src-Family Kinases/genetics ; src-Family Kinases/metabolism
Chemical Substances	Actins ; Integrins ; MRTFA protein, human ; Mrtfa protein, mouse ; PXN protein, human ; Paxillin ; RNA, Small Interfering ; Serum Response Factor ; Trans-Activators ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; PTK2 protein, human (EC 2.7.10.2) ; Ptk2 protein, mouse (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2)
Language	English
Publishing date	2016-10-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.12350
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Article ; Online: Docosahexaenoic Acid Promotes Axon Outgrowth by Translational Regulation of Tau and Collapsin Response Mediator Protein 2 Expression.

Mita, Toshinari / Mayanagi, Taira / Ichijo, Hiroshi / Fukumoto, Kentaro / Otsuka, Kotaro / Sakai, Akio / Sobue, Kenji

The Journal of biological chemistry

2016 Volume 291, Issue 10, Page(s) 4955–4965

Abstract: n-3 PUFAs are essential for neuronal development and brain function. However, the molecular mechanisms underlying their biological effects remain unclear. Here we examined the mechanistic action of docosahexaenoic acid (DHA), the most abundant n-3 ... ...

Abstract	n-3 PUFAs are essential for neuronal development and brain function. However, the molecular mechanisms underlying their biological effects remain unclear. Here we examined the mechanistic action of docosahexaenoic acid (DHA), the most abundant n-3 polyunsaturated fatty acids in the brain. We found that DHA treatment of cortical neurons resulted in enhanced axon outgrowth that was due to increased axon elongation rates. DHA-mediated axon outgrowth was accompanied by the translational up-regulation of Tau and collapsin response mediator protein 2 (CRMP2), two important axon-related proteins, and the activation of Akt and p70 S6 kinase. Consistent with these findings, rapamycin, a potent inhibitor of mammalian target of rapamycin (mTOR), prevented DHA-mediated axon outgrowth and up-regulation of Tau and CRMP2. In addition, DHA-dependent activation of the Akt-mTOR-S6K pathway enhanced 5'-terminal oligopyrimidine tract-dependent translation of Tau and CRMP2. Therefore, our results revealed an important role for the Akt-mTOR-S6K pathway in DHA-mediated neuronal development.
MeSH term(s)	Animals ; Axons/drug effects ; Axons/metabolism ; Cells, Cultured ; Docosahexaenoic Acids/pharmacology ; Intercellular Signaling Peptides and Proteins ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurogenesis ; Proto-Oncogene Proteins c-akt/metabolism ; Rats ; Rats, Wistar ; Ribosomal Protein S6 Kinases/metabolism ; Second Messenger Systems ; TOR Serine-Threonine Kinases/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Intercellular Signaling Peptides and Proteins ; Nerve Tissue Proteins ; collapsin response mediator protein-2 ; tau Proteins ; Docosahexaenoic Acids (25167-62-8) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Ribosomal Protein S6 Kinases (EC 2.7.11.1)
Language	English
Publishing date	2016-01-13
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.M115.693499
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Article ; Online: Caldesmon regulates axon extension through interaction with myosin II.

Morita, Tsuyoshi / Mayanagi, Taira / Sobue, Kenji

The Journal of biological chemistry

2011 Volume 287, Issue 5, Page(s) 3349–3356

Abstract: To begin the process of forming neural circuits, new neurons first establish their polarity and extend their axon. Axon extension is guided and regulated by highly coordinated cytoskeletal dynamics. Here we demonstrate that in hippocampal neurons, the ... ...

Abstract	To begin the process of forming neural circuits, new neurons first establish their polarity and extend their axon. Axon extension is guided and regulated by highly coordinated cytoskeletal dynamics. Here we demonstrate that in hippocampal neurons, the actin-binding protein caldesmon accumulates in distal axons, and its N-terminal interaction with myosin II enhances axon extension. In cortical neural progenitor cells, caldesmon knockdown suppresses axon extension and neuronal polarity. These results indicate that caldesmon is an important regulator of axon development.
MeSH term(s)	Animals ; Axons/metabolism ; Calmodulin-Binding Proteins/genetics ; Calmodulin-Binding Proteins/metabolism ; Cells, Cultured ; Cytoskeleton/genetics ; Cytoskeleton/metabolism ; Hippocampus/cytology ; Hippocampus/metabolism ; Humans ; Myosin Type II/genetics ; Myosin Type II/metabolism ; Neural Stem Cells/cytology ; Neural Stem Cells/metabolism ; Rats
Chemical Substances	Calmodulin-Binding Proteins ; Myosin Type II (EC 3.6.1.-)
Language	English
Publishing date	2011-12-09
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.M111.295618
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Article: Na+/H+ exchange regulatory factor 1 is required for ROMK1 K+ channel expression in the surface membrane of cultured M-1 cortical collecting duct cells

Suzuki, Takashi / Kazuyoshi Nakamura / Kenji Sobue / Manabu Kubokawa / Taira Mayanagi

Biochemical and biophysical research communications. 2017 July 22, v. 489

2017

Abstract: The ROMK1 K+ channel, a member of the ROMK channel family, is the major candidate for the K+ secretion pathway in the renal cortical collecting duct (CCD). ROMK1 possesses a PDZ domain-binding motif at its C-terminus that is considered a modulator of ... ...

Abstract	The ROMK1 K+ channel, a member of the ROMK channel family, is the major candidate for the K+ secretion pathway in the renal cortical collecting duct (CCD). ROMK1 possesses a PDZ domain-binding motif at its C-terminus that is considered a modulator of ROMK1 expression via interaction with Na+/H+ exchange regulatory factor (NHERF) 1 and NHERF2 scaffold protein. Although NHERF1 is a potential binding partner of the ROMK1 K+ channel, the interaction between NHERF1 and K+ channel activity remains unclear. Therefore, in this study, we knocked down NHERF1 in cultured M-1Â cells derived from mouse CCD and investigated the surface expression and K+ channel current in these cells after exogenous transfection with EGFP-ROMK1. NHERF1 knockdown resulted in reduced surface expression of ROMK1 as indicated by a cell biotinylation assay. Using the patch-clamp technique, we further found that the number of active channels per patched membrane and the Ba2+-sensitive whole-cell K+ current were decreased in the knockdown cells, suggesting that reduced K+ current was accompanied by decreased surface expression of ROMK1 in the NHERF1 knockdown cells. Our results provide evidence that NHERF1 mediates K+ current activity through acceleration of the surface expression of ROMK1 K+ channels in M-1Â cells.
Keywords	biotinylation ; mice ; patch-clamp technique ; potassium ; potassium channels ; scaffolding proteins ; secretion ; transfection
Language	English
Dates of publication	2017-0722
Size	p. 116-122.
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.2017.05.104
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Article: Folic acid is a potent chemoattractant of free-living amoebae in a new and amazing species of protist, Vahlkampfia sp.

Maeda, Yasuo / Mayanagi, Taira / Amagai, Aiko

Zoological science

2009 Volume 26, Issue 3, Page(s) 179–186

Abstract: Folic acid (folate; vitamin Bc) is well recognized as essential for the proper metabolism of the essential amino acid methionine as well as for the synthesis of adenine and thymine. A folate deficiency has been Implicated in a wide variety of disorders ... ...

Abstract	Folic acid (folate; vitamin Bc) is well recognized as essential for the proper metabolism of the essential amino acid methionine as well as for the synthesis of adenine and thymine. A folate deficiency has been Implicated in a wide variety of disorders from Alzheimer's disease to depression and neural tube defects. In the cellular slime molds, including Dictyostelium, vegetative growth-phase cells are known to chemotactically move toward folate that is secreted by bacterial food sources such as Escherichia coli. Intracellular folate signal transductlon, including G proteins, Ca(2+)channels, and the PIP3 pathway, has been reported in D. discoideum. To our surprise, the genuine chemoattractant(s) of free-living protozoan amoebae have remained to be determined, possibly because of lack of a pertinent method for assaying chemotaxis. We recently isolated a primitive free-living amoeba from the soil of Costa Rica and identified it as a new species of the genus Vahlkampfia belonging to Subclass Gymnamoebia, which includes Entamoeba and Acanthamoeba. The amoebae can grow and multiply quite rapidly, engulfing nearby bacteria such as E. coli. Importantly, we have demonstrated here using a quite simple but finely designed chemotaxis assay that the Vahlkampfia amoebae exhibit chemotaxis toward higher folate concentrations. Riboflavin and cyanocobalamin were also found to serve as positive chemoattractants. Among these chemoattractants, folate is of particular importance because its function seems to be evolutionarily conserved as a potent chemoattractant of amoeboid cells in a wide range of organisms as well as in the Protista and cellular slime molds.
MeSH term(s)	Animals ; Biological Evolution ; Chemotaxis/physiology ; Eukaryota/classification ; Eukaryota/cytology ; Eukaryota/drug effects ; Eukaryota/genetics ; Folic Acid/pharmacology ; Riboflavin/pharmacology ; Vitamin B 12/pharmacology
Chemical Substances	Folic Acid (935E97BOY8) ; Vitamin B 12 (P6YC3EG204) ; Riboflavin (TLM2976OFR)
Language	English
Publishing date	2009-03
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2038883-4
ISSN	0289-0003
ISSN	0289-0003
DOI	10.2108/zsj.26.179
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