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Article ; Online: FAT4 Fine-Tunes Kidney Development by Regulating RET Signaling.

Zhang, Hongtao / Bagherie-Lachidan, Mazdak / Badouel, Caroline / Enderle, Leonie / Peidis, Philippos / Bremner, Rod / Kuure, Satu / Jain, Sanjay / McNeill, Helen

Developmental cell

2019 Volume 48, Issue 6, Page(s) 780–792.e4

Abstract: FAT4 mutations lead to several human diseases that disrupt the normal development of the kidney. However, the underlying mechanism remains elusive. In studying the duplex kidney phenotypes observed upon deletion of Fat4 in mice, we have uncovered an ... ...

Abstract	FAT4 mutations lead to several human diseases that disrupt the normal development of the kidney. However, the underlying mechanism remains elusive. In studying the duplex kidney phenotypes observed upon deletion of Fat4 in mice, we have uncovered an interaction between the atypical cadherin FAT4 and RET, a tyrosine kinase receptor essential for kidney development. Analysis of kidney development in Fat4
MeSH term(s)	Animals ; Cadherins/chemistry ; Cadherins/deficiency ; Cadherins/metabolism ; Gene Deletion ; Glial Cell Line-Derived Neurotrophic Factor/metabolism ; Glial Cell Line-Derived Neurotrophic Factor Receptors/metabolism ; Humans ; Kidney/abnormalities ; Kidney/embryology ; Kidney/metabolism ; Mice ; Nerve Tissue Proteins/deficiency ; Nerve Tissue Proteins/metabolism ; Protein Binding ; Proto-Oncogene Proteins c-ret/metabolism ; Signal Transduction ; Up-Regulation
Chemical Substances	Cadherins ; Dchs1 protein, mouse ; Fat4 protein, mouse ; Fjx1 protein, mouse ; Gfra1 protein, mouse ; Glial Cell Line-Derived Neurotrophic Factor ; Glial Cell Line-Derived Neurotrophic Factor Receptors ; Nerve Tissue Proteins ; Proto-Oncogene Proteins c-ret (EC 2.7.10.1)
Language	English
Publishing date	2019-03-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2019.02.004
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Zs.MG 76: Show issues

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Article ; Online: What drives cyst formation in PKD?

Bagherie-Lachidan, Mazdak / McNeill, Helen

Journal of the American Society of Nephrology : JASN

2010 Volume 21, Issue 2, Page(s) 200–202

MeSH term(s)	Animals ; Cell Division/physiology ; Cell Polarity/physiology ; Disease Models, Animal ; Humans ; Kidney/pathology ; Mice ; Mutation/genetics ; Polycystic Kidney Diseases/genetics ; Polycystic Kidney Diseases/physiopathology ; Receptors, Cell Surface/genetics ; Signal Transduction/physiology ; TRPP Cation Channels/genetics
Chemical Substances	PKHD1 protein, human ; Pkhd1 protein, mouse ; Receptors, Cell Surface ; TRPP Cation Channels ; polycystic kidney disease 1 protein ; polycystic kidney disease 2 protein
Language	English
Publishing date	2010-02
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	1085942-1
ISSN	1533-3450 ; 1046-6673
ISSN (online)	1533-3450
ISSN	1046-6673
DOI	10.1681/ASN.2009121261
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Article ; Online: Cortisol differentially alters claudin isoforms in cultured puffer fish gill epithelia.

Bui, Phuong / Bagherie-Lachidan, Mazdak / Kelly, Scott P

Molecular and cellular endocrinology

2010 Volume 317, Issue 1-2, Page(s) 120–126

Abstract: A primary cultured gill epithelium from the puffer fish Tetraodon nigroviridis was developed to examine the corticosteroid regulation of claudin isoform mRNA abundance in fish gills. Preparations were composed of polygonal epithelial cells exhibiting ... ...

Abstract	A primary cultured gill epithelium from the puffer fish Tetraodon nigroviridis was developed to examine the corticosteroid regulation of claudin isoform mRNA abundance in fish gills. Preparations were composed of polygonal epithelial cells exhibiting concentric apical microridges and zonula occludens-1 immunoreactivity along cell margins. No evidence was found to indicate the presence of Na(+)-K(+)-ATPase-immunoreactive or mitochondria-rich cells in cultured preparations. Therefore, epithelia appear to be composed of gill pavement cells (PVCs) only. An RT-PCR profile of 12 salinity responsive gill claudin tight junction (TJ) proteins (Tncldn3a, -3c, -6, -8d, -10d, -10e, -11a, -23b, -27a, -27c, -32a, and -33b) revealed the absence of Tncldn6, -10d and -10e in cultured epithelia, suggesting that these isoforms are not associated with gill PVCs. Cortisol treatment of cultured epithelia dose-dependently increased or decreased mRNA abundance of select claudin isoforms. Transcript abundance of several claudin isoforms was unaffected by cortisol treatment. These data provide evidence for the cell specific distribution of claudins in fish gills and suggest that heterogeneous alterations in the abundance of select claudin isoforms contribute to the corticosteroid regulation of gill permeability.
MeSH term(s)	Acclimatization/drug effects ; Animals ; Claudins/genetics ; Claudins/metabolism ; Epithelium/drug effects ; Epithelium/metabolism ; Fresh Water ; Gene Expression Profiling ; Gene Expression Regulation/drug effects ; Gills/drug effects ; Gills/metabolism ; Hydrocortisone/pharmacology ; Immunohistochemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Salinity ; Seawater ; Tetraodontiformes/genetics ; Tetraodontiformes/metabolism ; Tissue Culture Techniques
Chemical Substances	Claudins ; Protein Isoforms ; RNA, Messenger ; Hydrocortisone (WI4X0X7BPJ)
Language	English
Publishing date	2010-04-12
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2009.12.002
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Article: Claudin-3 tight junction proteins in Tetraodon nigroviridis: cloning, tissue-specific expression, and a role in hydromineral balance.

Bagherie-Lachidan, Mazdak / Wright, Stephen I / Kelly, Scott P

American journal of physiology. Regulatory, integrative and comparative physiology

2008 Volume 294, Issue 5, Page(s) R1638–47

Abstract: Claudins are a large family of integral transmembrane tight junction (TJ) proteins involved in regulating the permeability of the paracellular pathway. In these studies, we clone and describe the tissue distribution of four claudin-3 genes (designated ... ...

Abstract	Claudins are a large family of integral transmembrane tight junction (TJ) proteins involved in regulating the permeability of the paracellular pathway. In these studies, we clone and describe the tissue distribution of four claudin-3 genes (designated Tncldn3a, Tncldn3b, Tncldn3c, and Tncldn3d) from the euryhaline spotted green puffer fish Tetraodon nigroviridis and examine the response of Tetraodon and Tncldn3 mRNAs to salinity variation (freshwater, FW; seawater, SW; and hypersaline seawater, HSW). In Tetraodon, genes encoding for claudin-3 TJ proteins are widely expressed, suggesting that claudin-3 proteins participate in regulating paracellular permeability across various epithelia within fishes. Of particular note is the widespread distribution of Tncldn3 genes in tissues that regulate hydromineral balance (gills, skin, kidney, and intestine). Renal and intestinal tissues express all four Tncldn3 genes, while the gills and skin specifically express Tncldn3a and Tncldn3c. In response to salinity variation, Tetraodon exhibits characteristics typical of a euryhaline fish species: moderate changes in blood osmolality and muscle moisture content; alterations in gill, kidney, and intestinal Na(+)-K(+)-ATPase activity; and unaltered Na(+)-K(+)-ATPase activity in the integument. In conjunction with these changes, Tncldn3 mRNA expression exhibits marked and significant salinity-dependent alterations that are both tissue and gene specific. Overall, our data suggest that a decreased abundance of claudin-3 in Tetraodon occurs in "leakier" epithelia and that claudin-3 TJ proteins will likely play an important role in the maintenance of hydromineral balance across osmoregulatory epithelia of euryhaline fishes.
MeSH term(s)	Actins/biosynthesis ; Actins/genetics ; Animals ; Claudin-3 ; Cloning, Molecular ; Electrophoresis, Agar Gel ; Gene Expression Profiling ; Membrane Proteins/metabolism ; Osmolar Concentration ; Phylogeny ; Reverse Transcriptase Polymerase Chain Reaction ; Seawater ; Sodium/blood ; Sodium-Potassium-Exchanging ATPase/metabolism ; Terminology as Topic ; Tetraodontiformes/classification ; Tetraodontiformes/physiology ; Tissue Distribution ; Water/metabolism ; Water-Electrolyte Balance/physiology
Chemical Substances	Actins ; Claudin-3 ; Membrane Proteins ; Water (059QF0KO0R) ; Sodium (9NEZ333N27) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
Language	English
Publishing date	2008-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603839-6
ISSN	1522-1490 ; 0363-6119
ISSN (online)	1522-1490
ISSN	0363-6119
DOI	10.1152/ajpregu.00039.2008
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Article ; Online: Claudin-8 and -27 tight junction proteins in puffer fish Tetraodon nigroviridis acclimated to freshwater and seawater.

Bagherie-Lachidan, Mazdak / Wright, Stephen I / Kelly, Scott P

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology

2008 Volume 179, Issue 4, Page(s) 419–431

Abstract: Genes encoding for claudin-8 and -27 tight junction proteins in the euryhaline puffer fish (Tetraodon nigroviridis) were identified using its recently sequenced genome. Phylogenetic analysis indicated that multiple genes encoding for claudin-8 proteins ( ... ...

Abstract	Genes encoding for claudin-8 and -27 tight junction proteins in the euryhaline puffer fish (Tetraodon nigroviridis) were identified using its recently sequenced genome. Phylogenetic analysis indicated that multiple genes encoding for claudin-8 proteins (designated Tncldn8a, Tncldn8b, Tncldn8c and Tncldn8d) arose by tandem gene duplication. In contrast, both tandem and whole genome duplication events appear to have generated genes encoding for claudin-27 proteins (designated Tncldn27a, Tncldn27b, Tncldn27c and Tncldn27d). Tncldn8 and Tncldn27 mRNA were widely distributed in Tetraodon, suggesting involvement in various physiological processes. All Tncldn8 and Tncldn27 genes were expressed in gill and skin tissue (i.e., epithelia exposed directly to the external environment). A potential role for claudin-8 and -27 proteins in the regulation of hydromineral balance in Tetraodon was investigated by examining alterations in mRNA abundance in select ionoregulatory tissue of fish acclimated to freshwater (FW) and seawater (SW). In FW or SW, Tetraodon exhibited alterations in Na(+)-K(+)-ATPase activity (a correlate of transcellular transport) typical of a euryhaline teleost fish. Simultaneously, tissue and gene specific alterations in Tncldn8 and Tncldn27 transcript abundance occurred. These data provide some insight into the duplication history of cldn8 and cldn27 genes in fishes and suggest a possible role for claudin-8 and -27 proteins in the osmoregulatory strategies of euryhaline teleosts.
MeSH term(s)	Acclimatization/genetics ; Acclimatization/physiology ; Animals ; Claudins ; DNA Primers/genetics ; Evolution, Molecular ; Fresh Water/chemistry ; Gene Expression Profiling ; Gene Expression Regulation/physiology ; Genes, Duplicate/genetics ; Gills/metabolism ; Membrane Proteins/genetics ; Phylogeny ; Reverse Transcriptase Polymerase Chain Reaction ; Seawater/chemistry ; Skin/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism ; Tetraodontiformes/genetics ; Tight Junctions/genetics
Chemical Substances	Claudins ; DNA Primers ; Membrane Proteins ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; claudin 8 (HJ6C19SU7L)
Language	English
Publishing date	2008-12-27
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	231245-1
ISSN	1432-136X ; 0174-1578
ISSN (online)	1432-136X
ISSN	0174-1578
DOI	10.1007/s00360-008-0326-0
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Article ; Online: Epithelial remodeling and claudin mRNA abundance in the gill and kidney of puffer fish (Tetraodon biocellatus) acclimated to altered environmental ion levels.

Duffy, Nicole M / Bui, Phuong / Bagherie-Lachidan, Mazdak / Kelly, Scott P

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology

2010 Volume 181, Issue 2, Page(s) 219–238

Abstract: In water of varying ion content, the gills and kidney of fishes contribute significantly to the maintenance of salt and water balance. However, little is known about the molecular architecture of the tight junction (TJ) complex and the regulation of ... ...

Abstract	In water of varying ion content, the gills and kidney of fishes contribute significantly to the maintenance of salt and water balance. However, little is known about the molecular architecture of the tight junction (TJ) complex and the regulation of paracellular permeability characteristics in these tissues. In the current studies, puffer fish (Tetraodon biocellatus) were acclimated to freshwater (FW), seawater (SW) or ion-poor freshwater (IPW) conditions. Following acclimation, alterations in systemic endpoints of hydromineral status were examined in conjunction with changes in gill and kidney epithelia morphology/morphometrics, as well as claudin TJ protein mRNA abundance. T. biocellatus were able to maintain endpoints of hydromineral status within relatively tight limits across the broad range of water ion content examined. Both gill and kidney tissue exhibited substantial alterations in morphology as well as claudin TJ protein mRNA abundance. These responses were particularly pronounced when comparing fish acclimated to SW versus those acclimated to IPW. TEM observations of IPW-acclimated fish gills revealed the presence of cells that exhibited the typical characteristics of gill mitochondria-rich cells (e.g. voluminous, Na(+)-K(+)-ATPase-immunoreactive, exposed to the external environment at the apical surface), but were not mitochondria-rich. To our knowledge, this type of cell has not previously been described in hyperosmoregulating fish gills. Furthermore, modifications in the morphometrics and claudin mRNA abundance of kidney tissue support the notion that spatial alterations in claudin TJ proteins along the nephron of fishes will likely play an important role in the regulation of salt and water balance in these organisms.
MeSH term(s)	Acclimatization/physiology ; Analysis of Variance ; Animals ; Claudins/metabolism ; Gills/metabolism ; Gills/ultrastructure ; Immunohistochemistry ; Ions/analysis ; Kidney/metabolism ; Kidney/ultrastructure ; Microscopy, Electron ; Osmolar Concentration ; Reverse Transcriptase Polymerase Chain Reaction ; Salinity ; Sodium-Potassium-Exchanging ATPase/metabolism ; Tetraodontiformes/metabolism
Chemical Substances	Claudins ; Ions ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
Language	English
Publishing date	2010-10-26
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	231245-1
ISSN	1432-136X ; 0174-1578
ISSN (online)	1432-136X
ISSN	0174-1578
DOI	10.1007/s00360-010-0517-3
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Article ; Online: Spatial and salinity-induced alterations in claudin-3 isoform mRNA along the gastrointestinal tract of the pufferfish Tetraodon nigroviridis.

Clelland, Eric S / Bui, Phuong / Bagherie-Lachidan, Mazdak / Kelly, Scott P

Comparative biochemistry and physiology. Part A, Molecular & integrative physiology

2010 Volume 155, Issue 2, Page(s) 154–163

Abstract: In fishes, variation in paracellular permeability is important for regulating salt and water balance. Paracellular permeability is maintained by TJs in vertebrate epithelia. This study examined the spatial distribution and effects of salinity on claudin- ... ...

Abstract	In fishes, variation in paracellular permeability is important for regulating salt and water balance. Paracellular permeability is maintained by TJs in vertebrate epithelia. This study examined the spatial distribution and effects of salinity on claudin-3 isoform mRNA expression and abundance along the gastrointestinal (GI) tract of the euryhaline puffer fish (Tetraodon nigroviridis) and related these to morphological heterogeneity of the TJ complex. The puffer fish GI tract was divided into three regions (anterior, middle and posterior) and four isoforms of claudin-3 (Tncldn3a, Tncldn3b, Tncldn3c and Tncldn3d) were found to be expressed in each section. The effect of freshwater (FW) or seawater (SW) acclimation on regional 1) Tncldn3 isoform mRNA abundance, 2) TJ complex morphology and 3) Na(+)-K(+)-ATPase (NKA) activity was examined. In situ hybridization indicated that all Tncldn3 isoforms localized to the mucosal epithelium in the intestine. The mRNA abundance of Tncldn3 isoforms varied spatially along the GI tract. Furthermore, region as well as isoform specific alterations in mRNA abundance could be observed along the GI tract in response to salinity change. Qualitative TEM observations suggested that the depth of TJ complexes increased from anterior to posterior along the GI tract and that TJ complexes in the GI tract of FW fish were deeper than those in SW. NKA activity increased from anterior to posterior in fish acclimated to FW, whereas activity in fish acclimated to SW was uniformly high along the length of the intestine. Taken together data; (1) suggest a progressive decrease in epithelial permeability from anterior to posterior along the longitudinal axis of the puffer fish GI tract, (2) indicate that claudin-3 protein isoforms may play a role in regulating paracellular movement of solutes across this epithelium, and (3) provide further evidence that claudin-3 proteins are involved in the homeostatic control of salt and water balance in fishes.
MeSH term(s)	Animals ; Claudin-3 ; Epithelium/enzymology ; Epithelium/metabolism ; Epithelium/ultrastructure ; Fish Proteins/genetics ; Fresh Water ; Gastrointestinal Tract/enzymology ; Gastrointestinal Tract/metabolism ; Gastrointestinal Tract/ultrastructure ; Gene Expression Profiling ; In Situ Hybridization ; Intestinal Mucosa/enzymology ; Intestinal Mucosa/metabolism ; Intestinal Mucosa/ultrastructure ; Membrane Proteins/genetics ; Microscopy, Electron, Transmission ; Protein Isoforms/genetics ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Salinity ; Seawater ; Sodium-Potassium-Exchanging ATPase/metabolism ; Tetraodontiformes/genetics ; Tetraodontiformes/metabolism ; Tight Junctions/enzymology ; Tight Junctions/metabolism ; Tight Junctions/ultrastructure
Chemical Substances	Claudin-3 ; Fish Proteins ; Membrane Proteins ; Protein Isoforms ; RNA, Messenger ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9)
Language	English
Publishing date	2010-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	121246-1
ISSN	1531-4332 ; 0300-9629 ; 1095-6433
ISSN (online)	1531-4332
ISSN	0300-9629 ; 1095-6433
DOI	10.1016/j.cbpa.2009.10.038
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Article ; Online: Stromal Fat4 acts non-autonomously with Dchs1/2 to restrict the nephron progenitor pool.

Bagherie-Lachidan, Mazdak / Reginensi, Antoine / Pan, Qun / Zaveri, Hitisha P / Scott, Daryl A / Blencowe, Benjamin J / Helmbacher, Françoise / McNeill, Helen

Development (Cambridge, England)

2015 Volume 142, Issue 15, Page(s) 2564–2573

Abstract: Regulation of the balance between progenitor self-renewal and differentiation is crucial to development. In the mammalian kidney, reciprocal signalling between three lineages (stromal, mesenchymal and ureteric) ensures correct nephron progenitor self- ... ...

Abstract	Regulation of the balance between progenitor self-renewal and differentiation is crucial to development. In the mammalian kidney, reciprocal signalling between three lineages (stromal, mesenchymal and ureteric) ensures correct nephron progenitor self-renewal and differentiation. Loss of either the atypical cadherin FAT4 or its ligand Dachsous 1 (DCHS1) results in expansion of the mesenchymal nephron progenitor pool, called the condensing mesenchyme (CM). This has been proposed to be due to misregulation of the Hippo kinase pathway transcriptional co-activator YAP. Here, we use tissue-specific deletions to prove that FAT4 acts non-autonomously in the renal stroma to control nephron progenitors. We show that loss of Yap from the CM in Fat4-null mice does not reduce the expanded CM, indicating that FAT4 regulates the CM independently of YAP. Analysis of Six2(-/-);Fat4(-/-) double mutants demonstrates that excess progenitors in Fat4 mutants are dependent on Six2, a crucial regulator of nephron progenitor self-renewal. Electron microscopy reveals that cell organisation is disrupted in Fat4 mutants. Gene expression analysis demonstrates that the expression of Notch and FGF pathway components are altered in Fat4 mutants. Finally, we show that Dchs1, and its paralogue Dchs2, function in a partially redundant fashion to regulate the number of nephron progenitors. Our data support a model in which FAT4 in the stroma binds to DCHS1/2 in the mouse CM to restrict progenitor self-renewal.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Analysis of Variance ; Animals ; Cadherins/metabolism ; Cell Cycle Proteins ; Cell Differentiation/physiology ; Cell Lineage/physiology ; Fluorescent Antibody Technique ; Gene Expression Profiling ; Immunoblotting ; In Situ Hybridization ; In Situ Nick-End Labeling ; Mice ; Mice, Knockout ; Microscopy, Electron ; Nephrons/ultrastructure ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Sequence Analysis, RNA ; Signal Transduction/physiology ; Stem Cells/cytology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cadherins ; Cell Cycle Proteins ; Dchs1 protein, mouse ; Fat4 protein, mouse ; Phosphoproteins ; Yap1 protein, mouse ; Hippo protein, mouse (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2015-06-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.122648
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Article: Claudin-8 and -27 tight junction proteins in puffer fish Tetraodon nigroviridis acclimated to freshwater and seawater

Bagherie-Lachidan, Mazdak / Wright, Stephen I / Kelly, Scott P

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology. 2009 May, v. 179, no. 4

2009

Abstract	Genes encoding for claudin-8 and -27 tight junction proteins in the euryhaline puffer fish (Tetraodon nigroviridis) were identified using its recently sequenced genome. Phylogenetic analysis indicated that multiple genes encoding for claudin-8 proteins (designated Tncldn8a, Tncldn8b, Tncldn8c and Tncldn8d) arose by tandem gene duplication. In contrast, both tandem and whole genome duplication events appear to have generated genes encoding for claudin-27 proteins (designated Tncldn27a, Tncldn27b, Tncldn27c and Tncldn27d). Tncldn8 and Tncldn27 mRNA were widely distributed in Tetraodon, suggesting involvement in various physiological processes. All Tncldn8 and Tncldn27 genes were expressed in gill and skin tissue (i.e., epithelia exposed directly to the external environment). A potential role for claudin-8 and -27 proteins in the regulation of hydromineral balance in Tetraodon was investigated by examining alterations in mRNA abundance in select ionoregulatory tissue of fish acclimated to freshwater (FW) and seawater (SW). In FW or SW, Tetraodon exhibited alterations in Na⁺-K⁺-ATPase activity (a correlate of transcellular transport) typical of a euryhaline teleost fish. Simultaneously, tissue and gene specific alterations in Tncldn8 and Tncldn27 transcript abundance occurred. These data provide some insight into the duplication history of cldn8 and cldn27 genes in fishes and suggest a possible role for claudin-8 and -27 proteins in the osmoregulatory strategies of euryhaline teleosts.
Language	English
Dates of publication	2009-05
Size	p. 419-431.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ZDB-ID	231245-1
ISSN	1432-136X ; 0174-1578
ISSN (online)	1432-136X
ISSN	0174-1578
DOI	10.1007/s00360-008-0326-0
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Article ; Online: Fat1 interacts with Fat4 to regulate neural tube closure, neural progenitor proliferation and apical constriction during mouse brain development.

Badouel, Caroline / Zander, Mark A / Liscio, Nicole / Bagherie-Lachidan, Mazdak / Sopko, Richelle / Coyaud, Etienne / Raught, Brian / Miller, Freda D / McNeill, Helen

Development (Cambridge, England)

2015 Volume 142, Issue 16, Page(s) 2781–2791

Abstract: Mammalian brain development requires coordination between neural precursor proliferation, differentiation and cellular organization to create the intricate neuronal networks of the adult brain. Here, we examined the role of the atypical cadherins Fat1 ... ...

Abstract	Mammalian brain development requires coordination between neural precursor proliferation, differentiation and cellular organization to create the intricate neuronal networks of the adult brain. Here, we examined the role of the atypical cadherins Fat1 and Fat4 in this process. We show that mutation of Fat1 in mouse embryos causes defects in cranial neural tube closure, accompanied by an increase in the proliferation of cortical precursors and altered apical junctions, with perturbations in apical constriction and actin accumulation. Similarly, knockdown of Fat1 in cortical precursors by in utero electroporation leads to overproliferation of radial glial precursors. Fat1 interacts genetically with the related cadherin Fat4 to regulate these processes. Proteomic analysis reveals that Fat1 and Fat4 bind different sets of actin-regulating and junctional proteins. In vitro data suggest that Fat1 and Fat4 form cis-heterodimers, providing a mechanism for bringing together their diverse interactors. We propose a model in which Fat1 and Fat4 binding coordinates distinct pathways at apical junctions to regulate neural progenitor proliferation, neural tube closure and apical constriction.
MeSH term(s)	Animals ; Blotting, Western ; Brain/embryology ; Cadherins/genetics ; Cadherins/metabolism ; Cell Proliferation/physiology ; Gene Knockdown Techniques ; Mice ; Microscopy, Fluorescence ; Neural Stem Cells/physiology ; Neural Tube/embryology ; Neural Tube/metabolism ; beta-Galactosidase
Chemical Substances	Cadherins ; Fat4 protein, mouse ; Fath protein, mouse ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2015-07-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.123539
Database	MEDical Literature Analysis and Retrieval System OnLINE

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