G2Cdb::Gene report

Gene id
Gene symbol
Homo sapiens
cadherin 10, type 2 (T2-cadherin)
G00000647 (Mus musculus)

Databases (7)

ENSG00000040731 (Ensembl human gene)
1008 (Entrez Gene)
1050 (G2Cdb plasticity & disease)
CDH10 (GeneCards)
604555 (OMIM)
Marker Symbol
HGNC:1749 (HGNC)
Protein Sequence
Q9Y6N8 (UniProt)

Literature (11)

Pubmed - other

  • Hippocampal atrophy as a quantitative trait in a genome-wide association study identifying novel susceptibility genes for Alzheimer's disease.

    Potkin SG, Guffanti G, Lakatos A, Turner JA, Kruggel F, Fallon JH, Saykin AJ, Orro A, Lupoli S, Salvi E, Weiner M, Macciardi F and Alzheimer's Disease Neuroimaging Initiative

    Department of Psychiatry and Human Behavior, University of California Irvine, Irvine, CA, USA. sgpotkin@uci.edu

    Background: With the exception of APOE epsilon4 allele, the common genetic risk factors for sporadic Alzheimer's Disease (AD) are unknown.

    We completed a genome-wide association study on 381 participants in the ADNI (Alzheimer's Disease Neuroimaging Initiative) study. Samples were genotyped using the Illumina Human610-Quad BeadChip. 516,645 unique Single Nucleotide Polymorphisms (SNPs) were included in the analysis following quality control measures. The genotype data and raw genetic data are freely available for download (LONI, http://www.loni.ucla.edu/ADNI/Data/). Two analyses were completed: a standard case-control analysis, and a novel approach using hippocampal atrophy measured on MRI as an objectively defined, quantitative phenotype. A General Linear Model was applied to identify SNPs for which there was an interaction between the genotype and diagnosis on the quantitative trait. The case-control analysis identified APOE and a new risk gene, TOMM40 (translocase of outer mitochondrial membrane 40), at a genome-wide significance level of < or =10(-6) (10(-11) for a haplotype). TOMM40 risk alleles were approximately twice as frequent in AD subjects as controls. The quantitative trait analysis identified 21 genes or chromosomal areas with at least one SNP with a p-value < or =10(-6), which can be considered potential "new" candidate loci to explore in the etiology of sporadic AD. These candidates included EFNA5, CAND1, MAGI2, ARSB, and PRUNE2, genes involved in the regulation of protein degradation, apoptosis, neuronal loss and neurodevelopment. Thus, we identified common genetic variants associated with the increased risk of developing AD in the ADNI cohort, and present publicly available genome-wide data. Supportive evidence based on case-control studies and biological plausibility by gene annotation is provided. Currently no available sample with both imaging and genetic data is available for replication.

    Conclusions: Using hippocampal atrophy as a quantitative phenotype in a genome-wide scan, we have identified candidate risk genes for sporadic Alzheimer's disease that merit further investigation.

    Funded by: NCRR NIH HHS: P20 RR020837, P20 RR020837-01, U24 RR021992, U24-RR021992; NIA NIH HHS: 3 U01 AG024904-03S5, U01 AG024904, U01 AG024904-01, U19 AG010483, U24 AG021886

    PloS one 2009;4;8;e6501

  • Common genetic variants on 5p14.1 associate with autism spectrum disorders.

    Wang K, Zhang H, Ma D, Bucan M, Glessner JT, Abrahams BS, Salyakina D, Imielinski M, Bradfield JP, Sleiman PM, Kim CE, Hou C, Frackelton E, Chiavacci R, Takahashi N, Sakurai T, Rappaport E, Lajonchere CM, Munson J, Estes A, Korvatska O, Piven J, Sonnenblick LI, Alvarez Retuerto AI, Herman EI, Dong H, Hutman T, Sigman M, Ozonoff S, Klin A, Owley T, Sweeney JA, Brune CW, Cantor RM, Bernier R, Gilbert JR, Cuccaro ML, McMahon WM, Miller J, State MW, Wassink TH, Coon H, Levy SE, Schultz RT, Nurnberger JI, Haines JL, Sutcliffe JS, Cook EH, Minshew NJ, Buxbaum JD, Dawson G, Grant SF, Geschwind DH, Pericak-Vance MA, Schellenberg GD and Hakonarson H

    Center for Applied Genomics, Children's Hospital of Philadelphia, Pennsylvania 19104, USA.

    Autism spectrum disorders (ASDs) represent a group of childhood neurodevelopmental and neuropsychiatric disorders characterized by deficits in verbal communication, impairment of social interaction, and restricted and repetitive patterns of interests and behaviour. To identify common genetic risk factors underlying ASDs, here we present the results of genome-wide association studies on a cohort of 780 families (3,101 subjects) with affected children, and a second cohort of 1,204 affected subjects and 6,491 control subjects, all of whom were of European ancestry. Six single nucleotide polymorphisms between cadherin 10 (CDH10) and cadherin 9 (CDH9)-two genes encoding neuronal cell-adhesion molecules-revealed strong association signals, with the most significant SNP being rs4307059 (P = 3.4 x 10(-8), odds ratio = 1.19). These signals were replicated in two independent cohorts, with combined P values ranging from 7.4 x 10(-8) to 2.1 x 10(-10). Our results implicate neuronal cell-adhesion molecules in the pathogenesis of ASDs, and represent, to our knowledge, the first demonstration of genome-wide significant association of common variants with susceptibility to ASDs.

    Funded by: Medical Research Council; NCRR NIH HHS: M01 RR000064, M01-RR00064, UL1 RR024134, UL1 RR024134-01, UL1-RR024134-03; NICHD NIH HHS: HD055751, HD055782-01, HD055784, N01-HD-4-3368, N01-HD-4-3383, P50 HD055748, P50 HD055751, P50 HD055751-01, P50 HD055782, P50 HD055782-01, P50 HD055784, P50 HD055784-01, P50 HD055784-010002, P50 HD055784-020002, P50 HD055784-030002; NIMH NIH HHS: 1U24MH081810, MH061009, MH0666730, MH080647, MH081754, MH64547, MH69359, R01 MH061009, R01 MH061009-01A1, R01 MH064547, R01 MH064547-01, R01 MH064547-01S1, R01 MH064547-02, R01 MH064547-02S1, R01 MH064547-03, R01 MH064547-04, R01 MH064547-05, R01 MH069359, R01 MH069359-01A2, R01 MH080647, R01 MH080647-11, R01 MH081754, R01 MH081754-01, R01 MH081754-02, U24 MH081810, U54 MH066673, U54 MH066673-01A10001; NINDS NIH HHS: NS049261, NS26630, NS36768, P01 NS026630, P01 NS026630-109001, R01 NS036768, R01 NS036768-06, R01 NS049261, R01 NS049261-01A2

    Nature 2009;459;7246;528-33

  • A genome-wide association study of autism reveals a common novel risk locus at 5p14.1.

    Ma D, Salyakina D, Jaworski JM, Konidari I, Whitehead PL, Andersen AN, Hoffman JD, Slifer SH, Hedges DJ, Cukier HN, Griswold AJ, McCauley JL, Beecham GW, Wright HH, Abramson RK, Martin ER, Hussman JP, Gilbert JR, Cuccaro ML, Haines JL and Pericak-Vance MA

    Miami Institute for Human Genomics, University of Miami, Miller School of Medicine, Miami, FL, USA.

    Although autism is one of the most heritable neuropsychiatric disorders, its underlying genetic architecture has largely eluded description. To comprehensively examine the hypothesis that common variation is important in autism, we performed a genome-wide association study (GWAS) using a discovery dataset of 438 autistic Caucasian families and the Illumina Human 1M beadchip. 96 single nucleotide polymorphisms (SNPs) demonstrated strong association with autism risk (p-value < 0.0001). The validation of the top 96 SNPs was performed using an independent dataset of 487 Caucasian autism families genotyped on the 550K Illumina BeadChip. A novel region on chromosome 5p14.1 showed significance in both the discovery and validation datasets. Joint analysis of all SNPs in this region identified 8 SNPs having improved p-values (3.24E-04 to 3.40E-06) than in either dataset alone. Our findings demonstrate that in addition to multiple rare variations, part of the complex genetic architecture of autism involves common variation.

    Funded by: NIGMS NIH HHS: T32 GM080178; NIMH NIH HHS: MH080647, R01 MH080647, R01 MH080647-12; NINDS NIH HHS: NS26630, NS36768, P01 NS026630, P01 NS026630-19, P01 NS026630-190010, R01 NS036768, R01 NS036768-10

    Annals of human genetics 2009;73;Pt 3;263-73

  • A human protein-protein interaction network: a resource for annotating the proteome.

    Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H and Wanker EE

    Max Delbrueck Center for Molecular Medicine, 13092 Berlin-Buch, Germany.

    Protein-protein interaction maps provide a valuable framework for a better understanding of the functional organization of the proteome. To detect interacting pairs of human proteins systematically, a protein matrix of 4456 baits and 5632 preys was screened by automated yeast two-hybrid (Y2H) interaction mating. We identified 3186 mostly novel interactions among 1705 proteins, resulting in a large, highly connected network. Independent pull-down and co-immunoprecipitation assays validated the overall quality of the Y2H interactions. Using topological and GO criteria, a scoring system was developed to define 911 high-confidence interactions among 401 proteins. Furthermore, the network was searched for interactions linking uncharacterized gene products and human disease proteins to regulatory cellular pathways. Two novel Axin-1 interactions were validated experimentally, characterizing ANP32A and CRMP1 as modulators of Wnt signaling. Systematic human protein interaction screens can lead to a more comprehensive understanding of protein function and cellular processes.

    Cell 2005;122;6;957-68

  • Developmental patterns of cadherin expression and localization in relation to compartmentalized thalamocortical terminations in rat barrel cortex.

    Gil OD, Needleman L and Huntley GW

    Fishberg Research Center for Neurobiology, The Mount Sinai School of Medicine, New York, New York 10029, USA.

    The wiring of synaptic circuitry during development is remarkably precise, but the molecular interactions that enable such precision remain largely to be defined. Cadherins are cell adhesion molecules hypothesized to play roles in axon growth and synaptic targeting during development. We previously showed that N-cadherin localizes to ventrobasal (VB) thalamocortical synapses in rat somatosensory (barrel) cortex during formation of the whisker-map in layer IV (Huntley and Benson [1999] J. Comp. Neurol. 407:453-471). Such specific association of N-cadherin with one identified afferent pathway raises the prediction that other cadherins are expressed in barrel cortex and that these are, in some combination, also differentially associated with distinct inputs. Here, we first show that N-cadherin and three other classic cadherins (cadherin-6, -8, and -10) are expressed contemporaneously in barrel cortex with relative levels of postnatal expression that are highest during the first 2 weeks, when afferent and intrinsic circuitries are forming and synaptogenesis is maximal. Each displayed distinct, but partly overlapping laminar patterns of expression that changed over time. Cadherin-8 probe hybridization formed a particularly striking pattern of intermittent, columnar patches extending from layer V through layer III, which was first detectable at approximately postnatal day 3. The patches were centered precisely over regions of dysgranular layer IV and, in the whisker barrel field, over barrel septa. This pattern is similar to that formed by the terminal distribution of thalamocortical afferents arising from the posterior nucleus (POm), suggesting cadherin-8 association with the POm thalamocortical synaptic circuit. Consistent with this, cadherin-8 mRNAs were enriched in the POm nucleus, and cadherin-8 immunolabeling in layer IV was enriched in barrel septa and codistributed with labeled POm thalamocortical synaptic-like puncta. The striking molecular parcellation of at least two different cadherins to the two, converging thalamic pathways that terminated in non-overlapping barrel center and septal compartments in layer IV strongly suggested that cadherins provide requisite molecular recognition and targeting that enable precise construction of thalamocortical and other synaptic circuitry.

    Funded by: NIDA NIH HHS: DA07135-22; NINDS NIH HHS: NS34659

    The Journal of comparative neurology 2002;453;4;372-88

  • Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins.

    Shimoyama Y, Tsujimoto G, Kitajima M and Natori M

    Department of Surgery, National Okura Hospital, 2-10-1 Okura, Setagaya-ku, Tokyo 157-8535, Japan. shimoyay@din.or.jp

    We identified three novel human type-II classic cadherins, cadherin-7, -9 and -10, by cDNA cloning and sequencing, and confirmed that they interact with catenins and function in cell-cell adhesion as do other classic cadherins. Cell-cell binding activities of the eight human type-II classic cadherins, including the three new molecules, were evaluated by long-term cell-aggregation experiments using mouse L fibroblast clones transfected with the individual cadherins. The experiments indicated that all the type-II cadherins appeared to possess similar binding strength, which was virtually equivalent to that of E-cadherin. We next examined the binding specificities of the type-II cadherins using the mixed cell-aggregation assay. Although all of the type-II cadherins exhibited binding specificities distinct from that of E-cadherin, heterophilic interactions ranging from incomplete to complete were frequently observed among them. The combinations of cadherin-6 and -9, cadherin-7 and -14, cadherin-8 and -11, and cadherin-9 and -10 interacted in a complete manner, and in particular cadherin-7 and -14, and cadherin-8 and -11 showed an indistinguishable binding specificity against other cadherin subclasses, at least in this assay system. Although these data were obtained from an in vitro study, they should be useful for understanding cadherin-mediated mechanisms of development, morphogenesis and cell-cell interactions in vivo.

    The Biochemical journal 2000;349;Pt 1;159-67

  • The human cadherin-10 gene: complete coding sequence, predominant expression in the brain, and mapping on chromosome 5p13-14.

    Kools P, Vanhalst K, Van den Eynde E and van Roy F

    Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology (VIB)-University of Ghent, Belgium.

    In a quest for novel cadherin gene family members in the human dbEST database, an interesting EST clone was identified and chosen for subsequent analysis. Using the technique of 5' rapid amplification of cDNA ends, we isolated the complete coding sequence and a large part of the UTRs of a novel gene. The sequence appeared to correspond to the human cadherin-10 gene, whose sequence was only partially known before. The expression pattern of this cadherin was found to be largely brain-specific, with additional expression in both adult and fetal kidney, and with minor expression in prostate and fetal lung. By FISH analysis the genomic location was determined at human chromosome 5p13-14, which is nearby the reported positions of the human cadherin-6, -12, and cadherin-14 (CDH18) genes. Cadherin-10 shows high relationship to the human cadherin-6 gene.

    FEBS letters 1999;452;3;328-34

  • Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion.

    Ali J, Liao F, Martens E and Muller WA

    Department of Cell Physiology and Immunology, Rockefeller University, New York, USA.

    Objective: To identify proteins responsible for intercellular junction integrity in human umbilical vein endothelial cells (HUVEC), we produced a monoclonal antibody that recognized an endothelial cell-specific, junctionally restricted protein. We characterized and cloned the antigen to study its functional properties.

    Methods: The size and cellular distribution of the antigen were determined by immunofluorescence and immunoprecipitation. The molecule was cloned and transfected into cell lines, and its role in cell-cell adhesion and growth rate was determined.

    Results: Monoclonal antibody hec1 recognizes VE-cadherin, an endothelial cell-restricted cell adhesion molecule. VE-cadherin is localized to the borders between apposing endothelial cells but is diffusely distributed on subconfluent or migrating cells. Transfection of fibroblasts with VE-cadherin imparts to them the ability to adhere to each other in a calcium-dependent homophilic manner. Expression of VE-cadherin over a several-log range does not change the growth rate of these cells.

    Conclusions: Despite the fact that VE-cadherin is a "nonclassical" cadherin by structure, it functions as a classic cadherin by imparting to cells the ability to adhere in a calcium-dependent, homophilic manner. On HUVEC it appears to play a role in maintaining monolayer integrity.

    Funded by: NHLBI NIH HHS: HL09393, HL46849

    Microcirculation (New York, N.Y. : 1994) 1997;4;2;267-77

  • E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton.

    Hülsken J, Birchmeier W and Behrens J

    Max-Delbrück-Center for Molecular Medicine, Berlin, Germany.

    beta-Catenin is involved in the formation of adherens junctions of mammalian epithelia. It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of beta-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of beta-catenin; the NH2-terminal domain of beta-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to alpha-catenin. Plakoglobin (gamma-catenin), which is structurally related to beta-catenin, mediates identical interactions. We thus show that the APC tumor suppressor gene product forms strikingly similar associations as found in cell junctions and suggest that beta-catenin and plakoglobin are central regulators of cell adhesion, cytoskeletal interaction, and tumor suppression.

    The Journal of cell biology 1994;127;6 Pt 2;2061-9

  • Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.

    Suzuki S, Sano K and Tanihara H

    Department of Ophthalmology, University of Southern California, School of Medicine, Los Angeles 90033.

    To examine the diversity of the cadherin family, we isolated cDNAs from brain and retina cDNA preparations with the aid of polymerase chain reaction. The products obtained included cDNAs for two of three known cadherins as well as eight distinct cDNAs, of which deduced amino acid sequences show significant similarity with the known cadherin sequences. Larger cDNA clones were isolated from human cDNA libraries for six of the eight new molecules. The deduced amino acid sequences show that the overall structure of these molecules is very similar to that of the known cadherins, indicating that these molecules are new members of the cadherin family. We have tentatively designated these cadherins as cadherin-4 through -11. The new molecules, with the exception of cadherin-4, exhibit features that distinguish them as a group from previously cloned cadherins; they may belong to a new subfamily of cadherins. Northern blot analysis showed that most of these cadherins are expressed mainly in brain, although some are expressed in other tissues as well. These findings show that the cadherin family of adhesion molecules is much larger than previously thought, and suggest that the new cadherins may play an important role in cell-cell interactions within the central nervous system.

    Funded by: NEI NIH HHS: EY-08106

    Cell regulation 1991;2;4;261-70

Gene lists (5)

Gene List Source Species Name Description Gene count
L00000009 G2C Homo sapiens Human PSD Human orthologues of mouse PSD adapted from Collins et al (2006) 1080
L00000016 G2C Homo sapiens Human PSP Human orthologues of mouse PSP adapted from Collins et al (2006) 1121
L00000061 G2C Homo sapiens BAYES-COLLINS-MOUSE-PSD-CONSENSUS Mouse cortex PSD consensus (ortho) 984
L00000069 G2C Homo sapiens BAYES-COLLINS-HUMAN-PSD-FULL Human cortex biopsy PSD full list 1461
L00000071 G2C Homo sapiens BAYES-COLLINS-MOUSE-PSD-FULL Mouse cortex PSD full list (ortho) 1556
© G2C 2014. The Genes to Cognition Programme received funding from The Wellcome Trust and the EU FP7 Framework Programmes:
EUROSPIN (FP7-HEALTH-241498), SynSys (FP7-HEALTH-242167) and GENCODYS (FP7-HEALTH-241995).

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