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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/06/05 14:20:38」(JST)
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Junction plakoglobin |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
3IFQ
|
|
|
Identifiers |
Symbols |
JUP ; ARVD12; CTNNG; DP3; DPIII; PDGB; PKGB |
External IDs |
OMIM: 173325 MGI: 96650 HomoloGene: 1680 GeneCards: JUP Gene |
Gene ontology |
Molecular function |
• transcription coactivator activity
• structural molecule activity
• structural constituent of cell wall
• protein binding
• protein kinase binding
• protein phosphatase binding
• protein homodimerization activity
• alpha-catenin binding
• cadherin binding
|
Cellular component |
• nucleus
• transcription factor complex
• cytoplasm
• cytosol
• cytoskeleton
• intermediate filament
• plasma membrane
• cell-cell junction
• cell-cell adherens junction
• zonula adherens
• fascia adherens
• cytoplasmic side of plasma membrane
• intercalated disc
• actin cytoskeleton
• basolateral plasma membrane
• apicolateral plasma membrane
• lateral plasma membrane
• catenin complex
• Z disc
• hemidesmosome
• desmosome
• protein-DNA complex
• extracellular vesicular exosome
• gamma-catenin-TCF7L2 complex
|
Biological process |
• negative regulation of transcription from RNA polymerase II promoter
• cell morphogenesis
• desmosome assembly
• negative regulation of heart induction by canonical Wnt signaling pathway
• atrioventricular valve morphogenesis
• negative regulation of Wnt signaling pathway involved in heart development
• cytoskeletal anchoring at plasma membrane
• gastrulation
• ectoderm development
• nervous system development
• morphogenesis of embryonic epithelium
• single organismal cell-cell adhesion
• cell migration
• cell junction assembly
• adherens junction organization
• regulation of cell proliferation
• positive regulation of protein import into nucleus
• skin development
• cell-cell junction organization
• oocyte development
• detection of mechanical stimulus
• positive regulation of sequence-specific DNA binding transcription factor activity
• protein heterooligomerization
• endothelial cell-cell adhesion
• cellular response to indole-3-methanol
• ventricular cardiac muscle cell action potential
• bundle of His cell to Purkinje myocyte communication
• regulation of heart rate by cardiac conduction
• establishment of protein localization to plasma membrane
• positive regulation of canonical Wnt signaling pathway
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
|
Entrez |
3728 |
16480 |
|
Ensembl |
ENSG00000173801 |
ENSMUSG00000001552 |
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UniProt |
P14923 |
Q02257 |
|
RefSeq (mRNA) |
NM_002230 |
NM_010593 |
|
RefSeq (protein) |
NP_002221 |
NP_034723 |
|
Location (UCSC) |
Chr 17:
39.78 – 39.94 Mb |
Chr 11:
100.37 – 100.4 Mb |
|
PubMed search |
[1] |
[2] |
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Junction plakoglobin, also known as gamma-catenin or JUP, is a protein that in humans is encoded by the JUP gene.[1] It is a member of the catenin protein family and homologous to β-catenin.
Contents
- 1 Function
- 2 Clinical significance
- 3 Interactions
- 4 See also
- 5 References
- 6 Further reading
- 7 External links
Function
This gene encodes a major cytoplasmic protein that is the only known constituent common to submembranous plaques of both desmosomes and intermediate junctions. This protein forms distinct complexes with cadherins and desmosomal cadherins and is a member of the catenin family, since it contains a distinct repeating amino acid motif called the armadillo repeat.[1]
Plakoglobin (gamma-catenin) was originally identified as a component of desmosomes, where it can bind to the cadherin family member desmoglein I. Plakoglobin also associates with classical cadherins such as E-cadherin; in that context, it was called gamma-catenin. Plakoglobin is O-glycosylated near its N-terminal destruction box.
Clinical significance
Mutation of the gene encoding plakoglobin has been implicated as one of the causes of the cardiomyopathy known as arrhythmogenic right ventricular dysplasia (ARVD).[2] The form of ARVD in which a mutated form of plakoglobin is present was first identified in a small cluster of families on the Greek island of Naxos. This form of the disorder is autosomal recessive. The phenotype of the Naxos variant of ARVD is unique in that it involves the hair and skin as well as the right ventricle. Affected individuals have wooly, kinky hair; there is also palmar and plantar erythema at birth that progresses to keratosis as the palms and soles of the feet are used in crawling and walking. These findings co-segregate 100% with the development of ARVD by early adolescence.
It is also implicated in Pemphigus vulgaris along with genes encoding for Desmoglein 1 and 3.
Interactions
Plakoglobin has been shown to interact with:
- APC,[3][4]
- CTNNA1,[5][6][7]
- CTNNB1,[8][9]
- CDH1,[3][8][10][11][12]
- CDH2,[5][13]
- CDH3,[14]
- CDH5,[15][16]
- DSG2,[17][18][19]
- DSP,[20][21]
- MUC1,[22]
- PKP2,[23]
- PTPkappa (PTPRK),[24] and
- PTPrho (PTPRT).[25]
See also
- Catenin
- List of conditions caused by problems with junctional proteins
References
- ^ a b "Entrez Gene: JUP junction plakoglobin".
- ^ Garcia-Gras E, Lombardi R, Giocondo MJ, Willerson JT, Schneider MD, Khoury DS, Marian AJ (July 2006). "Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy". J. Clin. Invest. 116 (7): 2012–21. doi:10.1172/JCI27751. PMC 1483165. PMID 16823493.
- ^ a b Shibata T, Gotoh M, Ochiai A, Hirohashi S (August 1994). "Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 203 (1): 519–22. doi:10.1006/bbrc.1994.2213. PMID 8074697.
- ^ Daniel JM, Reynolds A B (September 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819–24. PMC 230726. PMID 7651399.
- ^ a b Sacco PA, McGranahan T M, Wheelock M J, Johnson K R (August 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): 20201–6. doi:10.1074/jbc.270.34.20201. PMID 7650039.
- ^ Roe S, Koslov E R, Rimm D L (June 1998). "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity". Cell Adhes. Commun. 5 (4): 283–96. doi:10.3109/15419069809040298. PMID 9762469.
- ^ Obama H, Ozawa M (April 1997). "Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin)". J. Biol. Chem. 272 (17): 11017–20. doi:10.1074/jbc.272.17.11017. PMID 9110993.
- ^ a b Hazan RB, Norton L (April 1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton". J. Biol. Chem. 273 (15): 9078–84. doi:10.1074/jbc.273.15.9078. PMID 9535896.
- ^ Kucerová D, Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (December 2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. 8 (6): 695–8. doi:10.3892/ijmm.8.6.695. PMID 11712088.
- ^ Kinch MS, Clark G J, Der C J, Burridge K (July 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. 130 (2): 461–71. doi:10.1083/jcb.130.2.461. PMC 2199929. PMID 7542250.
- ^ Hinck L, Näthke I S, Papkoff J, Nelson W J (June 1994). "Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly". J. Cell Biol. 125 (6): 1327–40. doi:10.1083/jcb.125.6.1327. PMC 2290923. PMID 8207061.
- ^ Knudsen KA, Wheelock M J (August 1992). "Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin". J. Cell Biol. 118 (3): 671–9. doi:10.1083/jcb.118.3.671. PMC 2289540. PMID 1639850.
- ^ Straub BK, Boda Judit, Kuhn Caecilia, Schnoelzer Martina, Korf Ulrike, Kempf Tore, Spring Herbert, Hatzfeld Mechthild, Franke Werner W (December 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. 116 (Pt 24): 4985–95. doi:10.1242/jcs.00815. PMID 14625392.
- ^ Klingelhöfer J, Troyanovsky R B, Laur O Y, Troyanovsky S (August 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". J. Cell. Sci. 113 (16): 2829–36. PMID 10910767.
- ^ Lewalle JM, Bajou K, Desreux J, Mareel M, Dejana E, Noël A, Foidart J M (December 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. 237 (2): 347–56. doi:10.1006/excr.1997.3799. PMID 9434630.
- ^ Shasby DM, Ries Dana R, Shasby Sandra S, Winter Michael C (June 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (6): L1330–8. doi:10.1152/ajplung.00329.2001. PMID 12003790.
- ^ Bannon LJ, Cabrera B L, Stack M S, Green K J (November 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin complexes". J. Invest. Dermatol. 117 (5): 1302–6. doi:10.1046/j.1523-1747.2001.01512.x. PMID 11710948.
- ^ "The amino- and carboxyl-terminal tails of (beta)-catenin reduce its affinity for desmoglein 2". J. Cell. Sci. 113 (10): 1737–45. May 2000. PMID 10769205.
- ^ Ozawa M, Terada H, Pedraza C (November 1995). "The fourth armadillo repeat of plakoglobin (gamma-catenin) is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor suppressor APC protein". J. Biochem. 118 (5): 1077–82. doi:10.1093/jb/118.5.1077. PMID 8749329.
- ^ Kowalczyk AP, Navarro P, Dejana E, Bornslaeger E A, Green K J, Kopp D S, Borgwardt J E (October 1998). "VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions". J. Cell. Sci. 111 (20): 3045–57. PMID 9739078.
- ^ Kowalczyk AP, Bornslaeger E A, Borgwardt J E, Palka H L, Dhaliwal A S, Corcoran C M, Denning M F, Green K J (November 1997). "The Amino-terminal Domain of Desmoplakin Binds to Plakoglobin and Clusters Desmosomal Cadherin–Plakoglobin Complexes". J. Cell Biol. 139 (3): 773–84. doi:10.1083/jcb.139.3.773. PMC 2141713. PMID 9348293.
- ^ Li Y, Yu Wei-Hsuan, Ren Jian, Chen Wen, Huang Lei, Kharbanda Surender, Loda Massimo, Kufe Donald (August 2003). "Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein". Mol. Cancer Res. 1 (10): 765–75. PMID 12939402.
- ^ Chen X, Bonne Stefan, Hatzfeld Mechthild, van Roy Frans, Green Kathleen J (March 2002). "Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling". J. Biol. Chem. 277 (12): 10512–22. doi:10.1074/jbc.M108765200. PMID 11790773.
- ^ Fuchs M, Müller T, Lerch M M, Ullrich A (July 1996). "Association of human protein-tyrosine phosphatase kappa with members of the armadillo family". J. Biol. Chem. 271 (28): 16712–9. doi:10.1074/jbc.271.28.16712. PMID 8663237.
- ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135.
Further reading
- Cowin P, Kapprell HP, Franke WW, Tamkun J, Hynes RO (September 1986). "Plakoglobin: a protein common to different kinds of intercellular adhering junctions". Cell 46 (7): 1063–73. doi:10.1016/0092-8674(86)90706-3. PMID 3530498.
- Franke WW, Goldschmidt MD, Zimbelmann R, Mueller HM, Schiller DL, Cowin P (June 1989). "Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein". Proc. Natl. Acad. Sci. U.S.A. 86 (11): 4027–31. doi:10.1073/pnas.86.11.4027. PMC 287381. PMID 2726765.
- Mathur M, Goodwin L, Cowin P (May 1994). "Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin". J. Biol. Chem. 269 (19): 14075–80. PMID 8188687.
- Beavon IR (2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation". Eur. J. Cancer 36 (13 Spec No): 1607–20. doi:10.1016/S0959-8049(00)00158-1. PMID 10959047.
- Wilson PD (2001). "Polycystin: new aspects of structure, function, and regulation". J. Am. Soc. Nephrol. 12 (4): 834–45. PMID 11274246.
- Protonotarios NI, Tsatsopoulou AA, Gatzoulis KA (2002). "Arrhythmogenic right ventricular cardiomyopathy caused by a deletion in plakoglobin (Naxos disease)". Cardiac electrophysiology review 6 (1–2): 72–80. doi:10.1023/A:1017943323473. PMID 11984022.
- Knudsen KA, Wheelock MJ (1992). "Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin". J. Cell Biol. 118 (3): 671–9. doi:10.1083/jcb.118.3.671. PMC 2289540. PMID 1639850.
- Arnemann J, Spurr NK, Wheeler GN, Parker AE, Buxton RS (1991). "Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and plakoglobin DPIII (JUP)". Genomics 10 (3): 640–5. doi:10.1016/0888-7543(91)90446-L. PMID 1889810.
- Kinch MS, Clark GJ, Der CJ, Burridge K (1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. 130 (2): 461–71. doi:10.1083/jcb.130.2.461. PMC 2199929. PMID 7542250.
- Aberle H, Bierkamp C, Torchard D, Serova O, Wagner T, Natt E, Wirsching J, Heidkämper C, Montagna M, Lynch HT et al. (1995). "The human plakoglobin gene localizes on chromosome 17q21 and is subjected to loss of heterozygosity in breast and ovarian cancers". Proc. Natl. Acad. Sci. U.S.A. 92 (14): 6384–8. doi:10.1073/pnas.92.14.6384. PMC 41522. PMID 7604000.
- Sacco PA, McGranahan TM, Wheelock MJ, Johnson KR (1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): 20201–6. doi:10.1074/jbc.270.34.20201. PMID 7650039.
- Daniel JM, Reynolds AB (1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819–24. PMC 230726. PMID 7651399.
- Kanai Y, Ochiai A, Shibata T, Oyama T, Ushijima S, Akimoto S, Hirohashi S (1995). "c-erbB-2 gene product directly associates with beta-catenin and plakoglobin". Biochem. Biophys. Res. Commun. 208 (3): 1067–72. doi:10.1006/bbrc.1995.1443. PMID 7702605.
- Roh JY, Stanley JR (1995). "Plakoglobin binding by human Dsg3 (pemphigus vulgaris antigen) in keratinocytes requires the cadherin-like intracytoplasmic segment". J. Invest. Dermatol. 104 (5): 720–4. doi:10.1111/1523-1747.ep12606963. PMID 7738346.
- Shibamoto S, Hayakawa M, Takeuchi K, Hori T, Miyazawa K, Kitamura N, Johnson KR, Wheelock MJ, Matsuyoshi N, Takeichi M et al. (1995). "Association of p120, a tyrosine kinase substrate, with E- cadherin/catenin complexes". J. Cell Biol. 128 (5): 949–57. doi:10.1083/jcb.128.5.949. PMC 2120395. PMID 7876318.
- Rubinfeld B, Souza B, Albert I, Munemitsu S, Polakis P (1995). "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin". J. Biol. Chem. 270 (10): 5549–55. doi:10.1074/jbc.270.10.5549. PMID 7890674.
- Troyanovsky SM, Troyanovsky RB, Eshkind LG, Leube RE, Franke WW (1994). "Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation". Proc. Natl. Acad. Sci. U.S.A. 91 (23): 10790–4. doi:10.1073/pnas.91.23.10790. PMC 45111. PMID 7971964.
- Shibata T, Gotoh M, Ochiai A, Hirohashi S (1994). "Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 203 (1): 519–22. doi:10.1006/bbrc.1994.2213. PMID 8074697.
- Hinck L, Näthke IS, Papkoff J, Nelson WJ (1994). "Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly". J. Cell Biol. 125 (6): 1327–40. doi:10.1083/jcb.125.6.1327. PMC 2290923. PMID 8207061.
- Arnemann J, Sullivan KH, Magee AI, King IA, Buxton RS (1993). "Stratification-related expression of isoforms of the desmosomal cadherins in human epidermis". J. Cell. Sci. 104 (3): 741–50. PMID 8314871.
- Ozawa M, Nuruki K, Toyoyama H, Ohi Y (1996). "Cloning of an alternative form of plakoglobin (gamma-catenin) lacking the fourth armadillo repeat". J. Biochem. 118 (4): 836–40. PMID 8576101.
- Fuchs M, Müller T, Lerch MM, Ullrich A (1996). "Association of human protein-tyrosine phosphatase kappa with members of the armadillo family". J. Biol. Chem. 271 (28): 16712–9. doi:10.1074/jbc.271.28.16712. PMID 8663237.
External links
- GeneReviews/NCBI/NIH/UW entry on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant
- OMIM entries on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant
- gamma-Catenin at the US National Library of Medicine Medical Subject Headings (MeSH)
Proteins of the cytoskeleton
|
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Human |
|
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Nonhuman |
- Major sperm proteins
- Prokaryotic cytoskeleton
|
|
See also: cytoskeletal defects
Index of cells
|
|
Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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|
Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
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Histology: Epithelial proteins (TH H1.00.01.1)
|
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Lateral/cell-cell |
- Cell adhesion molecules: Adherens junction
- Desmosome
- Ion channels: Gap junction/Connexon
- Cytoskeleton: Desmosome
- Desmoplakin
- Plakoglobin
- Tonofibril
- other membrane proteins: Tight junction
- Claudin
- Occludin
- MARVELD2
|
|
Basal/cell-matrix |
- Basal lamina
- Hemidesmosome/Tonofibril
- Focal adhesion
- Costamere
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Apical |
- Cilia/Kinocilium
- Microvilli/Stereocilia (STRC)
|
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Index of cells
|
|
Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
|
|
Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
|
|
|
UpToDate Contents
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English Journal
- Mesenchymal-epithelial transitions: Spontaneous and cumulative syntheses of epithelial marker molecules and their assemblies to novel cell junctions connecting human hematopoietic tumor cells to carcinomatoid tissue structures.
- Franke WW, Rickelt S.SourceHelmholtz Group for Cell Biology, German Cancer Research Center, Heidelberg, Germany. w.franke@dkfz.de.
- International journal of cancer. Journal international du cancer.Int J Cancer.2011 Dec 1;129(11):2588-99. doi: 10.1002/ijc.26227. Epub 2011 Aug 17.
- Using biochemical as well as light- and electron-microscopic immunolocalization methods, in cultures of unicellular human blood tumor cells, we have studied the phenomenon of spontaneous and cumulative syntheses of certain epithelial proteins and glycoproteins and their assemblies to two major kinds
- PMID 21647878
- Recombinant WNTs differentially activate β-catenin-dependent and -independent signalling in mouse microglia-like cells.
- Kilander MB, Halleskog C, Schulte G.SourceSection Receptor Biology & Signalling, Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
- Acta physiologica (Oxford, England).Acta Physiol (Oxf).2011 Nov;203(3):363-72. doi: 10.1111/j.1748-1716.2011.02324.x. Epub 2011 Jun 20.
- Aim:? The objective of this study was to compare the efficacy of different recombinant, commercially available Wingless/Int-1 (WNTs) with regard to WNT/β-catenin signalling, dishevelled (DVL) and G protein activation and the induction of cell proliferation in a microglia-like cell line called N13
- PMID 21557822
Japanese Journal
- Heterogeneous and abnormal localization of desmosomal proteins in oral intraepithelial neoplasms
- Aizawa Sohichi,Ochiai Takanaga,Ara Toshiaki,Yamada Haruki,Hasegawa Hiromasa
- Journal of Oral Science 56(3), 209-214, 2014
- … All samples were stained using antibodies against desmoglein 1 (DSG1), desmocollin 3 (DSC3), junction plakoglobin (JUP) and serine peptidase inhibitor Kazal type 5 (SPINK5) domain. …
- NAID 130004691130
- 心筋症について : 最近明らかになってきたこと (特集 心筋疾患に対するアプローチ)
- Compound and Digenic Heterozygosity in Desmosome Genes as a Cause of Arrhythmogenic Right Ventricular Cardiomyopathy in Japanese Patients
- NAKAJIMA Tadashi,KANEKO Yoshiaki,IRIE Tadanobu,TAKAHASHI Rieko,KATO Toshimitsu,IIJIMA Takafumi,ISO Tatsuya,KURABAYASHI Masahiko
- Circulation journal : official journal of the Japanese Circulation Society 76(3), 737-743, 2012-02-25
- … Genetic screening for major ARVC-causing genes (junction plakoglobin, desmoplakin, plakophilin-2 (PKP2), desmoglein-2 (DSG2), and desmocollin-2) was performed. …
- NAID 10030130444
Related Links
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