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Claudin 9

CLDN9, Claudin-9, nmf329
This gene encodes a member of the claudin family. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions. This protein is one of the entry cofactors for hepatitis C virus. Mouse studies revealed that this gene is required for the preservation of sensory cells in the hearing organ and the gene deficiency is associated with deafness. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: claudin-6, claudin-1, claudin-4, claudin-3, HAD
Papers on CLDN9
A spontaneous metastasis model reveals the significance of claudin-9 overexpression in lung cancer metastasis.
Haribabu et al., Louisville, United States. In Clin Exp Metastasis, Jan 2016
Microarray analysis of 3LL and p-3LL cells as well as the primary tumors derived from these cells revealed altered expression of several genes including significant upregulation of a tight junction protein, claudin-9.
Selection of a hepatitis C virus with altered entry factor requirements reveals a genetic interaction between the E1 glycoprotein and claudins.
Evans et al., New York City, United States. In Hepatology, Oct 2015
Indeed, CLDN1/CLDN6 double-KO Huh-7.5 cells supported infection by the mutant virus only when CLDN1, CLDN6, or CLDN9 was expressed.
Expression of claudin-5, -7, -8 and -9 in cervical carcinoma tissues and adjacent non-neoplastic tissues.
Wang et al., Zibo, China. In Int J Clin Exp Pathol, 2014
The positive expression rates of claudin-9 in cervical carcinoma tissues and adjacent non-neoplastic tissues were 38.9% and 56.9% respectively (P < 0.05).
Overexpression of the cell adhesion molecule claudin-9 is associated with invasion in pituitary oncocytomas.
Zhang et al., Beijing, China. In Hum Pathol, 2014
The most significantly altered gene, claudin-9 (CLDN9), was further confirmed by quantitative real-time polymerase chain reaction, Western blot, and immunohistochemical staining in 10 invasive pituitary oncocytoma samples and 10 noninvasive pituitary oncocytoma samples.
Isolate-dependent use of claudins for cell entry by hepatitis C virus.
Pietschmann et al., In Hepatology, 2014
In addition, CLDN6 and CLDN9 have been shown to substitute for CLDN1 as HCV entry factors in human nonliver cells.
Deafness in occludin-deficient mice with dislocation of tricellulin and progressive apoptosis of the hair cells.
Tsukita et al., Kyoto, Japan. In Biol Open, 2013
These phenotypes of Occ(-/-) mice are very similar with those of claudin-14 or claudin-9 deficient mice, leading us to speculate on the existence of imbalance induced by TJ abnormalities, such as localized ionic components.
Functional analysis of claudin-6 and claudin-9 as entry factors for hepatitis C virus infection of human hepatocytes by using monoclonal antibodies.
Baumert et al., Strasbourg, France. In J Virol, 2013
The relevance of claudin-6 and claudin-9 in hepatitis C virus (HCV) entry remains elusive.
Complexity and developmental changes in the expression pattern of claudins at the blood-CSF barrier.
Ghersi-Egea et al., Lyon, France. In Histochem Cell Biol, 2012
It differed from the adult pattern in that the pore-forming claudin-2, claudin-9, and claudin-22 increased during development, while claudin-3 and claudin-6 decreased.
Innate immunity and non-Hodgkin's lymphoma (NHL) related genes in a nested case-control study for gastric cancer risk.
Kang et al., Seoul, South Korea. In Plos One, 2011
Six significant SNPs in four innate immunity (DEFA6, DEFB1, JAK3, and ACAA1) and 11 SNPs in nine NHL-related genes (INSL3, CHMP7, BCL2L11, TNFRSF8, RAD50, CASP7, CHUK, CD79B, and CLDN9) with a permutated p-value <0.01 were re-genotyped in the Replication phase among 386 cases and 348 controls.
Claudin-6, 7, or 9 overexpression in the human gastric adenocarcinoma cell line AGS increases its invasiveness, migration, and proliferation rate.
Rendon-Huerta et al., Mexico. In Cancer Invest, 2011
Increased expression of claudin-6, claudin-7, or claudin-9 is sufficient to enhance tumorigenic properties of a gastric adenocarcinoma cell line.
Characterization and evaluation of the antitumour activity of a dual-targeting monoclonal antibody against claudin-3 and claudin-4.
Ando et al., Tokyo, Japan. In Anticancer Res, 2010
RESULTS: A monoclonal antibody, KM3907 (IgG2a), which recognised CLDN3 and CLDN4, but not CLDN5, CLDN6 and CLDN9, was successfully isolated.
Distribution and expression pattern of claudins 6, 7, and 9 in diffuse- and intestinal-type gastric adenocarcinomas.
Montaño et al., Mexico. In J Gastrointest Cancer, 2010
Claudins 6, 7, and 9 expressions are closely related to gastric carcinogenesis.
Inhibition of basal p38 or JNK activity enhances epithelial barrier function through differential modulation of claudin expression.
Montesano et al., Genève, Switzerland. In Am J Physiol Cell Physiol, 2009
Silencing of either JNK1 or JNK2 increased claudin-9 mRNA expression while decreasing claudin-8 mRNA.
A claudin-9-based ion permeability barrier is essential for hearing.
Bánfi et al., Iowa City, United States. In Plos Genet, 2009
Claudin-9 is required for the preservation of sensory cells in the hearing organ.
Prevention of murine experimental corneal trauma by epigenetic events regulating claudin 6 and claudin 9.
Ohguro et al., Sapporo, Japan. In Jpn J Ophthalmol, 2008
RESULTS: Treatment with epigenetic regulators such as TSA, 5-aza, and DMSO significantly enhanced the expression of TJ-associated genes such as claudin 6 and claudin 9 in corneal cells, changing transcriptional signals by demethylating CpG islands.
The tight junction proteins claudin-1, -6, and -9 are entry cofactors for hepatitis C virus.
Dragic et al., United States. In J Virol, 2008
claudin-6 and claudin-9 expressed in CD81+ cells also enable the entry of HCV pseudoparticles derived from six of the major genotypes.
Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus.
Deng et al., Beijing, China. In J Virol, 2007
Residues N38 and V45 in the first extracellular loop (EL1) of CLDN9 are necessary for HCV entry.
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