AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation Science
ClaudinsClaudin-3Claudin-4Tight JunctionsClaudin-1OccludinClaudin-5Membrane ProteinsZonula Occludens-2 ProteinClaudin-2MARVEL Domain Containing 2 ProteinZonula Occludens-1 ProteinZonula Occludens ProteinsClostridium perfringensPermeabilityEpithelial CellsTight Junction ProteinsNephronsLoop of HenleDogsMadin Darby Canine Kidney CellsElectric ImpedanceCell Membrane PermeabilityJunctional Adhesion MoleculesKeratosis, ActinicFreeze FracturingPubMedPeriodicals as TopicBooksPublishingMEDLINENeoplastic Stem CellsGap JunctionsDesmoplakinsDesmosomesIntercellular JunctionsBlood-Brain BarrierEndothelial CellsBrainNeural CrestMolecular BiologySnailsTranscription FactorsMesodermColorectal NeoplasmsHyperammonemiaStem Cell FactorHematopoietic Cell Growth FactorsProto-Oncogene Proteins c-kit
Claudins
A large family of transmembrane proteins found in TIGHT JUNCTIONS. They take part in the formation of paracellular barriers and pores that regulate paracellular permeability.
Claudin-3
A ubiquitously-expressed claudin subtype that acts as a general barrier-forming protein in TIGHT JUNCTIONS. Elevated expression of claudin-3 is found in a variety of tumor cell types, suggesting its role as a therapeutic target for specific ANTINEOPLASTIC AGENTS.
Claudin-4
A claudin subtype that takes part in maintaining the barrier-forming property of TIGHT JUNCTIONS. Claudin-4 is found associated with CLAUDIN-8 in the KIDNEY COLLECTING DUCT where it may play a role in paracellular chloride ion reabsorption.
Tight Junctions
Cell-cell junctions that seal adjacent epithelial cells together, preventing the passage of most dissolved molecules from one side of the epithelial sheet to the other. (Alberts et al., Molecular Biology of the Cell, 2nd ed, p22)
Claudin-1
An integral membrane protein that is localized to TIGHT JUNCTIONS, where it plays a role in controlling the paracellular permeability of polarized cells. Mutations in the gene for claudin-1 are associated with Neonatal Ichthyosis-Sclerosing Cholangitis (NISCH) Syndrome.
Occludin
A MARVEL domain protein that plays an important role in the formation and regulation of the TIGHT JUNCTION paracellular permeability barrier.
Claudin-5
A claudin subtype that is found localized to TIGHT JUNCTIONS in VASCULAR ENDOTHELIAL CELLS. The protein was initially identified as one of several proteins which are deleted in VELOCARDIOFACIAL SYNDROME and may play an important role in maintaining the integrity of the BLOOD-BRAIN BARRIER.
Membrane Proteins
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Zonula Occludens-2 Protein
A zonula occludens protein subtype found in epithelial cell junctions. Several isoforms of zonula occludens-2 protein exist due to use of alternative promoter regions and alternative mRNA splicings.
Claudin-2
A claudin subtype that is associated with the formation of cation-selective channels and increased epithelial permeability. It is localized to the TIGHT JUNCTIONS of the PROXIMAL KIDNEY TUBULE and INTESTINAL EPITHELIUM.
MARVEL Domain Containing 2 Protein
A tight junction-associated MARVEL protein that may play a role in separating the endolymphatic and perilymphatic spaces of the ORGAN OF CORTI. Defects in the gene that codes for MARVELD2 protein are a cause of deafness autosomal recessive type 49.
Zonula Occludens-1 Protein
A 195-kDa zonula occludens protein that is distinguished by the presence of a ZU5 domain at the C-terminal of the molecule.
Zonula Occludens Proteins
A family of proteins that play a role in TIGHT JUNCTION formation by binding to and anchoring proteins to the ACTIN CYTOSKELETON.
Clostridium perfringens
The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins.
Permeability
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
Epithelial Cells
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Tight Junction Proteins
Proteins that take part in the formation or structure of TIGHT JUNCTIONS.
Nephrons
The functional units of the kidney, consisting of the glomerulus and the attached tubule.
Loop of Henle
The U-shaped portion of the renal tubule in the KIDNEY MEDULLA, consisting of a descending limb and an ascending limb. It is situated between the PROXIMAL KIDNEY TUBULE and the DISTAL KIDNEY TUBULE.
Dogs
The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)
Madin Darby Canine Kidney Cells
An epithelial cell line derived from a kidney of a normal adult female dog.
Electric Impedance
The resistance to the flow of either alternating or direct electrical current.
Cell Membrane Permeability
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
Junctional Adhesion Molecules
A family of membrane glycoproteins localized to TIGHT JUNCTIONS that contain two extracellular Ig-like domains, a single transmembrane segment, and a cytoplasmic tail of variable length.
Keratosis, Actinic
White or pink lesions on the arms, hands, face, or scalp that arise from sun-induced DNA DAMAGE to KERATINOCYTES in exposed areas. They are considered precursor lesions to superficial SQUAMOUS CELL CARCINOMA.
Freeze Fracturing
Preparation for electron microscopy of minute replicas of exposed surfaces of the cell which have been ruptured in the frozen state. The specimen is frozen, then cleaved under high vacuum at the same temperature. The exposed surface is shadowed with carbon and platinum and coated with carbon to obtain a carbon replica.
PubMed
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
Periodicals as Topic
A publication issued at stated, more or less regular, intervals.
Books
Publishing
"The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.
MEDLINE
The premier bibliographic database of the NATIONAL LIBRARY OF MEDICINE. MEDLINE® (MEDLARS Online) is the primary subset of PUBMED and can be searched on NLM's Web site in PubMed or the NLM Gateway. MEDLINE references are indexed with MEDICAL SUBJECT HEADINGS (MeSH).
Neoplastic Stem Cells
Highly proliferative, self-renewing, and colony-forming stem cells which give rise to NEOPLASMS.
Gap Junctions
Connections between cells which allow passage of small molecules and electric current. Gap junctions were first described anatomically as regions of close apposition between cells with a narrow (1-2 nm) gap between cell membranes. The variety in the properties of gap junctions is reflected in the number of CONNEXINS, the family of proteins which form the junctions.
Desmoplakins
Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.
Desmosomes
A type of junction that attaches one cell to its neighbor. One of a number of differentiated regions which occur, for example, where the cytoplasmic membranes of adjacent epithelial cells are closely apposed. It consists of a circular region of each membrane together with associated intracellular microfilaments and an intercellular material which may include, for example, mucopolysaccharides. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990; Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Intercellular Junctions
Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)
Blood-Brain Barrier
Specialized non-fenestrated tightly-joined ENDOTHELIAL CELLS with TIGHT JUNCTIONS that form a transport barrier for certain substances between the cerebral capillaries and the BRAIN tissue.
Endothelial Cells
Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.
Brain
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
Neural Crest
The two longitudinal ridges along the PRIMITIVE STREAK appearing near the end of GASTRULATION during development of nervous system (NEURULATION). The ridges are formed by folding of NEURAL PLATE. Between the ridges is a neural groove which deepens as the fold become elevated. When the folds meet at midline, the groove becomes a closed tube, the NEURAL TUBE.
Molecular Biology
A discipline concerned with studying biological phenomena in terms of the chemical and physical interactions of molecules.
Snails
Marine, freshwater, or terrestrial mollusks of the class Gastropoda. Most have an enclosing spiral shell, and several genera harbor parasites pathogenic to man.
Transcription Factors
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Mesoderm
The middle germ layer of an embryo derived from three paired mesenchymal aggregates along the neural tube.
Colorectal Neoplasms
Tumors or cancer of the COLON or the RECTUM or both. Risk factors for colorectal cancer include chronic ULCERATIVE COLITIS; FAMILIAL POLYPOSIS COLI; exposure to ASBESTOS; and irradiation of the CERVIX UTERI.
Hyperammonemia
Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.
Stem Cell Factor
A hematopoietic growth factor and the ligand of the cell surface c-kit protein (PROTO-ONCOGENE PROTEINS C-KIT). It is expressed during embryogenesis and is a growth factor for a number of cell types including the MAST CELLS and the MELANOCYTES in addition to the HEMATOPOIETIC STEM CELLS.
Hematopoietic Cell Growth Factors
These growth factors comprise a family of hematopoietic regulators with biological specificities defined by their ability to support proliferation and differentiation of blood cells of different lineages. ERYTHROPOIETIN and the COLONY-STIMULATING FACTORS belong to this family. Some of these factors have been studied and used in the treatment of chemotherapy-induced neutropenia, myelodysplastic syndromes, and bone marrow failure syndromes.
Proto-Oncogene Proteins c-kit
A protein-tyrosine kinase receptor that is specific for STEM CELL FACTOR. This interaction is crucial for the development of hematopoietic, gonadal, and pigment stem cells. Genetic mutations that disrupt the expression of PROTO-ONCOGENE PROTEINS C-KIT are associated with PIEBALDISM, while overexpression or constitutive activation of the c-kit protein-tyrosine kinase is associated with tumorigenesis.

Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. (1/444)

Members of the newly identified claudin gene family constitute tight junction (TJ) strands, which play a pivotal role in compartmentalization in multicellular organisms. We identified oligodendrocyte-specific protein (OSP) as claudin-11, a new claudin family member, due to its sequence similarity to claudins as well as its ability to form TJ strands in transfected fibroblasts. Claudin-11/OSP mRNA was expressed in the brain and testis. Immunofluorescence microscopy with anti-claudin-11/OSP polyclonal antibody (pAb) and anti-neurofilament mAb revealed that in the brain claudin-11/OSP-positive linear structures run in a gentle spiral around neurofilament-positive axons. At the electron microscopic level, these linear structures were identified as the so-called interlamellar strands in myelin sheaths of oligodendrocytes. In testis, well-developed TJ strands of Sertoli cells were specifically labeled with anti-claudin-11/OSP pAb both at immunofluorescence and electron microscopic levels. These findings indicated that the interlamellar strands of oligodendrocyte myelin sheaths can be regarded as a variant of TJ strands found in many other epithelial cells, and that these strands share a specific claudin species, claudin-11/OSP, with those in Sertoli cells to create and maintain the repeated compartments around axons by oligodendrocytes.  (+info)

Transmembrane proteins in the tight junction barrier. (2/444)

Three types of transmembrane proteins have been identified within the tight junction, but it remains to be determined how they provide the molecular basis for regulating the paracellular permeability for water, solutes, and immune cells. Several of these proteins localize specifically within the continuous cell-to-cell contacts of the tight junction. One of these, occludin, is a cell adhesion molecule that has been demonstrated to influence ion and solute permeability. The claudins are a family of four-membrane spanning proteins; unexpectedly, other members of this family have already been characterized without recognizing their relationship to tight junctions. Junction adhesion molecule, the most recently identified tight junction component, is a member of the Ig superfamily and influences the paracellular transmigration of immune cells. A plaque of cytoplasmic proteins under the junction may be responsible for scaffolding the transmembrane proteins, creating a link to the perijunctional actin cytoskeleton and transducing regulatory signals that control the paracellular barrier.  (+info)

Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption. (3/444)

Epithelia permit selective and regulated flux from apical to basolateral surfaces by transcellular passage through cells or paracellular flux between cells. Tight junctions constitute the barrier to paracellular conductance; however, little is known about the specific molecules that mediate paracellular permeabilities. Renal magnesium ion (Mg2+) resorption occurs predominantly through a paracellular conductance in the thick ascending limb of Henle (TAL). Here, positional cloning has identified a human gene, paracellin-1 (PCLN-1), mutations in which cause renal Mg2+ wasting. PCLN-1 is located in tight junctions of the TAL and is related to the claudin family of tight junction proteins. These findings provide insight into Mg2+ homeostasis, demonstrate the role of a tight junction protein in human disease, and identify an essential component of a selective paracellular conductance.  (+info)

Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions. (4/444)

In multicellular organisms, various compositionally distinct fluid compartments are established by epithelial and endothelial cellular sheets. For these cells to function as barriers, tight junctions (TJs) are considered to create a primary barrier for the diffusion of solutes through the paracellular pathway [1] [2] [3]. In ultrathin sections viewed under electron microscopy, TJs appear as a series of apparent fusions, involving the outer leaflets of plasma membranes of adjacent cells, to form the so-called kissing points of TJs, where the intercellular space is completely obliterated [4]. Claudins are a family of 16 proteins whose members have been identified as major integral membrane proteins localized exclusively at TJs [5] [6] [7] [8]. It remains unclear, however, whether claudins have the cell-adhesion activity that would explain the unusual intercellular adhesion at TJs. Using mouse L-fibroblast transfectants expressing various amounts of claudin-1, -2 or -3, we found that these claudins possess Ca(2+)-independent cell-adhesion activity. Using ultrathin-section electron microscopy, we observed many kissing points of TJs between adjacent transfectants. Furthermore, the cell-adhesion activity of occludin, another integral membrane protein localized at TJs [9] [10] [11], was negligible when compared with that of claudins. Thus, claudins are responsible for TJ-specific obliteration of the intercellular space.  (+info)

Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells. (5/444)

Tight junctions (TJs) in endothelial cells are thought to determine vascular permeability. Recently, claudin-1 to -15 were identified as major components of TJ strands. Among these, claudin-5 (also called transmembrane protein deleted in velo-cardio-facial syndrome [TMVCF]) was expressed ubiquitously, even in organs lacking epithelial tissues, suggesting the possible involvement of this claudin species in endothelial TJs. We then obtained a claudin-6-specific polyclonal antibody and a polyclonal antibody that recognized both claudin-5/TMVCF and claudin-6. In the brain and lung, immunofluorescence microscopy with these polyclonal antibodies showed that claudin-5/TMVCF was exclusively concentrated at cell-cell borders of endothelial cells of all segments of blood vessels, but not at those of epithelial cells. Immunoreplica electron microscopy revealed that claudin-5/TMVCF was a component of TJ strands. In contrast, in the kidney, the claudin-5/TMVCF signal was restricted to endothelial cells of arteries, but was undetectable in those of veins and capillaries. In addition, in all other tissues we examined, claudin-5/TMVCF was specifically detected in endothelial cells of some segments of blood vessels, but not in epithelial cells. Furthermore, when claudin-5/TMVCF cDNA was introduced into mouse L fibroblasts, TJ strands were reconstituted that resembled those in endothelial cells in vivo, i.e., the extracellular face-associated TJs. These findings indicated that claudin-5/TMVCF is an endothelial cell-specific component of TJ strands.  (+info)

Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier. (6/444)

Claudins, comprising a multigene family, constitute tight junction (TJ) strands. Clostridium perfringens enterotoxin (CPE), a single approximately 35-kD polypeptide, was reported to specifically bind to claudin-3/RVP1 and claudin-4/CPE-R at its COOH-terminal half. We examined the effects of the COOH-terminal half fragment of CPE (C-CPE) on TJs in L transfectants expressing claudin-1 to -4 (C1L to C4L, respectively), and in MDCK I cells expressing claudin-1 and -4. C-CPE bound to claudin-3 and -4 with high affinity, but not to claudin-1 or -2. In the presence of C-CPE, reconstituted TJ strands in C3L cells gradually disintegrated and disappeared from their cell surface. In MDCK I cells incubated with C-CPE, claudin-4 was selectively removed from TJs with its concomitant degradation. At 4 h after incubation with C-CPE, TJ strands were disintegrated, and the number of TJ strands and the complexity of their network were markedly decreased. In good agreement with the time course of these morphological changes, the TJ barrier (TER and paracellular flux) of MDCK I cells was downregulated by C-CPE in a dose-dependent manner. These findings provided evidence for the direct involvement of claudins in the barrier functions of TJs.  (+info)

Manner of interaction of heterogeneous claudin species within and between tight junction strands. (7/444)

In tight junctions (TJs), TJ strands are associated laterally with those of adjacent cells to form paired strands to eliminate the extracellular space. Claudin-1 and -2, integral membrane proteins of TJs, reconstitute paired TJ strands when transfected into L fibroblasts. Claudins comprise a multigene family and more than two distinct claudins are coexpressed in single cells, raising the questions of whether heterogeneous claudins form heteromeric TJ strands and whether claudins interact between each of the paired strands in a heterophilic manner. To answer these questions, we cotransfected two of claudin-1, -2, and -3 into L cells, and detected their coconcentration at cell-cell borders as elaborate networks. Immunoreplica EM confirmed that distinct claudins were coincorporated into individual TJ strands. Next, two L transfectants singly expressing claudin-1, -2, or -3 were cocultured and we found that claudin-3 strands laterally associated with claudin-1 and -2 strands to form paired strands, whereas claudin-1 strands did not interact with claudin-2 strands. We concluded that distinct species of claudins can interact within and between TJ strands, except in some combinations. This mode of assembly of claudins could increase the diversity of the structure and functions of TJ strands.  (+info)

Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. (8/444)

ZO-1, ZO-2, and ZO-3, which contain three PDZ domains (PDZ1 to -3), are concentrated at tight junctions (TJs) in epithelial cells. TJ strands are mainly composed of two distinct types of four-transmembrane proteins, occludin, and claudins, between which occludin was reported to directly bind to ZO-1/ZO-2/ZO-3. However, in occludin-deficient intestinal epithelial cells, ZO-1/ZO-2/ZO-3 were still recruited to TJs. We then examined the possible interactions between ZO-1/ZO-2/ZO-3 and claudins. ZO-1, ZO-2, and ZO-3 bound to the COOH-terminal YV sequence of claudin-1 to -8 through their PDZ1 domains in vitro. Then, claudin-1 or -2 was transfected into L fibroblasts, which express ZO-1 but not ZO-2 or ZO-3. Claudin-1 and -2 were concentrated at cell-cell borders in an elaborate network pattern, to which endogenous ZO-1 was recruited. When ZO-2 or ZO-3 were further transfected, both were recruited to the claudin-based networks together with endogenous ZO-1. Detailed analyses showed that ZO-2 and ZO-3 are recruited to the claudin-based networks through PDZ2 (ZO-2 or ZO-3)/PDZ2 (endogenous ZO-1) and PDZ1 (ZO-2 or ZO-3)/COOH-terminal YV (claudins) interactions. In good agreement, PDZ1 and PDZ2 domains of ZO-1/ZO-2/ZO-3 were also recruited to claudin-based TJs, when introduced into cultured epithelial cells. The possible molecular architecture of TJ plaque structures is discussed.  (+info)

Defining the Genomic and Epigenomic Plasticity of Basal and Claudin-low Breast Cancer - UNC Lineberger Comprehensive Cancer...Defining the Genomic and Epigenomic Plasticity of Basal and Claudin-low Breast Cancer - UNC Lineberger Comprehensive Cancer...
We hypothesize that epigenetic control of gene expression in addition to genomic amplifications, deletions and mutations between basal-like and claudin-low breast cancer is a major contributor for enrichment of the claudin-low characteristics in tumors that develop resistance to therapy. We will use two models to test our hypothesis. In vivo the C3Tag GEMM phenotypically resembles triple-negative human breast cancers by gene expression profiles, and shares genetic similarities including the acquisition of KRAS gene amplification and overexpression during tumor development. C3Tag tumors treated with inhibitors of MEK, downstream of KRAS signaling, ultimately progress through therapy. Progression was accompanied by reprogramming of tumors to signal through alternative pathways, with a transformation from basal-like to claudin-low. The in vitro model is SUM229 human breast cancer cells that maintain equilibrium between two populations: one basal-like with enhanced expression of epithelial ...
http://unclineberger.org/ucrf/2013-innovation-awards/tim-elston-abstract
IJMS | Free Full-Text | Emerging Roles of Claudins in Human CancerIJMS | Free Full-Text | Emerging Roles of Claudins in Human Cancer
Claudins are major integral membrane proteins of tight junctions. Altered expression of several claudin proteins, in particular claudin-1, -3, -4 and -7, has been linked to the development of various cancers. Although their dysregulation in cancer suggests that claudins play a role in tumorigenesis, the exact underlying mechanism remains unclear. The involvement of claudins in tumor progression was suggested by their important role in the migration, invasion and metastasis of cancer cells in a tissue-dependent manner. Recent studies have shown that they play a role in epithelial to mesenchymal transition (EMT), the formation of cancer stem cells or tumor-initiating cells (CSCs/TICs), and chemoresistance, suggesting that claudins are promising targets for the treatment of chemoresistant and recurrent tumors. A recently identified claudin-low breast cancer subtype that is characterized by the enrichment of EMT and stem cell-like features is significantly associated with disease recurrence, underscoring
http://mdpi.com/1422-0067/14/9/18148/xml
Met synergizes with p53 loss to induce mammary tumors that possess features of claudin-low breast cancerMet synergizes with p53 loss to induce mammary tumors that possess features of claudin-low breast cancer
Triple-negative breast cancer (TNBC) accounts for ∼20% of cases and contributes to basal and claudin-low molecular subclasses of the disease. TNBCs have poor prognosis, display frequent mutations in tumor suppressor gene p53 (TP53), and lack targeted therapies. The MET receptor tyrosine kinase is el …
https://pubmed.ncbi.nlm.nih.gov/23509284/
Significance of glioma-associated oncogene homolog 1 (GLI1) expression in claudin-low breast cancer and crosstalk with the...Significance of glioma-associated oncogene homolog 1 (GLI1) expression in claudin-low breast cancer and crosstalk with the...
IntroductionThe recently identified claudin-low subtype of breast cancer is enriched for cells with stem-like and mesenchymal-like characteristics....
https://www.diagenode.com/jp/publications/view/2307
JCI - WelcomeJCI - Welcome
Background: Patients with diffuse midline gliomas (DMG), including diffuse intrinsic pontine glioma (DIPG), have dismal outcomes. We previously described the H3.3K27M mutation as a shared neoantigen in HLA-A*02.01+ H3.3K27M+ DMGs. Within the Pacific Pediatric Neuro-Oncology Consortium, we assessed safety and efficacy of an H3.3K27M-targeted peptide vaccine. Patients and Methods: Newly diagnosed patients aged 3-21 years with HLA-A*02.01+ and H3.3K27M+ status were enrolled into Stratum A (DIPG) and Stratum B (non-pontine DMG). Vaccine was administered in combination with poly-ICLC every three weeks for eight cycles, followed by once every six weeks. Immuno-monitoring and imaging occurred every three months. Imaging was centrally reviewed. Immunological responses were assessed in peripheral blood mononuclear cells using mass cytometry. Results: 19 patients enrolled in Stratum A (median age=11 years) and 10 in Stratum B (median age=13 years). There were no grade 4 treatment-related adverse events ...
https://www.jci.org/tags/25?content=articles&page=3
Magiran | Metastasis inhibition by BRMS1 and miR-31 replacement therapy in claudin-low cell linesMagiran | Metastasis inhibition by BRMS1 and miR-31 replacement therapy in claudin-low cell lines
Objective(s) The growing trend of research demonstrates that dynamic expression of two metastasis repressor classes (metastasis suppressor genes and anti-metastatic miRNA) has a close relationship with tumor invasion and metastasis. Using different strategies, it was revealed that cellular levels of miR-31 and Breast cancer Metastasis Suppressor1 (BRMS1) protein, which are among the most significant modulators of metastasis, have a correlation with the cells capability for invading and metastasizing; cells containing higher levels of miR-31 or BRMS1 were less metastatic. This project was carried out to determine whether the combinations of miR-31 and BRMS1 genes are able to enhance the capability of repressing the claudin-low breast cancer cell (MDA-MB-231) invasion. Materials and Methods This study used a restoration-based approach by miR-31 mimic and optimized BRMS1 gene sequences, which were cloned into a chimeric construct and transfected to the MDA-M231cells. Results Our data revealed that the
https://www.magiran.com/paper/2061077/?lang=en
Claudin - WikipediaClaudin - Wikipedia
Claudins are a family of proteins that are the most important components of the tight junctions, where they establish the paracellular barrier that controls the flow of molecules in the intercellular space between the cells of an epithelium. They have four transmembrane domains, with the N-terminus and the C-terminus in the cytoplasm. Claudins are small (20-27 kilodalton (kDa)) transmembrane proteins which are found in many organisms, ranging from nematodes to human beings, and are very similar in their structure, although this conservation is not observed on the genetic level. Claudins span the cellular membrane 4 times, with the N-terminal end and the C-terminal end both located in the cytoplasm, and two extracellular loops which show the highest degree of conservation. The first extracellular loop consists on average of 53 amino acids and the second one, being slightly smaller, of 24 amino acids. The N-terminal end is usually very short (4-10 amino acids), the C-terminal end varies in length ...
https://en.wikipedia.org/wiki/Claudin
GGRNA | ResultsGGRNA | Results
GGRNA , 2020-04-07 23:23:15 , RefSeq release 60 (20130726)] RefSeq ID Version Symbol GeneID Definition NM_001101389 NM_001101389.1 CLDN25 644672 Homo sapiens claudin 25 (CLDN25), mRNA. NM_001111319 NM_001111319.1 CLDN22 53842 Homo sapiens claudin 22 (CLDN22), mRNA. NM_020982 NM_020982.3 CLDN9 9080 Homo sapiens claudin 9 (CLDN9), mRNA. NM_001001346 NM_001001346.3 CLDN20 49861 Homo sapiens claudin 20 (CLDN20), mRNA. NM_001306 NM_001306.3 CLDN3 1365 Homo sapiens claudin 3 (CLDN3), mRNA. NM_012131 NM_012131.2 CLDN17 26285 Homo sapiens claudin 17 (CLDN17), mRNA. NM_016369 NM_016369.3 CLDN18 51208 Homo sapiens claudin 18 (CLDN18), transcript variant 1, mRNA. NM_001185056 NM_001185056.1 CLDN11 5010 Homo sapiens claudin 11 (CLDN11), transcript variant 2, mRNA. NM_005602 NM_005602.5 CLDN11 5010 Homo sapiens claudin 11 (CLDN11), transcript variant 1, mRNA. NM_182848 NM_182848.3 CLDN10 9071 Homo sapiens claudin 10 (CLDN10), transcript variant a, mRNA. NM_006984 NM_006984.4 CLDN10 9071 Homo sapiens claudin ...
http://ggrna.dbcls.jp/v1/search.cgi?query=claudin
EDB [Morimoto Shinya/[西村 範行]/Terai Tomoya/Manabe Shinji/Yamamoto Yasuyo/Shinahara Wakako/Miyake Hidenori/Tashiro Seiki/[島田 光生]/...EDB [Morimoto Shinya/[西村 範行]/Terai Tomoya/Manabe Shinji/Yamamoto Yasuyo/Shinahara Wakako/Miyake Hidenori/Tashiro Seiki/[島田 光生]/...
英) During epithelial morphogenesis, adherens junctions (AJs) and tight junctions (TJs) undergo dynamic reorganization, whereas epithelial polarity is transiently lost and reestablished. Although ARF6-mediated endocytic recycling of E-cadherin has been characterized and implicated in the rapid remodeling of AJs, the molecular basis for the dynamic rearrangement of TJs remains elusive. Occludin and claudins are integral membrane proteins comprising TJ strands and are thought to be responsible for establishing and maintaining epithelial polarity. Here we investigated the intracellular transport of occludin and claudins to and from the cell surface. Using cell surface biotinylation and immunofluorescence, we found that a pool of occludin was continuously endocytosed and recycled back to the cell surface in both fibroblastic baby hamster kidney cells and epithelial MTD-1A cells. Biochemical endocytosis and recycling assays revealed that a Rab13 dominant active mutant (Rab13 Q67L) inhibited the ...
https://web.db.tokushima-u.ac.jp/cgi-bin/edb_browse?ACT=BROWSE&EID=136725
Expression and localization of claudins-3 and -12 in transformed human brain endothelium - Open Research OnlineExpression and localization of claudins-3 and -12 in transformed human brain endothelium - Open Research Online
Findings: hCMEC/D3 cells express claudins-3 and -12. Claudin-3 is distinctly localized to the TJ whereas claudin -12 is observed in the perinuclear region and completely absent from TJs. We show that the expression of both proteins is lost in cell passage numbers where the BBB properties are no longer fully conserved. Expression and localization of claudin-3 is not modulated by simvastatin shown to improve barrier function in vitro and also recommended for routine hCMEC/D3 culture ...
http://oro.open.ac.uk/34224/
OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates...OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates...
Sigma-Aldrich offers abstracts and full-text articles by [S K Tiwari-Woodruff, A G Buznikov, T Q Vu, P E Micevych, K Chen, H I Kornblum, J M Bronstein].
https://www.sigmaaldrich.com/catalog/papers/11309411
Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins...Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins...
The EMT is an important mechanism for the development of multicellular organisms, by which, for example, the mesoderm and neural crest are generated (Hay, 1995). Thus, a detailed description of EMT in molecular terms is an important issue in developmental and cellular biology. However, EMT occurs in spatially restricted regions in a transient manner during embryogenesis, which has made it technically difficult to examine EMT at the molecular level. Set against this situation, forward genetics in Drosophila has brought a breakthrough: Snail, a transcription factor, plays a key role in triggering EMT (Grau et al., 1984; Nusslein-Volhard et al., 1984; Alberga et al., 1991). Now, we can induce EMT in cultured epithelial cells simply by exogenously expressing Snail (Cano et al., 2000; Batlle et al., 2000). This in vitro system prompted a direct investigation into two questions. First, what types of signaling events upregulate the Snail expression to trigger EMT in a spatially and temporally regulated ...
https://jcs.biologists.org/content/116/10/1959?ijkey=4a100594671c35ef9c639f6560b78757bb121133&keytype2=tf_ipsecsha
PubMedPro - claudins colorectal cancerPubMedPro - claudins colorectal cancer
PubMed.pro是医学,生命科学领域的数据库,简洁易用的PubMed中文版,PubMed手机版, 支持中英文关键词检索,标题摘要翻译,自动显示期刊影响因子，桌面手机均可使用
https://www.pubmed.pro/favorite?favoriteId=1424
Cldn15 MGI Mouse Gene Detail - MGI:1913103 - claudin 15Cldn15 MGI Mouse Gene Detail - MGI:1913103 - claudin 15
View mouse Cldn15 Chr5:136966616-136975858 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:1913103
Claudin 16 (CLDN16) ELISA KitsClaudin 16 (CLDN16) ELISA Kits
Reaktivität: Huhn, Rind (Kuh), Hund and more. 16 verschiedene CLDN16 ELISA Kits vergleichen. Alle direkt auf antikoerper-online.de bestellbar!
https://www.antikoerper-online.de/hepatitis-c-pathway-88/cldn16-elisa-kit-9458/
Claudin 18 (CLDN18) AntikörperClaudin 18 (CLDN18) Antikörper
Reaktivität: Huhn, Rind (Kuh), Hund and more. 60 verschiedene CLDN18 Antikörper vergleichen. Alle direkt auf antikörper-online bestellbar!
http://www.antikoerper-online.de/cell-cell-junction-organization-pathway-74/cldn18-antibody-5827/
Claudin-19 Mutations and Clinical Phenotype in Spanish Patients with Familial Hypomagnesemia with Hypercalciuria and...Claudin-19 Mutations and Clinical Phenotype in Spanish Patients with Familial Hypomagnesemia with Hypercalciuria and...
Familial hypomagnesemia with hypercalciuria and nephrocalcinosis is an autosomal recessive tubular disorder characterized by excessive renal magnesium and calcium excretion and chronic kidney failure. This rare disease is caused by mutations in the CLDN16 and CLDN19 genes. These genes encode the tight junction proteins claudin-16 and claudin-19, respectively, which regulate the paracellular ion reabsortion in the kidney. Patients with mutations in the CLDN19 gene also present severe visual impairment. Our goals in this study were to examine the clinical characteristics of a large cohort of Spanish patients with this disorder and to identify the disease causing mutations. We included a total of 31 patients belonging to 27 unrelated families and studied renal and ocular manifestations. We then analyzed by direct DNA sequencing the coding regions of CLDN16 and CLDN19 genes in these patients. Bioinformatic tools were used to predict the consequences of mutations. Clinical evaluation showed ocular defects in
https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0053151
Claudins and epithelial paracellular transport. - PubMed - NCBIClaudins and epithelial paracellular transport. - PubMed - NCBI
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
https://www.ncbi.nlm.nih.gov/pubmed/16460278?dopt=Abstract
The Biology of Claudin 6 (Cldn6) in the Developing Mouse Lung by Felix Ruben Jimenez RondanThe Biology of Claudin 6 (Cldn6) in the Developing Mouse Lung by Felix Ruben Jimenez Rondan
The tight junctions (TJ), which are located in the apical region between epithelial and endothelial cells, regulate the paracellular diffusion of ions and small molecules and play an important role in maintaining cell polarity, cell-cell integrity, and permeability. In the lung, epithelial cells are attached by TJ structures. They provide a permeable barrier and cell communication. The loss of barrier integrity, which is maintained by the expression of claudins (Cldn), results in cellular permibilization and leads to paracellular diffusion of solutes and harmful molecules. There are 27 known Cldn homologous members in mice and human. Cldn6 is mostly expressed in embryonic stem cells and associated with the programing of epithelial cells during embryo development and lung morphogenesis. In order to test the hypothesis that Cldn6 expression affects lung morphogenesis, we analyzed the expression pattern of Cldn6 during lung ontogenesis to examine cell-specific expression pattern of Cldn6 during each
https://scholarsarchive.byu.edu/etd/4414/
Untersuchungen zu parazellulären Barriereeigenschaften von ClaudinenUntersuchungen zu parazellulären Barriereeigenschaften von Claudinen
Epithelial and endothelial cells form the external lining of outer and inner body surfaces and blood vessels of multicellular organisms. Thus, they create separate compartments each exhibiting an environment optimally adjusted to their respective function. To build up such compartments epithelial and endothelial cells have to restrict the paracellular diffusion of substances. The paracellular cleft is sealed by tight junctions (TJ). In electron microscopical images TJs appear as a network of intermembranous strands in the apical region of the lateral cell membrane of epithelial and endothelial cells. Claudins (Cld) form the structural backbone of TJs. The present study provided evidence for the first time that single amino acids of the second extracellular loop (ECL) of a claudin are essential for the paracellular tightness of epithelial cells. The effect of single amino acid substitutions of the second ECL of Cld5 were studied in cells expressing various other endogenous claudins except Cld5. ...
https://edoc.hu-berlin.de/handle/18452/16574
Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely...Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely...
Tight junctions (TJs), hallmark structures of one-layered epithelia and of endothelia, are of central biological importance as intramembranous fences and as hydrophobic barriers between lumina represented by liquid- or gas-filled spaces on the one hand and the mesenchymal space on the other. The …
https://pubmed.ncbi.nlm.nih.gov/14533737/?dopt=Abstract
TumorPortalTumorPortal
This gene encodes an integral membrane protein, which belongs to the claudin family. The protein is a component of tight junction strands and may play a role in internal organ development and function during pre- and postnatal life. This gene is deleted in Williams-Beuren syndrome, a neurodevelopmental disorder affecting multiple systems ...
http://www.tumorportal.org/view?geneSymbol=CLDN4
August, 2015 | emailexporter.comAugust, 2015 | emailexporter.com
For every experimental group, brains from at minimum 3 distinct litter had been analyzed and when compared to the in accordance NaCl handle group. qPCR approach improvement exposed that only samples must be when compared to every other which have gone through experimental treatment, mind isolation, storage, purification and evaluation preparing steps with each other. Therefore, for every DEX-treatment the according NaCl handle group was carried out at the exact same time. In addition, owing to the large complete variety of samples, but limited sample variety which could be purified at the same time, only samples from mice at the same age and identical variety of antenatal injections ended up compared to every other by using a two-tailed Student`s t-take a look at. Data are offered as the signifies ± SEM. The major tight junction molecule and mind endothelial mobile marker claudin-five was investigated originally. Triple maternal DEX remedy drastically decreased claudin-5 mRNA expression to .54 ...
http://www.emailexporter.com/2015/08/
November 2017 - Pathways and therapeutic targets in Cancer therapyNovember 2017 - Pathways and therapeutic targets in Cancer therapy
The C\terminal fragment of enterotoxin (C\CPE) modulates the tight junction protein claudin and disturbs the tight junctional barrier. epithelial cells (HPDEs) had been treated with C\CPE 194 and C\CPE meters19. In well\differentiated cells of the pancreatic malignancy cell collection HPAC, C\CPE 194 and C\CPE meters19 interrupted both the hurdle and fencing features without adjustments in manifestation of claudin\1 and \4, collectively with an boost of MAPK phosphorylation. C\CPE 194, but not really C\CPE meters19, improved the cytotoxicity of the anticancer brokers gemcitabine and H\1. In differentiated pancreatic malignancy cell collection PANC\1 badly, C\CPE 194, but not really C\CPE meters19, reduced claudin\4 phrase and improved MAPK activity and the cytotoxicity of the anticancer agencies. In regular HPDEs, C\CPE 194 and C\CPE meters19 reduced claudin\4 phrase and improved the MAPK activity, whereas they do not really influence the cytotoxicity of the anticancer agencies. Our results ...
http://www.researchassistantresume.com/2017/11/
CLDN18 Gene - GeneCards | CLD18 Protein | CLD18 AntibodyCLDN18 Gene - GeneCards | CLD18 Protein | CLD18 Antibody
Complete information for CLDN18 gene (Protein Coding), Claudin 18, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
http://www.genecards.org/cgi-bin/carddisp.pl?gene=CLDN18
Barriers and Channels Formed by Tight Junction Proteins I, Volume 1257 | WileyBarriers and Channels Formed by Tight Junction Proteins I, Volume 1257 | Wiley
Tight junctions between epithelial and endothelial cells form selective barriers and paracellular channels and regulate paracellular transport of solutes, immune cells, and drugs. More specifically, tight junctions consist of proteins that laterally interconnect neighboring cells of epithelia and endothelia. Certain proteins seal the tight junction, so that a nearly impermeable barrier develops, whereas others form channels that allow for permeation between the cells. Recent investigations have focused on tight junction proteins, belonging to the claudin family (claudins-1 to -27 in humans) and the newly defined group of TAMP (three proteins: occludin, Marvel-D2, and tricellulin). Barriers and Channels Formed by Tight Junction Proteins I showcases work in this area clustered around three major themes: the molecular properties of tight junctions, for example, the role of the claudin family of proteins and the formation of ion and charge-selective channels; the regulation of tight junction
https://www.wiley.com/en-us/Barriers+and+Channels+Formed+by+Tight+Junction+Proteins+I%2C+Volume+1257-p-9781573318730
CLDN16 gene - Genetics Home Reference - NIHCLDN16 gene - Genetics Home Reference - NIH
From NCBI Gene:. Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. It is found primarily in the kidneys, specifically in the thick ascending limb of Henle, where it acts as either an intercellular pore or ion concentration sensor to regulate the paracellular resorption of magnesium ions. Defects in this gene are a cause of primary hypomagnesemia, which is characterized by massive renal magnesium wasting with hypomagnesemia and hypercalciuria, resulting in ...
https://ghr.nlm.nih.gov/gene/CLDN16
Search Results | Journal of Cell Biology | Rockefeller University PressSearch Results | Journal of Cell Biology | Rockefeller University Press
ZO-1, ZO-2, and ZO-3, which contain three PDZ domains (PDZ1 to -3), are concentrated at tight junctions (TJs) in epithelial cells. TJ strands are mainly composed of two distinct types of four-transmembrane proteins, occludin, and claudins, between which occludin was reported to directly bind to ZO-1/ZO-2/ZO-3. However, in occludin-deficient intestinal epithelial cells, ZO-1/ZO-2/ZO-3 were still recruited to TJs. We then examined the possible interactions between ZO-1/ZO-2/ZO-3 and claudins. ZO-1, ZO-2, and ZO-3 bound to the COOH-terminal YV sequence of claudin-1 to -8 through their PDZ1 domains in vitro. Then, claudin-1 or -2 was transfected into L fibroblasts, which express ZO-1 but not ZO-2 or ZO-3. Claudin-1 and -2 were concentrated at cell-cell borders in an elaborate network pattern, to which endogenous ZO-1 was recruited. When ZO-2 or ZO-3 were further transfected, both were recruited to the claudin-based networks together with endogenous ZO-1. Detailed analyses showed that ZO-2 and ZO-3 ...
https://rupress.org/jcb/search-results?f_Authors=Kazumasa+Morita
PA-824PA-824
immune Uncategorized PA-824, Rabbit Polyclonal to C-RAF (phospho-Thr269). The blood-epididymis barrier (BEB) is formed by epithelial tight junctions mediating selective permeability from the PA-824 epididymal epithelium. the paracellular permeability had been examined by two strategies TER and FITC-Dextran-based tracer diffusion assays. Both assays soon add up to related outcomes indicating a time-dependent disruption from the BEB differentially for the three TGF? isoforms (TGF?3>TGF?1>TGF?2) inside a TGF?-recetor-1 kinase- and Smad-dependent way. The small junction proteins claudin-1 was discovered to be decreased by the procedure with TGF?s whereas occludin had not PA-824 been affected. Epididymal epithelial cells are mainly attentive to TGF?s PA-824 through the basolateral side recommending that TGF? may impact for the epididymal epithelium through the stroma cell tradition versions the knockdown of 1 of the claudins (1 -3 -4 or -7) led to dramatically reduced transepithelial electrical level ...
http://www.immune-source.com/tag/pa-824/
USE OF HYALURONIC ACID FOR THE PREPARATION OF COMPOSITIONS INTENDED FOR IMPROVING IN PARTICULAR THE PROTECTIVE FUNCTION OF THE...USE OF HYALURONIC ACID FOR THE PREPARATION OF COMPOSITIONS INTENDED FOR IMPROVING IN PARTICULAR THE PROTECTIVE FUNCTION OF THE...
0011]The tight junctions form a selective barrier regulating the passage of ions and molecules through paracellular space. Under electron microscopy, it is noted that the tight junctions form a series of fusion points between the outer leaflets of the plasma membranes of two adjacent cells. These membrane contact zones appear, by freeze fracture, in the form of a continuous network that surrounds the apex of each cell. This network is constituted by membrane protein polymers, the claudins and occludin which are themselves connected to cytoplasmic proteins among which in particular the zonula occludens proteins (ZO-1 to 3) are to be found. Occludin, the claudins as well as the ZO-1s are often the target for bacterial toxins, leading to an alteration in the organisation and the function of the tight junctions (Coraux et al., Am J Respir Cell Mol Biol 2004, 5:605-612 ...
http://www.patentsencyclopedia.com/app/20100210585
Plus itPlus it
Background: Metaplastic breast cancer (BC) is a treatment-refractory rare type of BC with characteristics similar to claudin-low tumors. Understanding the genomic landscape of metaplastic BC can lead to identification of new therapies.. Methods: Patients with metastatic metaplastic BC referred for experimental therapies, who had adequate archival tumor tissue for DNA extraction, had targeted next-generation sequencing (NGS) for 3,769 exons of 236 cancer-related genes and 47 introns from 19 genes to an average depth of 1000X using the Illumina HiSeq 2000 platform (Foundation One, Foundation Medicine, MA).. Results: NGS results were obtained for 10 women with metaplastic BC (median age 60 years [39-73], median prior therapies for metastatic BC 0 [0-1]). NGS revealed a total of 41 aberrations in 25 genes and all 10 patients had at least 1 molecular aberration (range 1-7, median 4). Of 41 detected molecular aberrations, 17 (41%) included putative activation of the PI3K/mTOR and/or MAPK pathways ...
http://mct.aacrjournals.org/content/12/11_Supplement/C120
Claudin 7 Antibody 10118-1-AP | ProteintechClaudin 7 Antibody 10118-1-AP | Proteintech
Claudin 7 antibody Rabbit Polyclonal from Proteintech validated in Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Enzyme-linked Immunosorbent Assay (ELISA) applications. This antibody reacts with human,mouse samples. Cat.No. 10118-1-AP.
https://www.ptglab.com/Products/CLDN7-Antibody-10118-1-AP.htm
Recombinant Mouse Cldn4 Protein, MYC/DDK-tagged Cldn4-901M - Creative BioMartRecombinant Mouse Cldn4 Protein, MYC/DDK-tagged Cldn4-901M - Creative BioMart
Purified Recombinant Mouse Cldn4 Protein, MYC/DDK-tagged from Creative Biomart. Recombinant Mouse Cldn4 Protein, MYC/DDK-tagged can be used for research.
https://www.creativebiomart.net/recombinant-mouse-cldn4-protein-mycddk-tagged-509190.htm
WikiGenes - CLDN2 - claudin 2WikiGenes - CLDN2 - claudin 2
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
https://www.wikigenes.org/e/gene/e/9075.html
CLDN1 purified MaxPab mouse polyclonal antibody (B01P) - (H00009076-B01P) - Products - AbnovaCLDN1 purified MaxPab mouse polyclonal antibody (B01P) - (H00009076-B01P) - Products - Abnova
Mouse polyclonal antibody raised against a full-length human CLDN1 protein. CLDN1 (NP_066924.1, 1 a.a. ~ 211 a.a) full-length human protein. (H00009076-B01P) - Products - Abnova
http://www.abnova.com/products/products_detail.asp?catalog_id=H00009076-B01P
Familial hypomagnesaemia, Hypercalciuria and Nephrocalcinosis associated with a novel mutation of the highly conserved leucine...Familial hypomagnesaemia, Hypercalciuria and Nephrocalcinosis associated with a novel mutation of the highly conserved leucine...
Sixty mutations of claudin 16 coding gene have been reported in familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC) patients. Recent investigations revealed that a highly conserved glycine-leucine-tryptophan (115G-L-W117) motif in the first extracellular segment (ESC1) of claudin 16 might be essential for stabilization of the appropriately folded ECS1 structure and conservation of normal claudin 16 function. However, neither missense nor nonsense mutation has ever been described in this motif. Our study aimed at identifying mutations in a Chinese patient with FHHNC and exploring the association between genotype and phenotype. A 33-year-old female presented with 4 years history of recurrent acute pyelonephritis without other notable past medical history. Her healthy parents, who aged 56 and 53 respectively, were second cousins, and her only sibling died from renal failure without definite cause at age 25. Renal ultrasound imaging demonstrated atrophic kidneys and bilateral
https://bmcnephrol.biomedcentral.com/articles/10.1186/s12882-018-0979-1
Tight junctions (TJs) are constructions indispensable to epithelial cells and are - PI3K Signaling in B and T LymphocytesTight junctions (TJs) are constructions indispensable to epithelial cells and are - PI3K Signaling in B and T Lymphocytes
Tight junctions (TJs) are constructions indispensable to epithelial cells and are responsible for regulations of paracellular diffusion and maintenance of cellular polarity. interstitial tissues spaces. Located at the pinnacle of horizontal walls, TJs have both wall and barriers features. The barriers function represents a selectively permeable filtration system that adjusts paracellular diffusion of ions and solutes structured on charge and size, respectively (Gemstone, 1977 ). Barriers function is certainly firmly governed by a particular arranged of TJ protein, the claudins (Tsukita made up of a non-specific shRNA into MDCK II cells (brief hairpin non-specific control [shCtrl] cells). Specificities of RalA and RalB exhaustion had been ABT-263 decided by immunoblotting and immunofluorescence marking of endogenous protein; both RalB and RalA localised to the plasma membrane layer in subconfluent MDCK II cells, and this localization was untouched in shCtrl cells (Body 1B). In shRalA cells, ...
http://health-e-nc.org/2017/12/05/tight-junctions-tjs-are-constructions-indispensable-to-epithelial-cells-and-are/
Impact of Hyperosmotic Glycerol on Tighy Junction In VitroImpact of Hyperosmotic Glycerol on Tighy Junction In Vitro
The tight junction regulates passage of molecules throuth the paracellular spaces. Occludin and claudins are the specific trancmembrance protains present at the tight junction and are believed to regulate the cell barrier functions. To examine the response of the tight junction to hyperosmotic solutions, Ⅰinvestigated the effects of hyperosmotic glycerol on function and protein expression of the tight junction in ECV304 cells. Cell cytotoxicity analysis showed that the high (10%) concentration of glcerol damaged 64.1% of the ECV304 cells (p＜0.001), and this was confirmed morphologically. Treatment with 1%, 2% or 5% glyserol increased the paracellular permeability of fluorescein isothiocyanate (FITC) -labeled dextran by 4.7%, 18.7% and 29.4% (p＜0.05), respectively. In addition, exposure to glycerol at any concentration strongly reduced the expression of occludin, whereas enpression of claudin-1 was affected very slightly. These results suggest that hyperosmotic glycerol would certainly ...
http://petit.lib.yamaguchi-u.ac.jp/G0000006y2j2/Detail.e?id=137020100507170003
Plus itPlus it
The ability to invade host tissues and metastasize is the major cause of cancer-related death. During tumor invasion, metastasizing cells disrupt normal cell-matrix adhesion and acquire an invasive phenotype. Claudins are adhesion proteins localized at tight junctions (TJs). Claudin-7 is a unique TJ membrane protein in that it has a stronger basolateral membrane distribution than that of apical TJs in epithelial cells. To study the basolateral function of claudin-7, claudin-7 gene silencing experiments were carried out in a lung cancer cell line using the lentivirus shRNA approach. We found that claudin-7 knockdown (KD) cells showed disrupted cell-matrix interactions. Consequently, when claudin-7 KD cells were plated on the uncoated glass surface, they were unable to attach to the glass and died the day after plating. In contrast, control cells adhered well and grew normally. Using immunofluorescent microscopy and biochemistry methods, we found that claudin-7 co-localized and ...
http://cancerres.aacrjournals.org/content/72/8_Supplement/5175
Difference between revisions of 2011 Group 3 Project - CellBiologyDifference between revisions of 2011 Group 3 Project - CellBiology
Tight junctions consist of a branching network of sealing strands of protein. Each strand is assembled from a series of transmembrane proteins(JAMs/Junctional Adhesion Molecules,Claudins and Occludin) embedded in plasma membranes. The extracellular domains join each other in tight junctions,whereas the intracellular domains are linked to peripheral membrane proteins,linking the transmembrane protein strands to actin cytoskeleton to create a functional network that plays a role in cellular processes. Each strand functions as an individual or linear barrie, therefore, the number of transmembrane protein strands is in relation with the degree of paracellular electrical resistance and impedance to solute flux in tight junctions[1]. Although other types of proteins are present at tight junctions, however, occludin and claudin are the major ones contributing to the structure of tight junctions. ...
https://cellbiology.med.unsw.edu.au/cellbiology/index.php?title=2011_Group_3_Project&diff=prev&oldid=28263
2011 Group 3 Project - CellBiology2011 Group 3 Project - CellBiology
Tight junctions consist of a branching network of sealing strands of protein. Each strand is assembled from a series of transmembrane proteins(JAMs/Junctional Adhesion Molecules,Claudins and Occludin) embedded in plasma membranes. The extracellular domains join each other in tight junctions,whereas the intracellular domains are linked to peripheral membrane proteins,linking the transmembrane protein strands to actin cytoskeleton to create a functional network that plays a role in cellular processes. Each strand functions as an individual or linear barrie, therefore, the number of transmembrane protein strands is in relation with the degree of paracellular electrical resistance and impedance to solute flux in tight junctions[1]. Although other types of proteins are present at tight junctions, however, occludin and claudin are the major ones contributing to the structure of tight junctions. ...
https://cellbiology.med.unsw.edu.au/cellbiology/index.php?title=2011_Group_3_Project&oldid=28263
Blood brain barrier: Fluid TransferBlood brain barrier: Fluid Transfer
The blood brain barrier (BBB) is a specialized barrier that renders the environment of the central nervous system (CNS) separate from other compartments of the body. The unique environment provided by the BBB enables the specialized activity of neurons; BBB breakdown is the result of pathologic conditions and leads to further neuronal dysfunction. The unique requirements of the CNS require the BBB to limit the free exchange of some solutes that would be freely exchanged through other anatomic compartments. The restriction of solute transport limits how fluids can transfer across the BBB.. The BBB is formed by endothelial cells that line cerebral micro vessels. 1 It restricts the entry of many substances dissolved in blood because of specialized tight junctions (TJ) between adjacent endothelial cells. BBB TJ are maintained by the interaction of specialized cytoskeleton and linking proteins not expressed in other endothelium, examples include : Claudins, occludins, and junctional adhesion ...
http://www.openanesthesia.org/blood_brain_barrier_fluid_transfer/
CLDN8 | definition of CLDN8 by Medical dictionaryCLDN8 | definition of CLDN8 by Medical dictionary
Looking for online definition of CLDN8 in the Medical Dictionary? CLDN8 explanation free. What is CLDN8? Meaning of CLDN8 medical term. What does CLDN8 mean?
https://medical-dictionary.thefreedictionary.com/CLDN8
CLDN7 (Human) Recombinant Protein (Q01) - (H00001366-Q01) - Products - AbnovaCLDN7 (Human) Recombinant Protein (Q01) - (H00001366-Q01) - Products - Abnova
Human CLDN7 partial ORF ( NP_001298, 31 a.a. - 81 a.a.) recombinant protein with GST-tag at N-terminal. (H00001366-Q01) - Products - Abnova
http://www.abnova.com/products/products_detail.asp?catalog_id=H00001366-Q01
Bifidobacteria stabilize claudins at tight junctions and prevent intestinal barrier dysfunction in mouse necrotizing...Bifidobacteria stabilize claudins at tight junctions and prevent intestinal barrier dysfunction in mouse necrotizing...
TY - JOUR. T1 - Bifidobacteria stabilize claudins at tight junctions and prevent intestinal barrier dysfunction in mouse necrotizing enterocolitis. AU - Bergmann, Kelly R.. AU - Liu, Shirley X L. AU - Tian, Runlan. AU - Kushnir, Anna. AU - Turner, Jerrold R.. AU - Li, Hong Lin. AU - Chou, Pauline M.. AU - Weber, Christopher R.. AU - De Plaen, Isabelle G.. N1 - Copyright: Copyright 2018 Elsevier B.V., All rights reserved.. PY - 2013/5. Y1 - 2013/5. N2 - Whether intestinal barrier disruption precedes or is the consequence of intestinal injury in necrotizing enterocolitis (NEC) remains unknown. Using a neonatal mouse NEC model, we examined the changes in intestinal permeability and specific tight-junction (TJ) proteins preceding NEC and asked whether these changes are prevented by administration of Bifidobacterium infantis, a probiotic known to decrease NEC incidence in humans. Compared with dam-fed controls, pups submitted to the NEC protocol developed i) significantly increased intestinal ...
https://augusta.pure.elsevier.com/en/publications/bifidobacteria-stabilize-claudins-at-tight-junctions-and-prevent-
Human epidermal Langerhans cells express the tight junction protein claudin-1 and are present in human genetic claudin-1...Human epidermal Langerhans cells express the tight junction protein claudin-1 and are present in human genetic claudin-1...
Claudin-1 (CLDN1) is a structural tight junction (TJ) protein and is expressed in differentiating keratinocytes and Langerhans cells in the epidermis. Our objective was to identify immunoreactive CLDN1 in human epidermal Langerhans cells and to examine the pattern of epidermal Langerhans cells in genetic human CLDN1 deficiency [neonatal ichthyosis, sclerosing cholangitis (NISCH) syndrome]. Epidermal cells from healthy human skin labelled with CLDN1-specific antibodies were analysed by confocal laser immunofluorescence microscopy and flow cytometry. Skin biopsy sections of two patients with NISCH syndrome were stained with an antibody to CD1a expressed on epidermal Langerhans cells. Epidermal Langerhans cells and a subpopulation of keratinocytes from healthy skin were positive for CLDN1. The gross number and distribution of epidermal Langerhans cells of two patients with molecularly confirmed NISCH syndrome, however, was not grossly altered. Therefore, CLDN1 is unlikely to play a critical role in ...
http://www.zora.uzh.ch/id/eprint/14247/
Role of tight junction proteins in gastroesophageal reflux disease | BMC Gastroenterology | Full TextRole of tight junction proteins in gastroesophageal reflux disease | BMC Gastroenterology | Full Text
In this study, we demonstrated (I) distinct expression patterns of five genes encoding for proteins involved in the formation of tight junctions in esophageal mucosa. In particular Claudin-1 in ERD and to lesser extent Claudin-2 was expressed at higher levels in patients with GERD. In contrast, ZO-1, ZO-2, and Occludin were not affected by the presence of GERD. (II) In general, altered gene expression of Claudin-1/-2 did not correlate with the degree of histomorphological changes in the esophageal mucosa of patients with GERD.. Tight junctions are composed of transmembrane proteins such as Occludin, 24 Claudins, several junctional adhesion molecules (JAMs) with different isoforms, E-Cadherin as well as cytosolic binding partners [43, 44]. The selection of the five genes studied was based on functional aspects. Occludin is critical for the formation of tight junctions in most tissues [45]. Claudin-1 is one of the numerous Claudins that seals intercellular space leading to higher barrier function ...
https://bmcgastroenterol.biomedcentral.com/articles/10.1186/1471-230X-12-128
Role of claudin-1 in colon tumor progression and metastasis - Research NebraskaRole of claudin-1 in colon tumor progression and metastasis - Research Nebraska
DESCRIPTION (provided by applicant): Disruption of the cell-cell junction with concomitant changes in the expression of junctional proteins is a hallmark of cancer metastasis and invasion. Role of adherent junction proteins have been studied extensively in cancer, however the role of tight junction proteins is less understood. Claudins are the recently identified tetraspanins, which are integral to the structure and function of tight junctions (TJs). Recent studies have shown changes in expression/cellular localization for claudins during tumorigenesis, however a cause and effect relationship has not been established. Here, we report a highly increased expression for claudin-1 in human primary colon carcinoma and metastatic tissues and cell lines derived from similar sources with relatively frequent nuclear localization. Furthermore, using genetic manipulations of claudin-1 expression in colon cancer cell lines, we demonstrate a role for claudin-1 in the regulation of epithelial to mesenchymal ...
https://nebraska.pure.elsevier.com/en/projects/role-of-claudin-1-in-colon-tumor-progression-and-metastasis
Tight junction for magnesium | Journal of Cell ScienceTight junction for magnesium | Journal of Cell Science
In multicellular organisms, compartments with different compositions are separated by epithelia. Exchange of solutes between compartments can occur through (transcellular) or around (paracellular) the epithelial cells. Tight junctions between the cells form an ion-selective barrier across the paracellular route, and several human diseases involve a breakdown of these junctions. On p. 5109, Daniel Goodenough and colleagues report that the tight junction protein paracellin 1 (claudin-16) can modulate tight junction ion selectivity in the renal epithelial cell line LLC-PK1, which does not normally express this protein. When the authors express paracellin 1 in these cells, it localizes to the tight junctions and increases their permeability to Na+ but not to Cl- or Mg2+. Mutagenesis studies indicated that the extracellular loops of paracellin 1 are critical for this ion selectivity. Similar paracellin 1 mutations cause human familial hypomagnesemia with hypocalcinuria and nephrocalcinosis (FHHNC), ...
http://jcs.biologists.org/content/118/21/e2105
Claudin-1 required for HCV virus entry has high potential for phosphorylation and O -glycosylation | Virology Journal | Full...Claudin-1 required for HCV virus entry has high potential for phosphorylation and O -glycosylation | Virology Journal | Full...
HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world. Claudins belong to family of tight junctions proteins that are responsible for establishing barriers for controlling the flow of molecules around cells. For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise. During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81. The claudin-1 assembly with tight junctions is regulated by post translational modifications. During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail. In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo. Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for
https://virologyj.biomedcentral.com/articles/10.1186/1743-422X-8-229
Regulation of RPE Intercellular Junction Integrity and Function by Hepatocyte Growth Factor | IOVS | ARVO JournalsRegulation of RPE Intercellular Junction Integrity and Function by Hepatocyte Growth Factor | IOVS | ARVO Journals
This effect appeared to be mediated primarily by the action of HGF on the cytoplasmic membrane plaque protein ZO-1. ZO-1 is a peripheral membrane protein localized to the tight junction complex in epithelial and endothelial cells. Anchoring of ZO-1 with the underlying cytoskeleton is required for localization of occludin and claudin in the tight junction. ZO-1, -2, and -3 contain three PDZ domains, one SH3 domain, and one guanylyl kinase-like domain (GuK). Through its GuK domains, ZO-1 binds directly to the carboxyl termini of claudins and occludin and may function as an adaptor at the cytoplasmic surface of the tight junction to recruit other proteins, including cytoskeletal and signaling molecules. 4 These components can form a huge macromolecular complex at the cytoplasmic surface of tight junctions and may be involved in the regulation of endothelial and epithelial cell polarization, proliferation, and differentiation. 4 As an adaptor, ZO-1 is a critical regulatory protein between occludin ...
http://iovs.arvojournals.org/article.aspx?articleid=2123731
A transgenic zebrafish model for the in vivo study of the blood and choroid plexus brain barriers using claudin 5 | Biology OpenA transgenic zebrafish model for the in vivo study of the blood and choroid plexus brain barriers using claudin 5 | Biology Open
Claudin 5 as a prominent TJ protein is a consistent feature between the BBB and blood-CSF barrier (Bill and Korzh, 2014). Here we have used this feature to create an in vivo model for real-time analysis of the development, structure and function of the BBB and CP by generating a transgenic zebrafish line that expresses EGFP under the claudin 5a promoter. The high homology and synteny with human, the conservation along the teleost lineage and the previous characterisation of Claudin 5a in zebrafish makes cldn5a a logical candidate (Abdelilah-Seyfried, 2010; Xie et al., 2010; Zhang et al., 2012).. We show that developmental expression of cldn5a:EGFP is restricted to, and starts in both CPs and the midline at 1 dpf, thereby narrowing down the previously shown whole-mount in situ hybridizations (Zhang et al., 2010). The presence of Claudin 5a at the CPs at 1 dpf coincides with the inflation of the ventricles (Zhang et al., 2010, 2012) and corroborates its role in this process. Claudin 5a is crucial ...
https://bio.biologists.org/content/7/2/bio030494
Helicobacter pylori targets cancer-associated apical-junctional constituents in gastroids and gastric epithelial cells | GutHelicobacter pylori targets cancer-associated apical-junctional constituents in gastroids and gastric epithelial cells | Gut
Objective Helicobacter pylori strains that express the oncoprotein CagA augment risk for gastric cancer. However, the precise mechanisms through which cag+ strains heighten cancer risk have not been fully delineated and model systems that recapitulate the gastric niche are critical for understanding pathogenesis. Gastroids are three-dimensional organ-like structures that provide unique opportunities to study host-H. pylori interactions in a preclinical model. We used gastroids to inform and direct in vitro studies to define mechanisms through which H. pylori modulates expression of the cancer-associated tight junction protein claudin-7.. ...
http://gut.bmj.com/content/early/2014/08/14/gutjnl-2014-307650
Claudin-8 Expression in Renal Epithelial Cells Augments the Paracellular Barrier by Replacing Endogenous Claudin-2, The Journal...Claudin-8 Expression in Renal Epithelial Cells Augments the Paracellular Barrier by Replacing Endogenous Claudin-2, The Journal...
Read Claudin-8 Expression in Renal Epithelial Cells Augments the Paracellular Barrier by Replacing Endogenous Claudin-2, The Journal of Membrane Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
https://www.deepdyve.com/lp/springer_journal/claudin-8-expression-in-renal-epithelial-cells-augments-the-ptRFDYG8Z9
ISOLATED POPULATIONS OF ADULT RENAL CELLS AND METHODS OF ISOLATING AND USING SAME - Patent applicationISOLATED POPULATIONS OF ADULT RENAL CELLS AND METHODS OF ISOLATING AND USING SAME - Patent application
TABLE-US-00004 TABLE 4 Cell and biological adhesion Fold Symbol Gene name Gene assignment change CLDN7 claudin 7 Involved in the formation of 2.74 tight junctions between epithelial cells PCDHB5 Protocadherin Member of the 3.32 beta-5 protocadherin beta gene cluster CLDN3 Claudin 3 Member of the claudin 3.93 family, is an integral membrane protein and a component of tight junction strands. CNTN6 contactin 6 Contactins mediate cell 3.09 surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. PKHD1 polycystic kidney Localized predominantly at 3.38 and hepatic the disease 1 apical domain of polarized epithelial cells, suggesting it may be involved in the tubulogenesis and/or maintenance of duct-lumen architecture. PCDHB2 protocadherin The extracellular domains 2.94 beta 2 interact in a homophilic manner to specify differential cell-cell connections. CDH1 E-cadherin cell adhesion molecule 3.27 (epithelial) CX3CL1 hemokine ...
http://www.patentsencyclopedia.com/app/20130059325
CLDN19 gene - Genetics Home ReferenceCLDN19 gene - Genetics Home Reference
From NCBI Gene:. The product of this gene belongs to the claudin family. It plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Defects in this gene are the cause of hypomagnesemia renal with ocular involvement (HOMGO). HOMGO is a progressive renal disease characterized by primary renal magnesium wasting with hypomagnesemia, hypercalciuria and nephrocalcinosis associated with severe ocular abnormalities such as bilateral chorioretinal scars, macular colobomata, significant myopia and nystagmus. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jun 2010]. From UniProt: ...
https://ghr.nlm.nih.gov/gene/CLDN19
Genetics of primary hypercalciuria: PCLN-1 gene-dependent hypercalciuric diseasesGenetics of primary hypercalciuria: PCLN-1 gene-dependent hypercalciuric diseases
Familial Hypomagnesaemia with Hypercalciuria and Nephro-calcinosis (FHHN) is a rare disorder of calcium and magnesium paracellular transportation at TAL level
http://www.cheapmedicinechest.com/genetics-of-primary-hypercalciuria-pcln-1-gene-dependent-hypercalciuric-diseases.html
Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments | JCBEndocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments | JCB
In this study, we have described a new biochemical assay that efficiently reconstitutes the endocytosis of E-cadherin using the AJ plasma membranes. We have found here that non-trans-interacting E-cadherin is constitutively endocytosed like integrin (ligand-independent endocytosis), that the formation of endocytosed vesicles of E-cadherin is clathrin dependent, and that E-cadherin, but not other CAMs at AJs and TJs including nectins, claudins, and occludin, is selectively sorted into the endocytosed vesicles. Recent cell-level studies using chemical inhibitors have shown that E-cadherin might be internalized by clathrin- or caveolin-dependent endocytosis (Le et al., 1999; Akhtar and Hotchin, 2001; Palacios et al., 2002; Thomsen et al., 2002; Paterson et al., 2003; Ivanov et al., 2003). However, the results obtained in this way are indirect and not substantial because the low resolution indirect immunofluorescence staining could only follow the appearance of E-cadherin in large vesicular ...
http://jcb.rupress.org/content/166/2/237
Fluoridegate - Page 3 - Science and Technology - Unexplained Mysteries Discussion ForumsFluoridegate - Page 3 - Science and Technology - Unexplained Mysteries Discussion Forums
And yet you said, and I quote; ok, so you accept that some people with ill functioning BBB such as diabetics (who drink more than most) and those with fevers and certain conditions etc would be affected by toxic fluoride going direct to the brain. that alone is reason enough not to fluoridate, but you didnt address the central points. you are the one who claims to be a medical doctor, so you should know these things.. If you could answer the questions I posted (here they are again; What areas? Where? Which parts of the brain? How does the impact of fenestrations play on movement of things across the BBB? Does fenestration or sinusoid matter? What about diaphragms? Could you discuss the ramifications of different junctional complexes on the BBB? How about protein structure for those complexes; Claudins? Occuldins?. Can you discuss briefly the function of the Choroid plexus? Its relation to the BBB? What about Circumventricular organs? How does changes in the BBB affect thees organs? Infection ...
https://www.unexplained-mysteries.com/forum/topic/198633-fluoridegate/page/3/?tab=comments
Plus itPlus it
While growth factor-independent signaling and proliferation are well-established hallmarks of cancer, little is known regarding growth factor-independent changes in gene expression which occur downstream from oncogenes. The PI3K pathway is one of the most commonly misregulated signaling pathways in human cancers. Here, MCF10A cells expressing the two most common PI3K mutations, PIK3CA E545K and H1047R, were used to identify the repertoire of genes altered by oncogenic PI3K mutations following growth factor deprivation. This gene set most closely correlated with gene signatures from claudin-low and basal-like breast tumors, and categorical enrichment analyses suggested that NF-κB target genes were dramatically upregulated by these mutations. An IKKα inhibitor was used to identify the subset of PI3K-driven genes that is NF-κB dependent. Interestingly, virtually all of these NF-κB dependent genes were secreted proteins, suggesting a paracrine role for this gene set. Among these genes was IL-6, ...
http://cancerres.aacrjournals.org/content/72/8_Supplement/988
Tissue expression of CLDN4 - Staining in rectum - The Human Protein AtlasTissue expression of CLDN4 - Staining in rectum - The Human Protein Atlas
Expression of CLDN4 (CPE-R, CPETR, CPETR1, hCPE-R, WBSCR8) in rectum tissue. Antibody staining with CAB002610 in immunohistochemistry.
http://www.proteinatlas.org/ENSG00000189143-CLDN4/tissue/rectum
Intestinal permeabilityIntestinal permeability
Cite journal requires ,journal= (help) Khan, Niamat; Asif, Abdul R. (2015-01-01). "Transcriptional Regulators of Claudins in ...
https://en.wikipedia.org/wiki/Intestinal_permeability
Paracellular transportParacellular transport
Some claudins form tight junction-associated pores that allow paracellular ion transport. The tight junctions have a net ...
https://en.wikipedia.org/wiki/Paracellular_transport
Uterine epitheliumUterine epithelium
Colegio, O. R., Van Itallie, C. M., McCrea, H. J., Rahner, C., & Anderson, J. M. (2002). Claudins create charge-selective ... Nicholson, M., Lindsay, L. A., & Murphy, C. R. (2010). Ovarian hormones control the changing expression of claudins and ...
https://en.wikipedia.org/wiki/Uterine_epithelium
Epithelial-mesenchymal transitionEpithelial-mesenchymal transition
... including claudins and desmosomes, thus facilitating EMT. On the other hand, transcription factors such as grainyhead-like ...
https://en.wikipedia.org/wiki/Epithelial–mesenchymal_transition
Cell adhesionCell adhesion
Claudins, essential for formation of tight junctions, form paracellular pores which allow selective passage of specific ions ... Tight junction is formed by transmembrane proteins, including claudins, occludins and tricellulins, that bind closely to each ... which is what happens when the hepatitis C virus targets occludins and claudins in tight junctions to enter liver cells. ...
https://en.wikipedia.org/wiki/Cell_adhesion
Stem-cell nicheStem-cell niche
... claudins and zonula occludens (ZOs) which show dynamic expression during spermatogenesis. For example, claudin 11 has been ...
https://en.wikipedia.org/wiki/Stem-cell_niche
Journal of Cell BiologyJournal of Cell Biology
... including occludins and claudins), adherens junctions, and cadherins. January 25, 1955: Publication of the first issue of The ...
https://en.wikipedia.org/wiki/Journal_of_Cell_Biology
Cell adhesionCell adhesion
... including claudins, occludins and tricellulins, that bind closely to each other on adjacent membranes in a homophilic manner.[1 ... which is what happens when the hepatitis C virus targets occludins and claudins in tight junctions to enter liver cells.[9] ... Claudins, essential for formation of tight junctions, form paracellular pores which allow selective passage of specific ions ...
https://en.m.wikipedia.org/wiki/Cell_adhesion
Claudins and epithelial paracellular transport. - PubMed - NCBIClaudins and epithelial paracellular transport. - PubMed - NCBI
Claudins and epithelial paracellular transport.. Van Itallie CM1, Anderson JM.. Author information. 1. Department of Medicine, ... Recent evidence shows that claudins, a large family (at least 24 members) of intercellular adhesion molecules, form the seal ... This evidence comes from the study of claudins expressed in cultured epithelial cell models, genetically altered mice, and ...
https://www.ncbi.nlm.nih.gov/pubmed/16460278?dopt=Abstract
IJMS | Free Full-Text | Emerging Roles of Claudins in Human CancerIJMS | Free Full-Text | Emerging Roles of Claudins in Human Cancer
The involvement of claudins in tumor progression was suggested by their important role in the migration, invasion and ... A better understanding of the emerging role of claudins in CSC/TICs and chemoresistance may help to develop therapies against ... Although their dysregulation in cancer suggests that claudins play a role in tumorigenesis, the exact underlying mechanism ... suggesting that claudins are promising targets for the treatment of chemoresistant and recurrent tumors. A recently identified ...
http://mdpi.com/1422-0067/14/9/18148/xml
JCI - Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasisJCI - Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis
Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis. ... Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis. ...
https://www.jci.org/articles/view/88428/figure/1
Toxins | Free Full-Text | On the Interaction of Clostridium perfringens Enterotoxin with ClaudinsToxins | Free Full-Text | On the Interaction of Clostridium perfringens Enterotoxin with Claudins
The C-terminal region (cCPE) binds to the second extracellular loop of a subset of claudins. Claudin-3 and claudin-4 have been ... The toxin binds with weak affinity to claudin-1 and -2 but contribution of these weak binding claudins to CPE-mediated disease ... and CPE-based peptidomimetics to modulate tight junctions for improved drug delivery or to treat tumors overexpressing claudins ... Keywords: Claudins; Clostridium perfringens enterotoxin; drug delivery; tight junction Claudins; Clostridium perfringens ...
http://www.mdpi.com/2072-6651/2/6/1336
Claudins in a primary cultured puffer fish (Tetraodon nigroviridis) gill epitheliumClaudins in a primary cultured puffer fish (Tetraodon nigroviridis) gill epithelium
... Methods Mol Biol. 2011;762:179-94. doi: ...
https://pubmed.ncbi.nlm.nih.gov/21717357/?dopt=Abstract
Claudins and the Kidney | American Society of NephrologyClaudins and the Kidney | American Society of Nephrology
Regulation of claudins by post-translational modifications and cell signaling cascades. In: Claudins, edited by Yu AS, ... Claudins in Human Kidney Diseases. The first inherited disorder of claudins to be identified was FHHNC.70 This autosomal ... Role of Claudins in the Aldosterone-Sensitive Distal Nephron. *Regulation of ASDN Claudins by Aldosterone and With-No-Lysine ... Expression of Claudins in the Kidney. Most claudins are expressed in the renal tubule. Each segment and cell expresses multiple ...
https://jasn.asnjournals.org/content/26/1/11
Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. -...Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. -...
Rabbit polyclonal antibodies were produced against peptides from claudins 2 through 5. The distribution of individual claudins ... Claudins have very different expression patterns among and within gastrointestinal tissues. We propose these patterns underlie ... Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut.. ... and the finding that some claudins can be junctional, lateral, or show a gradient in junctional vs. lateral localization along ...
https://www.ncbi.nlm.nih.gov/pubmed/11159882?dopt=Abstract
Shop Claudins: Methods And ProtocolsShop Claudins: Methods And Protocols
not a shop Claudins: Methods while we focus you in to your property Y. The Web request that you received is only a responding ... The shop Claudins: Methods is on the Deep gala of the Warwalks by the Wasp-kinden bunch. walked-with-purpose of the Apt argues ... shop Claudins: knows near, non-critical, and provides us help you better! challenge a website to destroy a s plan. age agents 1 ... re-equip shop Claudins: Methods and across the something. That accepted to teach a mass teacher. But it has back a hundred ...
http://katrinacottagehousing.org/book.php?q=shop-Claudins%3A-Methods-and-Protocols.html
Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely...Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely...
Tight junction-related structures in the absence of a lumen: occludin, claudins and tight junction plaque proteins in densely ... Much to our surprise, however, we have now also discovered several major TJ proteins (claudins 1 and 4, occludin, cingulin, ...
https://pubmed.ncbi.nlm.nih.gov/14533737/?dopt=Abstract
Mucosal Expression of Claudins 2, 3 and 4 in Proximal and Distal Part of Duodenum in Children with Celiac Disease - Celiac.comMucosal Expression of Claudins 2, 3 and 4 in Proximal and Distal Part of Duodenum in Children with Celiac Disease - Celiac.com
Celiac.com 03/15/2010 A team of researchers recently set out to investigate mucosal expression of claudins 2, 3 and 4 in the ... Mucosal Expression of Claudins 2, 3 and 4 in Proximal and Distal Part of Duodenum in Children with Celiac Disease ... Mucosal Expression of Claudins 2, 3 and 4 in Proximal and Distal Part of Duodenum in Children with Celiac Disease ... Mucosal Expression of Claudins 2, 3 and 4 in Proximal and Distal Part of Duodenum in Children with Celiac Disease ...
https://www.celiac.com/articles.html/mucosal-expression-of-claudins-2-3-and-4-in-proximal-and-distal-part-of-duodenum-in-children-with-celiac-disease-r1625/
Expression and localization of claudins-3 and -12 in transformed human brain endothelium - Open Research OnlineExpression and localization of claudins-3 and -12 in transformed human brain endothelium - Open Research Online
... for the expression of brain endothelial specific claudins-3 and -12. Findings: hCMEC/D3 cells express claudins-3 and -12. ... Expression and localization of claudins-3 and -12 in transformed human brain endothelium.. Fluids and barriers of the CNS, 9 p ... blood brain barrier (BBB); hCMEC/D3; claudins; tight junction; statins. Academic Unit/School:. Faculty of Science, Technology, ... Expression and localization of claudins-3 and -12 in transformed human brain endothelium ...
http://oro.open.ac.uk/34224/
E7 oncoprotein from human papillomavirus 16 alters claudins expression and the sealing of epithelial tight junctionsE7 oncoprotein from human papillomavirus 16 alters claudins expression and the sealing of epithelial tight junctions
For example, in lung squamous cell carcinomas claudins -1, -2, -4 and -7 are expressed, while claudins -2, -3, -4, -5 and -7 ... the role of claudins, in particular claudins -1 (136,137), -2 (46,125,138), -4 (46,125,126) and -10 (33,139) has been ... claudins -2, -3 and -4), even though they are no longer present at the cell borders (23). With respect to claudins, there are ... Claudins -1, -4, -5 and -7 are expressed in the squamous cell carcinomas found in the oral cavity, while claudin-1 is expressed ...
https://www.spandidos-publications.com/10.3892/ijo.2020.5105
Differential Expression Patterns of Claudins, Tight Junction Membrane Proteins, in Mouse Nephron Segments | American Society of...Differential Expression Patterns of Claudins, Tight Junction Membrane Proteins, in Mouse Nephron Segments | American Society of...
Figure 7. Claudins expressed in the thin ascending limb of Henle. In addition to claudin-8 (Figure 3), claudin-3 and -4 were ... B) Claudins expressed in the collecting duct. In addition to claudin-8 (Figure 3), claudin-3 and -4 were concentrated at TJ of ... Figure 6. Claudins expressed in the thin descending limb of Henle. Only claudin-2 was detected in the thin descending limbs of ... Claudins, with molecular masses of approximately 23 kD, comprise a multigene family consisting of ,20 members (3,10-12). When ...
https://jasn.asnjournals.org/content/13/4/875
Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins...Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins...
... occludin and claudins (Furuse et al., 1993; Furuse et al., 1998a; Furuse et al., 1998b). Both occludin and claudins bear four ... Claudins and occludin are thought to constitute the backbone of TJ strands and to modulate some functions of TJs, respectively ... Claudins and occludin are integral membrane proteins localized at tight junctions, which are responsible for establishing and ... Tsukita, S. and Furuse, M. (1999b). Occludin and claudins in tight-junction strands: leading or supporting players? Trend Cell ...
https://jcs.biologists.org/content/116/10/1959?ijkey=4a100594671c35ef9c639f6560b78757bb121133&keytype2=tf_ipsecsha
Effect of claudins 6 and 9 on paracellular permeability in MDC...Effect of claudins 6 and 9 on paracellular permeability in MDC...
Effect of claudins 6 and 9 on paracellular permeability in MDCK II cells.: The neonatal proximal tubule has a lower ... Effect of claudins 6 and 9 on paracellular permeability in MDCK II cells.. Authors * Sas, David ... We transfected claudins 6 and 9 into Madin-Darby canine kidney II (MDCK II) cells and performed electrophysiological studies to ... Expression of claudins 6 and 9 resulted in an increased transepithelial resistance, decreased chloride permeability, and ...
https://www.mysciencework.com/publication/show/effect-claudins-6-9-paracellular-permeability-mdck-ii-cells-2c27380e
Claudins in intestinesClaudins in intestines
July 2013). Claudins in intestines. Tissue Barriers, (1:3), p.1-14. Retrieved from http://hdl.handle.net/10342/5297 Display/ ... Lu, Zhe and Ding, Lei and Lu, Qun and Chen, Yan-Hua, "Claudins in intestines," Tissue Barriers 1, no. 3 (July 2013), http://hdl ... Claudins in intestines. Tissue Barriers. July 2013; 1(3) 1-14. http://hdl.handle.net/10342/5297. Accessed March 08, 2021. ... "Claudins in intestines". Tissue Barriers. 1:3. (1-14.), July 2013. March 08, 2021. http://hdl.handle.net/10342/5297. ...
https://thescholarship.ecu.edu/handle/10342/5297
Search Results - Claudins.Search Results - 'Claudins.'
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https://voyagercatalog.kumc.edu/Search/Results?lookfor=%22Claudins.%22&type=AllFields&filter%5B%5D=topic_facet%3A%22Patients%22&filter%5B%5D=topic_facet%3A%22Disease%22&filter%5B%5D=topic_facet%3A%22history%22
PubMedPro - claudins colorectal cancerPubMedPro - claudins colorectal cancer
In gastrointestinal tract, claudins are mainly located in the intestinal epithelia; many types of claudins form a network of ... Claudins are transmembrane proteins important for tight junctions. Claudins regulate the paracellular transport and are crucial ... RESULTS:Immunohistochemical staining with claudins antibodies had membranous pattern; claudins expression in adjacent normal ... claudins form tight junctions together with occludin. Several claudins were shown to be up-regulated in various cancer types. ...
https://www.pubmed.pro/favorite?favoriteId=1424
The Diagnostic Role of Claudins in Serous EffusionsThe Diagnostic Role of Claudins in Serous Effusions
... American Journal of Clinical Pathology 2007 Jun;127(6):928-37. [Link] ... We analyzed the diagnostic role of claudins in effusion cytology in 325 effusions, including 218 ovarian, 49 breast, 15 ... Reactive mesothelial cells rarely expressed claudins. Claudin-7 expression was higher in ovarian than in breast adenocarcinoma ...
http://www.mesothelioma-line.com/2007/06/22/the-diagnostic-role-of-claudins-in-serous-effusions/
Claudins and Other Tight Junction Proteins - Comprehensive PhysiologyClaudins and Other Tight Junction Proteins - Comprehensive Physiology
... a significant number of claudins form channels across TJs which feature selectivity for cations (claudins 2, 10b, and 15), ... Claudins in cancer biology. Curr Top Membr 65: 293‐333, 2010. 258.. Van Deurs B, Koehler JK. Tight junctions in the choroid ... The claudins. Genome Biol 10: 235.1‐235.7, 2009. 146.. Lemmers C, Michel D, Lane‐Guermonprez L, Delgrossi MH, Médina E, Arsanto ... C) Model of cis and trans interactions between the claudins 1, 2, 3, 5, and 12 and working hypothesis for TJ assembly. Step 1 ...
http://www.comprehensivephysiology.com/WileyCDA/CompPhysArticle/refId-c110045.html
Expression and localization of claudins-3 and -12 in transformed human brain endothelium | Fluids and Barriers of the CNS |...Expression and localization of claudins-3 and -12 in transformed human brain endothelium | Fluids and Barriers of the CNS |...
... for the expression of brain endothelial specific claudins-3 and -12. hCMEC/D3 cells express claudins-3 and -12. Claudin-3 is ... Expression and localization of claudins-3 and -12 in transformed human brain endothelium. *Anja Schrade1,7. , ... The cells express endothelial specific and TJ markers including claudins-1 and -5 [8, 9]. The aim of the present study was to ... Like other claudins, it is regulated by post-translational modifications, a possible reason for the higher molecular weight ...
https://fluidsbarrierscns.biomedcentral.com/articles/10.1186/2045-8118-9-6
Intestinal permeability - WikipediaIntestinal permeability - Wikipedia
Cite journal requires ,journal= (help) Khan, Niamat; Asif, Abdul R. (2015-01-01). "Transcriptional Regulators of Claudins in ...
https://en.wikipedia.org/wiki/Intestinal_permeability
Handbook of Thin Film Deposition / Edition 3 by Krishna Seshan | 9781437778731 | Hardcover | Barnes & Noble®Handbook of Thin Film Deposition / Edition 3 by Krishna Seshan | 9781437778731 | Hardcover | Barnes & Noble®
Claudins This volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of ...
https://www.barnesandnoble.com/w/handbook-of-thin-film-deposition-krishna-seshan/1125544935
Claudins play a role in normal and tumor cell motility | BMC Cell Biology | Full TextClaudins play a role in normal and tumor cell motility | BMC Cell Biology | Full Text
20] that claudins have the potential to interact with MT1-MMP to activate MMP-2, suggest that claudins may increase MMP ... Extra-junctional claudins have been traditionally attributed to storage and mobilization of claudins to and from the tight ... Although it is still unclear how claudins may promote cell motility, it is becoming clear that claudins are indeed playing an ... Claudins -3, -4 and -7 are often present in breast [6-8], ovarian [9-11], and endometrial [12, 13] tumors and are often ...
https://bmccellbiol.biomedcentral.com/articles/10.1186/1471-2121-14-19
Paracellular transport - WikipediaParacellular transport - Wikipedia
Some claudins form tight junction-associated pores that allow paracellular ion transport. The tight junctions have a net ...
https://en.wikipedia.org/wiki/Paracellular_transport
IJMS | Free Full-Text | SCF/C-Kit/JNK/AP-1 Signaling Pathway Promotes Claudin-3 Expression in Colonic Epithelium and Colorectal...IJMS | Free Full-Text | SCF/C-Kit/JNK/AP-1 Signaling Pathway Promotes Claudin-3 Expression in Colonic Epithelium and Colorectal...
Keywords: claudins; colorectal cancer; c-kit; claudin-3; c-Jun N-terminal kinase; activator protein-1 claudins; colorectal ...
http://www.mdpi.com/1422-0067/18/4/765
Tight Junctions in Salivary EpitheliumTight Junctions in Salivary Epithelium
... from the 24 known claudins, only claudins-1, -8, -10, -11, and -16 have been detected in salivary glands. These claudins (i.e ... Claudins. Claudins are members of a multigene family, with , 24 members in humans/rodents [61], presenting a unique tissue ... K. Turksen and T.-C. Troy, "Barriers built on claudins," Journal of Cell Science, vol. 117, no. 12, pp. 2435-2447, 2004. View ... S. Tsukita and M. Furuse, "The structure and function of claudins, cell adhesion molecules at tight junctions," Annals of the ...
https://www.hindawi.com/journals/bmri/2010/278948/
Hypomagnesemia: Background, Pathophysiology, EtiologyHypomagnesemia: Background, Pathophysiology, Etiology
Claudins are the major components of tight-junction strands in the TAL, where the reabsorption of magnesium occurs. [14, 15] ...
https://emedicine.medscape.com/article/2038394-overview
A strategy for enrichment of claudins based on their affinity to Clostridium perfringens enterotoxin | BMC Molecular Biology |...A strategy for enrichment of claudins based on their affinity to Clostridium perfringens enterotoxin | BMC Molecular Biology |...
Numerous proteins were shown to be co-enriched with the CPE-binding claudins, but there are no indications (except for claudins ... The interaction of several claudins with Clostridium perfringens enterotoxin (CPE) has been exploited for an affinity-based ... Immunoblotting and mass spectrometry (MS) experiments demonstrate strong enrichment of the CPE-binding claudins -3, -4 and -7, ... CPE116-319 provides an efficient tool for single step enrichment of different claudins from cell lysates. ...
https://bmcmolbiol.biomedcentral.com/articles/10.1186/1471-2199-10-61/figures/4
A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of...A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of...
The endocytosis of claudins was facilitated when the intercellular motility was upregulated by wounding the cellular sheets. ... The endocytosis of claudins was facilitated when the intercellular motility was upregulated by wounding the cellular sheets. ... The endocytosis of claudins was facilitated when the intercellular motility was upregulated by wounding the cellular sheets. ... The endocytosis of claudins was facilitated when the intercellular motility was upregulated by wounding the cellular sheets. ...
https://keio.pure.elsevier.com/en/publications/a-peculiar-internalization-of-claudins-tight-junction-specific-ad
ProteinsJunctional adhesionEpithelial cellsEndogenous claudinsPermeabilityAdhesionBarrierOccludin and claudinsExtracellularIndividual claudinsLocalizationComponents of TJ strandsStrandsColorectal cancerExpressed in culturedPolyclonal antibodiesProximalProteinCytoplasmPhenotypeExpression patternsCellsPathogenesisTumorigenesisRegulationMethodsDistinctlyIntercellularTissuesStructuralRolesPoresRoleSignificantlyHuman CancerAffinity
Proteins23
  • Claudins are major integral membrane proteins of tight junctions. (mdpi.com)
  • The results promote the development of recombinant cCPE-proteins and CPE-based peptidomimetics to modulate tight junctions for improved drug delivery or to treat tumors overexpressing claudins. (mdpi.com)
  • Claudins are tight-junction membrane proteins that function as both pores and barriers in the paracellular pathway in epithelial cells. (asnjournals.org)
  • Aldosterone and the with-no-lysine (WNK) proteins likely regulate claudins to fine-tune distal nephron salt transport. (asnjournals.org)
  • 2 - 4 Claudins are members of a family of tight-junction membrane proteins that act simultaneously as paracellular pores and barriers and determine the selectivity to small ions and neutral solutes. (asnjournals.org)
  • Much to our surprise, however, we have now also discovered several major TJ proteins (claudins 1 and 4, occludin, cingulin, symplekin, protein ZO-1) and TJ-related structures in specific positions of formations of epithelium-derived tissues that lack any lumen and do not border on luminal or body surfaces. (nih.gov)
  • Claudins (CLDNs), belong to a large group of related adherent junction proteins, which are known to express characteristic patterns in inflammatory disorders. (celiac.com)
  • As the first step in understanding the physiologic functions of claudins (tight junction integral membrane proteins) in nephrons, the expression of claudin-1 to -16 in mouse kidneys was examined by Northern blotting. (asnjournals.org)
  • Two distinct types of integral membrane proteins have been identified as components of TJ strands, namely occludin and claudins ( 9 , 10 ). (asnjournals.org)
  • Claudins and occludin are integral membrane proteins localized at tight junctions, which are responsible for establishing and maintaining epithelial cell polarity. (biologists.org)
  • Claudins are tight-junction proteins between epithelial cells that determine paracellular permeability characteristics of epithelia. (mysciencework.com)
  • Claudins are key integral proteins of the tight junction. (biomedcentral.com)
  • Claudins are important transmembrane proteins in tight junctions. (biomedcentral.com)
  • The major TJ proteins are the transmembrane proteins claudins, occludin, and junctional adhesion molecules (JAMs) [ 21 - 23 ]. (hindawi.com)
  • Claudins are integral membrane proteins and components of tight junction strands. (genecards.org)
  • Recent investigations have focused on tight junction proteins, belonging to the claudin family (claudins-1 to -27 in humans) and the newly defined group of TAMP (three proteins: occludin, Marvel-D2, and tricellulin). (wiley.com)
  • TJs lay in the apical domain of epithelial cells and are mainly composed by transmembrane proteins such as occludin, claudins, JAMs, and tricellulin, that are associated with the cytoplasmic plaque formed by proteins from the MAGUK family, such as ZO-1/2/3, connecting TJ to the actin cytoskeleton, and cingulin and paracingulin connecting TJ to the microtubule network. (frontiersin.org)
  • Most of the claudins (claudin-12 being the exception) have a C-terminal PDZ-binding motif that can interact with other PDZ domain proteins, such as scaffolding protein, ZO-1, -2 and -3 [ PMID: 24665401 ]. (ebi.ac.uk)
  • Members of several gene families are important for blastocyst formation, including claudins, zonal occludins (TJ proteins), occludins, jam proteins, cell polarity proteins, Na/K-ATPases and aquaporins. (biologists.org)
  • Claudins are adhesion proteins localized at tight junctions (TJs). (aacrjournals.org)
  • By contrast, in MDCK I cells, PMA treatment resulted in redistribution of claudins 1, 3, 4 and 5 from the TJ and in reorganization of the proteins into more insoluble complexes. (deepdyve.com)
  • Yu, Alan 2007-05-22 00:00:00 Claudins are transmembrane proteins of the tight junction that determine and regulate paracellular ion permeability. (deepdyve.com)
  • In this review the authors summarize the major novel findings of a dysfunctional skin barrier in AD, with emphasis on tight junction components, such as claudins and on proteins of the keratinocyte differentiation, such as filaggrin. (minervamedica.it)
Junctional adhesion2
  • Tight junctions are composed of the junctional adhesion molecules, claudins (CLDNs) and occludins [ 3 - 5 ]. (pubmedcentralcanada.ca)
  • The main components of tight junctions are claudins, occludins, and junctional adhesion molecules (JAMs). (thermofisher.com)
Epithelial cells4
  • When Snail was overexpressed in cultured mouse epithelial cells, EMT was induced with concomitant repression of the expression of claudins and occludin not only at the protein but also at the mRNA level. (biologists.org)
  • To elucidate a potential function for claudins outside of their traditional role in tight junctions, subcellular localization of claudin-4 was determined in normal mammary epithelial cells as well as breast and ovarian cancer cell lines and the effects of a claudin mimic peptide on cell motility were determined. (biomedcentral.com)
  • These findings suggest that this peculiar internalization of claudins plays a crucial role in the remodeling of TJs, and that the fine regulation of this endocytosis is important for TJs to seal the intercellular space of epithelial cells that are moving against adjacent cells within cellular sheets. (elsevier.com)
  • Our findings show that PKC activation targets in characteristic ways the expression patterns, destination, detergent solubility and phosphorylation state of claudins in epithelial cells with different capacities to form an epithelial barrier. (deepdyve.com)
Endogenous claudins3
  • When TJs between two adjacent cells decreased in length during this remodeling, GFP-claudin-3 was frequently pinched off as a granular structure from GFP-positive TJs together with endogenous claudins. (elsevier.com)
  • The effect of single amino acid substitutions of the second ECL of Cld5 were studied in cells expressing various other endogenous claudins except Cld5. (hu-berlin.de)
  • Unlike in MDCK II cells, induction of claudin-8 in MDCK I cells (which did not affect levels of endogenous claudins) did not alter paracellular ion permeability. (deepdyve.com)
Permeability10
  • In the kidney, claudins determine the permeability and selectivity of different nephron segments along the renal tubule. (asnjournals.org)
  • It is widely believed that the specific set of claudins expressed by each nephron segment determines the unique paracellular permeability properties of that segment. (asnjournals.org)
  • Effect of claudins 6 and 9 on paracellular permeability in MDC. (mysciencework.com)
  • Expression of claudins 6 and 9 resulted in an increased transepithelial resistance, decreased chloride permeability, and decreased P(Na)/P(Cl) and P(HCO3)/P(Cl). (mysciencework.com)
  • These findings constitute the first characterization of the permeability characteristics of claudins 6 and 9 in a cell model and may explain why the neonatal proximal tubule has lower permeability to chloride and higher resistance than the adult proximal tubule. (mysciencework.com)
  • Claudins are major determinants of TJ permeability. (bireme.br)
  • Claudin-4 was the first claudin whose involvement in the TJ permeability in cultured cells was directly demonstrated, but the permeability properties of individual claudins including claudin-4 are still incompletely clarified. (bireme.br)
  • Our results suggest the need for further knockout analysis to reveal the permeability properties of individual claudins. (bireme.br)
  • Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. (genecards.org)
  • Claudins create a barrier to paracellular permeability, and claudin-5 gene deletion is lethal because of loss of blood-brain barrier integrity ( 14 ). (diabetesjournals.org)
Adhesion2
  • Recent evidence shows that claudins, a large family (at least 24 members) of intercellular adhesion molecules, form the seal and its variable pore-like properties. (nih.gov)
  • Because the gene encoding E-cadherin was also reported to be repressed by Snail, we concluded that EMT was associated with the simultaneous repression of the genes encoding E-cadherin and claudins/occludin (i.e. the expression of adherens and tight junction adhesion molecules, respectively). (biologists.org)
Barrier2
  • The aim of this study was to characterize the hCMEC/D3 cell line, an in vitro model of the human Blood Brain Barrier (BBB) for the expression of brain endothelial specific claudins-3 and -12. (open.ac.uk)
  • Although the structure and functions of the 27 different subtypes [ 1 ] of claudin are not fully understood, the tight junction barrier properties of claudins have been well characterized. (biomedcentral.com)
Occludin and claudins3
  • Both occludin and claudins have four transmembrane domains, but they demonstrate no sequence similarity with each other. (asnjournals.org)
  • Both occludin and claudins bear four transmembrane domains but do not show any sequence similarity with each other. (biologists.org)
  • Occludin and claudins in tight-junction strands: leading or supporting players? (ebi.ac.uk)
Extracellular3
  • The C-terminal region (cCPE) binds to the second extracellular loop of a subset of claudins. (mdpi.com)
  • Claudins are thought to polymerize to form continuous strands along the lateral membrane of one cell while the extracellular domains of claudins on adjacent cells bridge the paracellular space to interact with each other, much like the teeth of a zipper. (asnjournals.org)
  • The second extracellular loop of claudins is able to interact with the extracellular environment to promote normal and tumor cell motility when it is not associated with tight junction structures. (biomedcentral.com)
Individual claudins1
  • The distribution of individual claudins was detected by immunoblotting, and their cell type and subcellular localization were determined by immunofluorescence on cryosections of rat liver, pancreas, stomach, and small and large intestine. (nih.gov)
Localization5
  • Among differences in the gut are a crypt-to-villus decrease in claudin 2, a highly restricted expression of claudin 4 to colonic surface cells, and the finding that some claudins can be junctional, lateral, or show a gradient in junctional vs. lateral localization along the crypt-to-villus surface axis. (nih.gov)
  • The aim of the present study was to establish the protein expression and localization pattern of the other brain endothelial specific claudins-3 and -12 in the hCMEC/D3 cell line. (biomedcentral.com)
  • We found that claudin-4 knockout has no apparent effect on the localization of other claudins and electrophysiological properties in MDCK II cells. (bireme.br)
  • Claudin-4 knockout in addition to claudin-2 knockout slightly increased the localization of other claudins at TJs but showed no obvious effects on the electrophysiological properties in MDCK II cells. (bireme.br)
  • The localization of claudins was visualized with immunofluorescent staining. (arvojournals.org)
Components of TJ strands2
  • When each claudin species or occludin was overexpressed in mouse L fibroblasts, claudin molecules, but not occludin, were polymerized within the plasma membranes to reconstitute paired TJ strands, indicating that claudins are major structural components of TJ strands ( 13 ). (asnjournals.org)
  • We examined the expression pattern of claudins, the major components of TJ strands, in these cells: claudin-1 and -4 were expressed both in MDCK I and II cells, whereas the expression of claudin-2 was restricted to MDCK II cells. (nih.gov)
Strands1
  • Claudins, comprising a multigene family, constitute tight junction (TJ) strands. (semanticscholar.org)
Colorectal cancer3
  • Cell membrane staining intensity of all claudins was found significantly lower in colorectal cancer tissues when compared to paired normal mucosa (p = 0.001). (diva-portal.org)
  • In normal mucosa, cytoplasm showed no staining for claudins in any patient, whereas in paired colorectal cancer tissues, significant cytoplasmic staining appeared both for claudin 1 (p = 0.04) and claudin 4 (p = 0.01). (diva-portal.org)
  • Colorectal cancer cells showed dystopic cytoplasmic location of claudins. (diva-portal.org)
Expressed in cultured1
  • This evidence comes from the study of claudins expressed in cultured epithelial cell models, genetically altered mice, and human mutants. (nih.gov)
Polyclonal antibodies1
  • Rabbit polyclonal antibodies were produced against peptides from claudins 2 through 5. (nih.gov)
Proximal3
  • In the proximal tubule, claudins have a role in the bulk reabsorption of salt and water. (asnjournals.org)
  • Celiac.com 03/15/2010 - A team of researchers recently set out to investigate mucosal expression of claudins 2, 3 and 4 in the proximal and distal parts of duodenum in children with celiac disease. (celiac.com)
  • We have previously described the presence of two claudin isoforms, claudins 6 and 9, in the neonatal proximal tubule and subsequent reduction of these claudins during postnatal maturation. (mysciencework.com)
Protein3
  • Although claudins are well-known apical TJ protein, recent antibody-based research indicated that many claudins, including claudin-7, aren't only localized on the apical TJs but likewise have a solid basolateral membrane distribution in the epithelia of varied tissue [14C16]. (recob-tlse.org)
  • Claudins are the largest and most important protein family within the TJ. (hu-berlin.de)
  • This protein has four membrane spanning domains, similarly to claudins. (thermofisher.com)
Cytoplasm1
  • no information has been given on the recruitment of claudins from cytoplasm to tight junction. (frontiersin.org)
Phenotype1
  • Our findings demonstrate that claudin overexpression studies measure the combined effect of alterations in both endogenous and exogenous claudins, thus explaining the dependence of the phenotype on the host cell line. (deepdyve.com)
Expression patterns2
  • Claudins have very different expression patterns among and within gastrointestinal tissues. (nih.gov)
  • These segment-specific expression patterns of claudins are discussed, with special reference to the physiologic functions of tight junctions in nephrons. (asnjournals.org)
Cells11
  • The involvement of claudins in tumor progression was suggested by their important role in the migration, invasion and metastasis of cancer cells in a tissue-dependent manner. (mdpi.com)
  • Recent studies have shown that they play a role in epithelial to mesenchymal transition (EMT), the formation of cancer stem cells or tumor-initiating cells (CSCs/TICs), and chemoresistance, suggesting that claudins are promising targets for the treatment of chemoresistant and recurrent tumors. (mdpi.com)
  • hCMEC/D3 cells express claudins-3 and -12. (open.ac.uk)
  • In the present study the role of human papillomavirus (HPV) 16 E7 oncoprotein on the sealing of TJs was investigated and also the expression level of claudins in mouse cervix and in epithelial Madin‑Darby Canine Kidney (MDCK) cells. (spandidos-publications.com)
  • In MDCK cells the stable expression of E7 increased the space between adjacent cells and altered the architecture of the monolayers, induced the development of an acute peak of transepithelial electrical resistance accompanied by a reduced expression of claudins ‑1, ‑2 and ‑10, and an increase in claudin‑4. (spandidos-publications.com)
  • We transfected claudins 6 and 9 into Madin-Darby canine kidney II (MDCK II) cells and performed electrophysiological studies to determine the resultant changes in physiological characteristics of the cells. (mysciencework.com)
  • 001). Reactive mesothelial cells rarely expressed claudins. (mesothelioma-line.com)
  • Although over expression of claudins is well documented in epithelial-derived cancer cells, the role of claudins in tumor promotion has received little attention. (biomedcentral.com)
  • Turksen K. Claudins and cancer stem cells. (springer.com)
  • In HT29 cells, claudins 1, 3, 4 and 5 and possibly claudin 2 were redistributed to apical cell-cell contacts after PKC activation and the amounts of claudins 1, 3 and 5, but not of claudin 2, were increased in cell lysates. (deepdyve.com)
  • Claudins 1 and 4 were phosphorylated in both MDCK I and HT29 cells, but PKC-induced changes in claudin phosphorylation state were detected only in MDCK I cells. (deepdyve.com)
Pathogenesis2
  • It is likely that additional roles for claudins in the pathogenesis of other types of kidney diseases have yet to be uncovered. (asnjournals.org)
  • The investigation of claudins promises to reveal novel fundamental insights into the pathogenesis of many diseases, including acute kidney injury, salt-sensitive hypertension and kidney stone disease. (kumc.edu)
Tumorigenesis1
  • Although their dysregulation in cancer suggests that claudins play a role in tumorigenesis, the exact underlying mechanism remains unclear. (mdpi.com)
Regulation1
  • The critical role of epigenetic mechanisms in the regulation of claudin expression indicates the possible application of epigenetic therapy to target claudins. (mdpi.com)
Methods6
  • She has what the Super shop Claudins: Methods and Protocols of necessary teachers might report and the programs the ebook is: were small and available jap with implementing Socialization of d, or an Description of application to above recipient and Volume with the request that this, forth, gets the Al Saud worry on owner. (katrinacottagehousing.org)
  • They was me to pay with their proceedings in a many shop Claudins: Methods and and to be my Internet too in working them. (katrinacottagehousing.org)
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Distinctly1
  • A potential function for claudins not localized within tight junction structures can also be supported by the observation that during tumor progression, where disruption and loss of tight junction structures is a hallmark characteristic, certain claudin subtypes are distinctly expressed. (biomedcentral.com)
Intercellular1
  • The endocytosis of claudins was facilitated when the intercellular motility was upregulated by wounding the cellular sheets. (elsevier.com)
Tissues1
  • Claudins form the paracellular tight junction seal in epithelial tissues. (ebi.ac.uk)
Structural2
  • Claudins (Cld) form the structural backbone of TJs. (hu-berlin.de)
  • Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins. (nih.gov)
Roles1
  • Kwon, M.J. Emerging Roles of Claudins in Human Cancer. (mdpi.com)
Pores2
  • In the distal nephron, claudins need to form cation barriers and chloride pores to facilitate electrogenic sodium reabsorption and potassium and acid secretion. (asnjournals.org)
  • Some claudins form tight junction-associated pores that allow paracellular ion transport. (wikipedia.org)
Role2
  • A better understanding of the emerging role of claudins in CSC/TICs and chemoresistance may help to develop therapies against recurrent cancers. (mdpi.com)
  • We analyzed the diagnostic role of claudins in effusion cytology in 325 effusions, including 218 ovarian, 49 breast, 15 cervical or endometrial, 10 gastrointestinal, and 8 lung adenocarcinomas and 25 malignant mesotheliomas (MMs). (mesothelioma-line.com)
Significantly1
  • A recently identified claudin-low breast cancer subtype that is characterized by the enrichment of EMT and stem cell-like features is significantly associated with disease recurrence, underscoring the importance of claudins as predictors of tumor recurrence. (mdpi.com)
Human Cancer1
Affinity1
  • The toxin binds with weak affinity to claudin-1 and -2 but contribution of these weak binding claudins to CPE-mediated disease is questionable. (mdpi.com)
Handbook of Thin Film Deposition / Edition 3 by Krishna Seshan | 9781437778731 | Hardcover | Barnes & Noble®
Handbook of Thin Film Deposition / Edition 3 by Krishna Seshan | 9781437778731 | Hardcover | Barnes & Noble® (barnesandnoble.com)
IJMS | Free Full-Text | SCF/C-Kit/JNK/AP-1 Signaling Pathway Promotes Claudin-3 Expression in Colonic Epithelium and Colorectal...
IJMS | Free Full-Text | SCF/C-Kit/JNK/AP-1 Signaling Pathway Promotes Claudin-3 Expression in Colonic Epithelium and Colorectal... (mdpi.com)
Claudins and the Kidney | American Society of Nephrology
Claudins and the Kidney | American Society of Nephrology (jasn.asnjournals.org)
Hypomagnesemia: Background, Pathophysiology, Etiology
Hypomagnesemia: Background, Pathophysiology, Etiology (emedicine.medscape.com)
JCI - Paracellular epithelial sodium transport maximizes energy efficiency in the kidney
JCI - Paracellular epithelial sodium transport maximizes energy efficiency in the kidney (jci.org)
Targeting Therapeutics Across the Blood Brain Barrier (BBB), Prerequisite Towards Thrombolytic Therapy for Cerebrovascular...
Targeting Therapeutics Across the Blood Brain Barrier (BBB), Prerequisite Towards Thrombolytic Therapy for Cerebrovascular... (link.springer.com)
MiR-1303 Targets Claudin-18 Gene to Modulate Proliferation and Invasion of Gastric Cancer Cells | SpringerLink
MiR-1303 Targets Claudin-18 Gene to Modulate Proliferation and Invasion of Gastric Cancer Cells | SpringerLink (link.springer.com)
Disease-associated mutations of claudin-19 disrupt retinal neurogenesis and visual function | Communications Biology
Disease-associated mutations of claudin-19 disrupt retinal neurogenesis and visual function | Communications Biology (nature.com)
Genetic causes of hypomagnesemia, a clinical overview | SpringerLink
Genetic causes of hypomagnesemia, a clinical overview | SpringerLink (link.springer.com)
Section 4 Flashcards by | Brainscape
Section 4 Flashcards by | Brainscape (brainscape.com)
Genes | Free Full-Text | Principles of Genetic Engineering
Genes | Free Full-Text | Principles of Genetic Engineering (mdpi.com)
Barriers and Channels Formed by Tight Junction Proteins I, Volume 1257 | Wiley
Barriers and Channels Formed by Tight Junction Proteins I, Volume 1257 | Wiley (wiley.com)
Pathology and new players in the pathogenesis of brain edema | SpringerLink
Pathology and new players in the pathogenesis of brain edema | SpringerLink (link.springer.com)
PNAS Plus Significance Statements | PNAS
PNAS Plus Significance Statements | PNAS (pnas.org)
Tight Junctions - 2nd Edition - Marcelino Cereijido - James M. Ander
Tight Junctions - 2nd Edition - Marcelino Cereijido - James M. Ander (routledge.com)
Frontiers | Osmoregulation in Barnacles: An Evolutionary Perspective of Potential Mechanisms and Future Research Directions |...
Frontiers | Osmoregulation in Barnacles: An Evolutionary Perspective of Potential Mechanisms and Future Research Directions |... (frontiersin.org)
Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase ...
Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase ... (pnas.org)
JCI - Epithelial HIF-1α/claudin-1 axis regulates barrier dysfunction in eosinophilic esophagitis
JCI - Epithelial HIF-1α/claudin-1 axis regulates barrier dysfunction in eosinophilic esophagitis (jci.org)
Snail-induced claudin-11 prompts collective migration for tumour progression | Nature Cell Biology
Snail-induced claudin-11 prompts collective migration for tumour progression | Nature Cell Biology (nature.com)
Epithelial CD47 is critical for mucosal repair in the murine intestine in vivo | Nature Communications
Epithelial CD47 is critical for mucosal repair in the murine intestine in vivo | Nature Communications (nature.com)
Frontiers | Novobiocin, a Newly Found TRPV1 Inhibitor, Attenuates the Expression of TRPV1 in Rat Intestine and Intestinal...
Frontiers | Novobiocin, a Newly Found TRPV1 Inhibitor, Attenuates the Expression of TRPV1 in Rat Intestine and Intestinal... (frontiersin.org)
The Role of Tight Junctions and Aquaporins in Skin Dryness | SpringerLink
The Role of Tight Junctions and Aquaporins in Skin Dryness | SpringerLink (link.springer.com)
Activation of the renal Na+:Cl− cotransporter by angiotensin II is a WNK4-dependent process | PNAS
Activation of the renal Na+:Cl− cotransporter by angiotensin II is a WNK4-dependent process | PNAS (pnas.org)
Glucose Transporters in Retinal Pigment Epithelium Development | SpringerLink
Glucose Transporters in Retinal Pigment Epithelium Development | SpringerLink (link.springer.com)
Plus it
Plus it (cancerres.aacrjournals.org)
Changes in the distribution pattern of Claudin tight junction proteins during the progression of mouse skin tumorigenesis | BMC...
Changes in the distribution pattern of Claudin tight junction proteins during the progression of mouse skin tumorigenesis | BMC... (bmccancer.biomedcentral.com)