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.
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.
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.
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)
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.
A MARVEL domain protein that plays an important role in the formation and regulation of the TIGHT JUNCTION paracellular permeability barrier.
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.
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.
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.
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.
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.
A 195-kDa zonula occludens protein that is distinguished by the presence of a ZU5 domain at the C-terminal of the molecule.
A family of proteins that play a role in TIGHT JUNCTION formation by binding to and anchoring proteins to the ACTIN CYTOSKELETON.
The most common etiologic agent of GAS GANGRENE. It is differentiable into several distinct types based on the distribution of twelve different toxins.
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
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.
Proteins that take part in the formation or structure of TIGHT JUNCTIONS.
The functional units of the kidney, consisting of the glomerulus and the attached tubule.
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.
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)
An epithelial cell line derived from a kidney of a normal adult female dog.
The resistance to the flow of either alternating or direct electrical current.
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
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.
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.
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.

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)

Keratosis, actinic can occur on any sun-exposed area of the body, but it is most common on the face, ears, neck, hands, and arms. It typically develops in people who have fair skin, light hair, and light eyes, as well as those who spend a lot of time outdoors or live in sunny climates.

The symptoms of keratosis, actinic can vary depending on the severity of the condition, but may include:

* Scaly, rough, or crusty patches on the skin
* Redness, itching, or burning sensations on the affected areas
* Thickening and darkening of the skin in advanced cases
* Open sores or ulcers in severe cases

Keratosis, actinic can be diagnosed through a physical examination of the skin and may involve a biopsy to rule out other conditions. Treatment typically involves measures to protect the skin from further sun exposure, such as using sunscreen, wearing protective clothing, and seeking shade when the sun is strongest. In some cases, topical creams or ointments may be prescribed to help reduce inflammation and promote healing.

Prevention is key in avoiding keratosis, actinic, as it can be a chronic condition that can worsen over time if left untreated. Protecting the skin from sun exposure and seeking medical attention if symptoms persist or worsen can help prevent complications and improve quality of life for those affected by this condition.

It belongs to the group of claudins. Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial ... Swisshelm K, Macek R, Kubbies M (2005). "Role of claudins in tumorigenesis". Adv. Drug Deliv. Rev. 57 (6): 919-28. doi:10.1016/ ... with the COOH termini of claudins". J. Cell Biol. 147 (6): 1351-63. doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346. ...
Claudins seem to be on a tissue specific manner, because some of them are expressed only in a specific cell type. Claudin 11 is ... Claudins also have a function in a signaling of the cell adhesion, for example Cldn 7 binds directly to adhesion molecule EpCAM ... Most types of claudins have more than two isoforms, that have a distinguish size or function. The specific combination of these ... The C-terminal domain of claudins is required for their stability and targeting. This domain contains PDZ-binding motif, that ...
2004). "Expression patterns of claudins, tight junction adhesion molecules, in the inner ear". Hear. Res. 187 (1-2): 25-34. doi ... It belongs to the group of claudins. GRCh38: Ensembl release 89: ENSG00000157224 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... 2002). "Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments". J. Am. Soc ...
It belongs to the group of claudins. GRCh38: Ensembl release 89: ENSG00000171217 - Ensembl, May 2017 GRCm38: Ensembl release 89 ...
It belongs to the group of claudins. This gene encodes an integral membrane protein, which belongs to the claudin family. The ... 2000). "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins". J. ...
It belongs to the group of claudins; claudins are cell-cell junction proteins that keep that maintains cell- and tissue-barrier ...
It belongs to the group of claudins. This gene encodes a member of the claudin family. Claudins are integral membrane proteins ... Poliak S, Matlis S, Ullmer C, Scherer SS, Peles E (2002). "Distinct claudins and associated PDZ proteins form different ... with the COOH termini of claudins". J. Cell Biol. 147 (6): 1351-63. doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346. ...
It belongs to the group of claudins. Claudins, such as CLDN7, are involved in the formation of tight junctions between ... 2000). "Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins". J. ...
It belongs to the group of claudins. This gene is expressed in the inner ear, olfactory epithelium, and anterior pituitary ... 2004). "Expression patterns of claudins, tight junction adhesion molecules, in the inner ear". Hear. Res. 187 (1-2): 25-34. doi ... 2002). "Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments". J. Am. Soc ...
2000). "Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins". J. ... It belongs to the group of claudins. GRCh38: Ensembl release 89: ENSG00000156284 - Ensembl, May 2017 GRCm38: Ensembl release 89 ...
It belongs to the group of claudins. GRCh38: Ensembl release 89: ENSG00000177300 - Ensembl, May 2017 GRCm38: Ensembl release 89 ...
It belongs to the group of claudins. This gene encodes a member of the claudin family. Claudins are integral membrane proteins ... 2000). "Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight ...
It belongs to the group of claudins. CLDN18 belongs to the large claudin family of proteins, which form tight junction strands ...
It belongs to the group of claudins. Claudin-19 has been implicated in magnesium transport. Claudins, such as CLDN19, are ...
2002). "Claudins create charge-selective channels in the paracellular pathway between epithelial cells" (PDF). Am. J. Physiol ... It belongs to the group of claudins. Among its related pathways are Blood-Brain Barrier and Immune Cell Transmigration: VCAM-1/ ... 2002). "Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments". J. Am. Soc ... "Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins". Am. J. ...
2000). "Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins". J. ... It belongs to the group of claudins. The knockout mice of mouse homolog exhibit no phenotype, indicating that claudin-6 is ... 2003). "The renal segmental distribution of claudins changes with development". Kidney Int. 62 (2): 476-87. doi:10.1046/j.1523- ... 2002). "Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments". J. Am. Soc ...
It belongs to the group of claudins. Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial ...
It belongs to the group of claudins. Members of the claudin protein family, such as CLDN2, are expressed in an organ-specific ... 2000). "Direct Binding of Three Tight Junction-Associated Maguks, Zo-1, Zo-2, and Zo-3, with the Cooh Termini of Claudins". J. ... 2004). "Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins". Proc. Natl. Acad ...
Khan, Niamat; Asif, Abdul R. (1 January 2015). "Transcriptional Regulators of Claudins in Epithelial Tight Junctions". ...
Claudins have both cis and trans interactions between cell membranes. Cis-interactions is when claudins on the same membrane ... Claudins span the cellular membrane 4 times, with the N-terminal end and the C-terminal end both located in the cytoplasm, and ... All human claudins (with the exception of Claudin 12) have domains that let them bind to PDZ domains of scaffold proteins. The ... Claudins are a family of proteins which, along with occludin, are the most important components of the tight junctions (zonulae ...
Khan N, Asif AR (2015-01-01). "Transcriptional regulators of claudins in epithelial tight junctions". Mediators of Inflammation ...
Claudins allow for Mg2+ transport via the paracellular pathway; that is, it mediates the transport of the ion through the tight ...
It belongs to a related family of proteins called claudins. The protein encoded by CLDN14 is an integral membrane protein and a ... Van Itallie CM, Gambling TM, Carson JL, Anderson JM (2005). "Palmitoylation of claudins is required for efficient tight- ...
Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ...
Some claudins form tight junction-associated pores that allow paracellular ion transport. The tight junctions have a net ...
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 ...
JAM-1 also regulates the activity of many different claudins within different epithelial cells. Angiogenesis is the generation ...
Claudins were discovered after occludin and are a family of over 27 different members in mammals. They have a molecular weight ... The three major transmembrane proteins are occludin, claudins, and junction adhesion molecule (JAM) proteins. These associate ...
Poliak S, Matlis S, Ullmer C, Scherer SS, Peles E (2002). "Distinct claudins and associated PDZ proteins form different ...
There are three known claudins contained in the septate junctions, Megatrachea (Mega), Sinuous (Sinu) and Kune-kune (Kune). ... Among these three claudins, Kune-kune (Kune) plays a more central role in septate junctions organization and function. There ...
I met Ana 10 years ago, and of course, traveling. She is a wonderful woman, wanting to know everything. Very passionate about traveling and a lover of Italy, she has traveled up and down across the country. But its better if.... ...
The cells remain together with the help of certain proteins like claudins and zona occludin-1. Loss of these cell-cell junction ...
... group in which all five claudins display low expression [27]. The claudin-low subtype was a frequent phenomenon in metaplastic ...
Unfortunately, subclone #45 did not form enterocyte-like cell monolayers due to low expression of claudins and β-actin. However ...
Claudins (CLDNs) are a family of proteins and are important components of tight junctions (TJs) [1], which form a paracellular ... The gene structure and protein expression of claudins. CLDNs are a family of TJ proteins involved in the regulation of the ... Tsukita S, Tanaka H, Tamura A. The Claudins: from tight junctions to biological systems. Trends Biochem Sci. 2019;44(2):141-52. ... The crystal structure of the human Claudin4 gives the basic illustration of the Claudins structure, which contains the same ...
Claudins Medicine & Life Sciences 39% * Thiazides Medicine & Life Sciences 39% View full fingerprint ...
Overgaard CE, Mitchell LA, Koval M. Roles for claudins in alveolar epithelial barrier function. Ann N Y Acad Sci 1257: 167‐174 ... Schlingmann B, Molina SA, Claudins KM. Gatekeepers of lung epithelial function. Semin Cell Dev Biol 42: 47‐57, 2015. ...
Tsukita S, Furuse M. Occludin and claudins in tight-junction strands: leading or supporting players? Trends Cell Biol. 1999;9: ... In contrast to claudins, we showed that occludin was unaffected by C. perfringens and/or CORT administration as has been ... On the interaction of Clostridium perfringens enterotoxin with claudins. Toxins. 2010;2:1336-56. ...
The diagnostic role of claudins in serous effusions. Am J Clin Pathol, 127 (6), 928-37. DOI 10.1309/V025QRN3R9CJGNPX, PubMed ...
Claudins. _. Top Journals Top journals in which articles about this concept have been published. ...
Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ...
Evaluated expression of claudins in gastric cancer and determined their significance for patient outcome. Claudin-3 and claudin ... Female patients and non-smokers express these claudins more commonly suggesting that they may play a part in the carcinogenesis ...
Claudins constitute a family of integral mem brane proteins and have been identified as prominent structural components of TJ ... Nonetheless, theres minor dig this know-how in regards to the romantic relationship of ASK1 and claudins, especially claudin 6 ... Lots of studies have demonstrated that claudins may par ticipate in a number of signal transduction pathways. For example, ...
Dr Dhawan currently focuses her research on claudins, metastasis, tumorigenesis, signal transduction and trafficking, and cell ...
... mutations Epithelial-Mesenchymal Changeover Increased vimentin appearance Decreased E-Cadherin appearance Reduced Claudins 4 & ... Epithelial-Mesenchymal Changeover Increased vimentin manifestation Decreased E-Cadherin manifestation Reduced Claudins 4 & 7 ...
Although a causal relationship between β1 integrin and claudins has not been described, previous in vitro studies demonstrated ...
What is the diagnostic role of claudins in differentiating malignant mesothelioma and reactive mesothelial cells from ... yet it has been shown that claudins are essential and sufficient to form TJ strands.[4] The structure of claudins consists of ... The role of claudins in the differential diagnosis of serosal tumors is limited to 1 study to date. Soini et al[25] analyzed ... Claudins are a family of tight junction (TJ)-specific integral membrane proteins, including more than 20 members to date. TJs, ...
Claudins are discovered to be key players in renal epithelial physiology. They are involved in developmental, physiological, ... Claudins in barrier and transport function-the kidney Yongfeng Gong et al. Pflugers Arch. 2017 Jan. ... Claudins in barrier and transport function-the kidney Yongfeng Gong 1 , Jianghui Hou 2 ... Claudins and the kidney. Yu AS. Yu AS. J Am Soc Nephrol. 2015 Jan;26(1):11-9. doi: 10.1681/ASN.2014030284. Epub 2014 Jun 19. J ...
Claudins are the major components of tight-junction strands in the TAL, where the reabsorption of magnesium occurs. [14, 15] ...
MeSH Terms: Animals; Aquaporin 5/genetics; Aquaporin 5/metabolism; Aquaporins/genetics; Aquaporins/metabolism; Claudins/ ... genetics; Claudins/metabolism; Cystic Fibrosis Transmembrane Conductance Regulator/genetics; Cystic Fibrosis Transmembrane ...
6. [Claudins as prognostic factors of breast cancer].. Szász MA. Magy Onkol; 2012 Sep; 56(3):209-12. PubMed ID: 23139925. [TBL] ...
Claudins in kidney health and disease. Jo CH, Kim S, Kim GH. Jo CH, et al. Kidney Res Clin Pract. 2022 May;41(3):275-287. doi: ...
Assessing the role of claudins in maintaining the integrity of epididymal tight junctions using novel human epididymal cell ...
Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ...
Claudins - Preferred Concept UI. M0534915. Scope note. A large family of transmembrane proteins found in TIGHT JUNCTIONS. They ...
D2.455.426.559.389.127.250.374 Claudins D12.776.543.196 D12.776.543.984.200 Clodronic Acid D2.705.206.200 D2.705.429.500.200 ...
DE caused upregulation (3 to 5-fold) of mRNA transcripts for matrix metalloproteinase 9 (Mmp9), claudins (Cldn1 and Cldn2), and ...
Claudins Preferred Term Term UI T749746. Date04/21/2009. LexicalTag NON. ThesaurusID NLM (2010). ... Claudins Preferred Concept UI. M0534915. Registry Number. 0. Scope Note. A large family of transmembrane proteins found in ... Claudins. Tree Number(s). D12.776.543.940.200. Unique ID. D057167. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/D057167 ...
Claudins Preferred Term Term UI T749746. Date04/21/2009. LexicalTag NON. ThesaurusID NLM (2010). ... Claudins Preferred Concept UI. M0534915. Registry Number. 0. Scope Note. A large family of transmembrane proteins found in ... Claudins. Tree Number(s). D12.776.543.940.200. Unique ID. D057167. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/D057167 ...
Claudins are the major components of tight-junction strands in the TAL, where the reabsorption of magnesium occurs. [14, 15] ...
3-Kinases N0000168724 Clathrin N0000168725 Clathrin Heavy Chains N0000168726 Clathrin Light Chains N0000180272 Claudins ...
Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ... Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ...
Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ... Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical ...
BACKGROUND: Claudins are promising biomarkers for diagnosis and prognosis or targets for treatment. They play a major role in ...
Our current data suggest that claudins may be important for cell motility and invasion. Overall, the identification and ... Since our initial findings, other research groups have found that claudins are dysregulated in many other cancers. ...
Among the transmembrane proteins making up tight junctions are occludin, claudins, tricellulin, and junctional adhesions ( ... Claudins are a family of both tissue- and cell-type-specific proteins considered to be the main structural components of the ...
Here, we profile palmitoylation states of three human claudins, human CD20 and cysteine-engineered prokaryotic KcsA and ...
HN - 2010 BX - Circadian Clock Proteins and Peptides MH - Claudins UI - D057167 MN - D12.776.543.196 MS - A large family of ...
Our group also demonstrated that claudins, the key family of tight-junction sealing proteins, create charge- and size-selective ...
D2.455.426.559.389.127.250.374 Claudins D12.776.543.196 D12.776.543.984.200 Clodronic Acid D2.705.206.200 D2.705.429.500.200 ...
D2.455.426.559.389.127.250.374 Claudins D12.776.543.196 D12.776.543.984.200 Clodronic Acid D2.705.206.200 D2.705.429.500.200 ...
Claudins D12.776.543.984.200 D12.776.543.940.200 Clavulanic Acid D4.75.80.875.99.221.374.160 D3.633.100.300.374.160 Clavulanic ...
Claudins D12.776.543.984.200 D12.776.543.940.200 Clavulanic Acid D4.75.80.875.99.221.374.160 D3.633.100.300.374.160 Clavulanic ...
Claudins D12.776.543.984.200 D12.776.543.940.200 Clavulanic Acid D4.75.80.875.99.221.374.160 D3.633.100.300.374.160 Clavulanic ...
D2.455.426.559.389.127.250.374 Claudins D12.776.543.196 D12.776.543.984.200 Clodronic Acid D2.705.206.200 D2.705.429.500.200 ...
  • Unfortunately, subclone #45 did not form enterocyte-like cell monolayers due to low expression of claudins and β -actin. (aspetjournals.org)
  • Evaluated expression of claudins in gastric cancer and determined their significance for patient outcome. (cusabio.com)
  • 9. Claudins and other tight junction proteins. (nih.gov)
  • The cells remain together with the help of certain proteins like claudins and zona occludin-1. (firstpost.com)
  • Claudins are integral membrane proteins and components of tight junction strands. (nih.gov)
  • Claudins (CLDNs) are a family of proteins and are important components of tight junctions (TJs) [ 1 ], which form a paracellular barrier to control the flow of molecules between cells. (biomedcentral.com)
  • Our group also demonstrated that claudins, the key family of tight-junction sealing proteins, create charge- and size-selective pores through the tight junction to allow tissue-specific ion permeability. (nih.gov)
  • Our current data suggest that claudins may be important for cell motility and invasion. (nih.gov)
  • [ 8 ] Recent studies have shown that the barrier function of claudins can be modulated also through phosphorylation of the serine and/or threonine phosphorylation sites at the carboxy tail by various kinases such as WNK4 [ 9 ] and cyclic adenosine monophosphate dependent protein kinase. (medscape.com)
  • DE caused upregulation (3 to 5-fold) of mRNA transcripts for matrix metalloproteinase 9 (Mmp9), claudins (Cldn1 and Cldn2), and Gfap (1.6-fold) in the OB, suggestive of altered blood-brain barrier integrity and reactive gliosis. (cdc.gov)
  • Since our initial findings, other research groups have found that claudins are dysregulated in many other cancers. (nih.gov)
  • Claudins are a family of tight junction (TJ)-specific integral membrane proteins, including more than 20 members to date. (medscape.com)
  • Claudins are integral membrane proteins and components of tight junction strands. (nih.gov)
  • Although the function of claudins in cancer cells is not clear, recent findings suggest their involvement in cancer cell survival [ 16 ] and invasion [ 20 ] mechanisms. (medscape.com)
  • The expression pattern of claudins varies considerably among cell types and tissues. (medscape.com)
  • The role of claudins in the differential diagnosis of serosal tumors is limited to 1 study to date. (medscape.com)