Tissue‐specific expression of the tight junction proteins claudins and occludin in the rat salivary glands

Peppi, Marcello; Ghabriel, M. N.

doi:10.1111/j.0021-8782.2004.00332.x

Cited by 65 publications

(79 citation statements)

References 38 publications

(53 reference statements)

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“…In these segments, bovine claudin-4 showed distribution both at the TJ and the basolateral membranes. Many investigators have reported basolateral distribution of some claudins, including claudin-4 [1,17,22,23], although the precise roles of claudins in the plasma membrane compartment other than TJ remain unknown; they may simply represent a storage pool capable of being recruited to the TJ when required, or they may have some novel functions in intercellular adhesion and/or adhesion between cells and the extracellular matrix.…”

Section: Claudins Expressed In Tal Of Henle's Loopmentioning

confidence: 99%

Restricted Localization of Claudin-16 at the Tight Junction in the Thick Ascending Limb of Henle's Loop Together with Claudins 3, 4, and 10 in Bovine Nephrons

Ohta

Adachi

Takiguchi

et al. 2006

The Journal of Veterinary Medical Science

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ABSTRACT. Claudin-16 is one of the tight junction protein claudins and has been shown to contribute to reabsorption of divalent cations in the human kidney. In cattle, total deficiency of claudin-16 causes severe renal tubular dysplasia without aberrant metabolic changes of divalent cations, suggesting that bovine claudin-16 has some roles in renal tubule formation and paracellular transport that are somewhat different from those expected from the pathology of human disease. As the first step to clarify these roles, we examined the expression and distribution of claudin-16 and several other major claudin subtypes, claudins 1-4 and 10, in bovine renal tubular segments by immunofluorescence microscopy. Claudin-16 was exclusively distributed to the tight junction in the tubular segment positive for TammHorsfall glycoprotein, the thick ascending limb (TAL) of Henle's loop, and was found colocalized with claudins 3, 4, and 10. This study also demonstrates that bovine kidneys possess segment-specific expression patterns for claudins 2-4 and 10 that are different from those reported for mice. Particularly, distribution of claudin-4 in the TAL and distal convoluted tubules was characteristic of bovine nephrons as were differences in the expression patterns of claudins 2 and 3. These findings demonstrate that the total lack of claudin-16 in the TAL segment is the sole cause of renal tubular dysplasia in cattle and suggest that the tight junctions in distinct tubular segments including the TAL have barrier functions in paracellular permeability that are different among animal species. KEY WORDS: cattle, claudin-16, paracellular pathway, renal tubule, tight junction.J. Vet. Med. Sci. 68 (5): [453][454][455][456][457][458][459][460][461][462][463] 2006 Tight junctions (TJs) are located at the apicalmost region of lateral membranes of epithelial cells, and play a central role in sealing the intercellular space in epithelial cellular sheets. TJs create the primary barrier to the diffusion of solutes and water through the paracellular pathway and maintain cell polarity as a boundary between the apical and basolateral plasma membrane domains [7,26,29,34]. On freeze-fracture electron microscopy, TJs are visualized as a continuous anastomosing network of intramembranous particle strands, i.e., TJ strands, and complementary grooves [28]. The major components of TJ strands are the integral membrane proteins occludin and claudins, all of which have four transmembrane spans and two intervening extracellular loops [19]. Claudins consist of a family of more than 20 homologous subtypes, and they show tissue-specific and segment-specific distribution patterns in epithelia [19,29] such as those of the gastrointestinal tract [23] and renal tubules [15].Among these claudin proteins, claudin-16, formerly paracellin-1, has been shown to be responsible for inherited disease. Various mutations of the CLDN16 gene were reported to be the cause for familial hypomagnesemia with hypercalciuria and nephrocalcinosis (FHHNC) in the human [27]. Simon...

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Section: Claudins Expressed In Tal Of Henle's Loopmentioning

confidence: 99%

Restricted Localization of Claudin-16 at the Tight Junction in the Thick Ascending Limb of Henle's Loop Together with Claudins 3, 4, and 10 in Bovine Nephrons

Ohta

Adachi

Takiguchi

et al. 2006

The Journal of Veterinary Medical Science

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“…Previous data showed that a series of tight junction proteins including zonula occludens-1 (ZO-1), occludin, claudin-1, 23, 24 and 25 exist in rat SMG tissue (Peppi and Ghabriel, 2004). Thus, we examined these components in SMG-C6 cells and found that ZO-1, occludin, claudin-1, 23 and 24 mRNA were expressed, whereas claudin-2 and 25 mRNA were not detected (supplementary material Fig.…”

Section: Trpv1 and Occludin Are Expressed In Smg-c6 Cellsmentioning

confidence: 94%

“…It has been reported that, in addition to the aquaporin-5-mediated transcellular transport, the salivation induced by agonists such as carbachol and isoproterenol also involves increased paracellular permeability (Segawa, 1994;Murakami et al, 2001;Hashimoto and Murakami, 2009). To date, occludin has been found in human, rat and mouse major salivary glands (Peppi and Ghabriel, 2004;Kawedia et al, 2007;Lourenço et al, 2007). In murine submandibular gland (SMG) carcinoma cells, the expression of an N-terminally truncated occludin construct causes a decrease in transepithelial electrical resistance (TER) as well as an increase in paracellular permeability (Bamforth et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Occludin is required for TRPV1-modulated paracellular permeability in the submandibular gland

Cong

Zhang

Yang

et al. 2013

Journal of Cell Science

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SummaryOccludin plays an important role in maintaining tight junction barrier function in many types of epithelia. We previously reported that activation of transient receptor potential vanilloid subtype 1 (TRPV1) in rabbit submandibular gland promoted salivary secretion, partly by an increase in paracellular permeability. We have now explored the role of occludin in TRPV1-modulated paracellular permeability in a rat submandibular gland cell line SMG-C6. Both TRPV1 and occludin were expressed in SMG-C6 cells, and capsaicin induced redistribution of occludin, but not claudin-3, claudin-4 or E-cadherin, from the cell membrane into the cytoplasm. Capsaicin also decreased transepithelial electrical resistance (TER) and increased the Trypan Blue and FITC-dextran flux. Capsazepine (CPZ), a TRPV1 antagonist, inhibited the capsaicin-induced occludin redistribution and TER decrease. Moreover, occludin knockdown by shRNA suppressed, whereas occludin re-expression restored, the TER response to capsaicin. Mechanistically, TRPV1 activation increased ERK1/2 and MLC2 phosphorylation. PD98059, an ERK1/2 kinase inhibitor, abolished the capsaicin-induced MLC2 phosphorylation, whereas ML-7, an MLC2 kinase inhibitor, did not affect ERK1/2 phosphorylation, suggesting that ERK1/2 is the upstream signaling molecule of MLC2. Capsaicin also induced F-actin reorganization, which was abolished by CPZ, PD98059 and ML-7, indicating that TRPV1 activation altered F-actin organization in an ERK1/2-and MLC2-dependent manner. Furthermore, either PD98059 or ML-7 could abolish the capsaicin-induced TER response and occludin redistribution, whereas knockdown of ERK1/2 further confirmed that the TRPV1-modulated paracellular permeability was ERK1/2 dependent. Taken together, these results identified a crucial role of occludin in submandibular epithelial cells, and more importantly, demonstrated that occludin was required to mediate TRPV1-modulated paracellular permeability.

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“…However, Claudin 1 is unexpressed in the luteal endothelial compartment. This is different compared with endothelial cells of the brain and of rat salivary glands (Fujibe et al 2004, Peppi & Ghabriel 2004. In contrast to Claudin 1, Claudin 5 is exclusively localized in the endothelial compartment of the human corpus luteum (Groten et al 2006).…”

Section: Distribution Of Cell Junctional Proteins In the Human Corpusmentioning

confidence: 97%

Regulation of endothelial permeability in the primate corpora lutea: implications for ovarian hyperstimulation syndrome

Herr¹,

Bekes²,

Wulff³

2015

Reproduction

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In a developing human corpus luteum, a closely regulated cellular communication system exists between the luteal steroidogenic cells and endothelial cells. This system guaranties the vascularization process during luteal formation. The process is combined with rapid release of large amounts of progesterone into the bloodstream. The regulation of endothelial proliferation and permeability by LH and human chorionic gonadotropin (hCG) is integral to this process. On the cellular level, endothelial permeability is regulated by intercellular junctions, such as adherens junctions (AJ) and tight junctions (TJ), which act as zipper-like structures between interacting endothelial cells. Several cell junctional proteins are localized to the corpus luteum, including Occludin, Nectin 2, Claudin 1, and Claudin 5, as well as, vascular endothelial (VE)-Cadherin. It has been assumed that regulation of AJ-and TJ-proteins is of particular importance for permeability, and accordingly, for the functionality of the corpus luteum in early pregnancy, because treatment with hCG induces downregulation of juntional proteins in the luteal vessels. The effect of hCG on the adhesive molecules is mediated by VE growth factor (VEGF). On a functional level, the hCG-dependent and VEGF-mediated decrease in junctional proteins causes a decrease in the density of cell-cell closure and, accordingly, an increase in endothelial permeability. In doing so, the different junctional proteins are not only directly influenced by VEGF but also interact among themselves and influence each other reciprocally. Disturbances in this strictly, regulated interactions may explain the development of pathologies with increased vascular permeability, such as the ovarian hyperstimulation syndrome.Reproduction (2015) 149 R71-R79

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Tissue‐specific expression of the tight junction proteins claudins and occludin in the rat salivary glands

Cited by 65 publications

References 38 publications

Restricted Localization of Claudin-16 at the Tight Junction in the Thick Ascending Limb of Henle's Loop Together with Claudins 3, 4, and 10 in Bovine Nephrons

Restricted Localization of Claudin-16 at the Tight Junction in the Thick Ascending Limb of Henle's Loop Together with Claudins 3, 4, and 10 in Bovine Nephrons

Occludin is required for TRPV1-modulated paracellular permeability in the submandibular gland

Regulation of endothelial permeability in the primate corpora lutea: implications for ovarian hyperstimulation syndrome

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