The renal segmental distribution of claudins changes with development

Reyes, José L.; Lamas, Marta; Martín, Dolores; Namorado, María del Carmen; Islas, Socorro; Luna, J.; Tauc, Michel; González‐Mariscal, Lorenza

doi:10.1046/j.1523-1755.2002.00479.x

Cited by 151 publications

(136 citation statements)

References 55 publications

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“…3). This staining pattern is in agreement with the findings of Reyes et al (22). Thyroid hormone treatment did not alter the staining pattern of claudin 2 in proximal tubules in neonate.…”

Section: Resultssupporting

confidence: 93%

Developmental Changes in Proximal Tubule Tight Junction Proteins

et al. 2005

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We demonstrated previously that neonatal proximal tubules have a lower passive paracellular permeability to chloride ions and higher resistance than that of adult proximal tubules. In addition, administration of thyroid hormone to neonates, before the normal maturational increase in serum thyroid hormone levels, prematurely accelerates the developmental increase in chloride permeability to adult levels. To test the hypothesis that there is a maturational change in tight junction proteins and that thyroid hormone mediates these changes, we examined the two known tight junction proteins present in proximal tubules, occludin and claudin 2. Using immunoblot and immunohistochemistry, we demonstrated that claudin 2 has a 4-fold greater abundance in neonatal proximal tubules than in adult tubules. Occludin, however, has a 4-fold greater expression in adult tubules than in neonatal tubules. Administration of thyroid hormone to neonates did not affect claudin 2 expression, occludin expression, or the transepithelial resistance in rat proximal tubule cells in vitro. In conclusion, there are postnatal maturational changes in tight junction proteins. The factors that cause these maturational changes are unknown but unlikely to be due solely to the maturational increase in thyroid hormone.The proximal tubule receives an ultrafiltrate from the glomerulus and reabsorbs two thirds of the ultrafiltrate in a nearly iso-osmotic manner. In addition to active transcellular fluid transport, the proximal tubule reabsorbs solutes via passive diffusion across the paracellular pathway. The early proximal tubule reabsorbs glucose and amino acids and preferentially reabsorbs bicarbonate over chloride ions (1,2), which leaves the luminal fluid delivered to the late proximal tubule with a higher chloride concentration and lower bicarbonate concentration than that in the peritubular plasma (1,2). Passive solute transport is dependent on the gradients that develop between lumen and peritubular capillary and permeability properties of the paracellular pathway.Approximately two thirds of the filtered chloride is reabsorbed by the adult proximal tubule (1,3 active and transcellular and half is passive and paracellular (3-5). Active NaCl transport is mediated by the parallel operation of the Na+/H+ exchanger and a Cl−/base exchanger (3,4). Passive Cl absorption is mediated by diffusion of chloride ions down its concentration gradient generated in the early proximal tubule (6,7). Thus, the permeability properties of the paracellular pathway can affect a significant amount of proximal tubule NaCl transport.Furthermore, the permeability properties of the paracellular pathway serve as a barrier to prevent the back diffusion of glucose, amino acids, phosphate, bicarbonate, and other solutes that are in higher concentration in the peritubular fluid than in the lumen of the late proximal tubule. In previous in vitro rabbit microperfusion studies, our laboratory demonstrated that unlike the adult segment, the neonatal proximal tubule was impermeab...

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“…3). This staining pattern is in agreement with the findings of Reyes et al (22). Thyroid hormone treatment did not alter the staining pattern of claudin 2 in proximal tubules in neonate.…”

Section: Resultssupporting

confidence: 93%

Developmental Changes in Proximal Tubule Tight Junction Proteins

et al. 2005

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“…3 In fact, very few claudin mutations lead to abnormal renal physiology, in spite of the fact that most claudins are expressed within the adult nephron. 13,31,32 This strongly suggests that claudins may function in combination with other claudins to exert their effects on paracellular transport. There is evidence that claudins can both heteromerize and homomerize within tight junctions to influence paracellular transport, 33 but thus far a deeper understanding of how this influences cell and tissue function remains elusive.…”

Section: E964547-8mentioning

confidence: 99%

Claudin-7, -16, and -19 during mouse kidney development

et al. 2014

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Abbreviations: E, embryonic day; P, postnatal; FHHNC, familial hypomagnesaemia with hypercalciuria and nephrocalcinosis; nd, nephric duct; ub, ureteric bud; MET, mesenchymal to epithelial transition.Members of the claudin family of tight junction proteins are critical for establishing epithelial barriers and for the regulation of paracellular transport. To understand their roles during kidney development, we first performed RT-PCR analyses and determined that 23 claudin family members were expressed in embryonic day (E) 13.5 mouse kidneys. Based on their developmental expression and phenotypes in mouse models, we hypothesized that 3 claudin members could affect nephron formation during kidney development. Using whole mount in situ hybridization and immunohistochemistry, we demonstrated that Claudin-7 (Cldn7) was expressed in the nephric duct, the emerging ureteric bud, and in tubules derived from ureteric bud branching morphogenesis. In contrast, Claudin-16 (Cldn16) and Claudin-19 (Cldn19) were expressed at later stages of kidney development in immature renal tubules that become the Loop of Henle. To determine if a loss of these claudins would perturb kidney development, we examined newborn kidneys from mutant mouse models lacking Cldn7 or Cldn16. In both models, we noted no evidence for any congenital renal malformation and quantification of nephron number did not reveal a decrease in nephron number when compared to wildtype littermates. In summary, Cldn7, Cldn16, and Cldn19 are expressed in different epithelial lineages during kidney development. Mice lacking Cldn7 or Cldn16 do not have defects in de novo nephron formation, and this suggests that these claudins primarily function to regulate paracellular transport in the mature nephron.

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“…It is also clear that the patterns of claudin expression along the nephron changes with development, with CLDN-7 and -8 upregulated postnatally. 47 Figure 3. Schematic presentation of interaction possibilities between claudin molecules.…”

Section: The Renal Localization Of Claudinsmentioning

confidence: 99%