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Bernstein, MD, FCAP This article is Part II of a series that explores the physiology, genomics, and the proteomics of water and electrolytes in human and mammalian function in health and disease. In this portion of curation, we examine the role of special proteins at the tight junctions of cells, including the claudins.
Teleost fish living in freshwater are challenged by passive water influx; however the molecular mechanisms regulating water influx in fish are not well understood. The potential involvement of aquaporins AQP and epithelial tight junction proteins in the regulation of transcellular and paracellular water movement was investigated in larval zebrafish Danio rerio.
We observed that the half-time for saturation of water influx K u was 4. These findings suggest a high turnover rate of water between the fish and the environment.
Immunohistochemistry and confocal microscopy revealed that AQP1a1 protein was expressed in cells on the yolk sac epithelium. These findings indicate that the epithelial tight junctions normally act to restrict paracellular water influx. Together, the results of the present study provide direct in vivo evidence that water movement can occur through transcellular routes via AQP ; the paracellular routes may become significant when the paracellular permeability is increased.
Apr 1, ; 7: The functional role of the tight junction protein claudin-b in larval zebrafish Danio rerio was investigated. We showed that claudin-b protein is expressed at epithelial cell-cell contacts on the skin.
Translational gene knockdown of claudin-b protein expression caused developmental defects, including edema in the pericardial cavity and yolk sac.
Claudin-b morphants exhibited an increase in epithelial permeability to the paracellular marker polyethylene glycol PEG and fluorescein isothiocyanate-dextran FD Accumulation of FD-4 was confined mainly to the yolk sac and pericardial cavity in the claudin-b morphants, suggesting these regions became particularly leaky in the absence of claudin-b expression.
Feb ; 2: Freshwater teleosts are challenged by diffusive ion loss across permeable epithelia including gills and skin. Although the mechanisms regulating ion loss are poorly understood, a significant component is thought to involve paracellular efflux through pathways formed via tight junction proteins.
Using a green fluorescent protein-expressing line of transgenic zebrafish, we found that claudin-b was expressed along the lamellar epithelium as well as on the filament in the inter-lamellar regions. Claudin-b also appeared to be associated with other cell types, including the pavement cells.
In the kidney, claudin-b was expressed predominantly in the collecting tubules. Claudin and claudin function in the thick ascending limb.
Hou J, Goodenough DA. Sep ; 19 5: The dissociation of salt and water reabsorption in the TAL serves both to dilute the urine and to establish the corticomedullary osmolality gradient. Active transcellular salt reabsorption results in a lumen-positive transepithelial voltage that drives passive paracellular reabsorption of divalent cations.
Claudins are the key components of the paracellular channel. The paracellular channels in the tight junction have properties of ion selectivity, pH dependence and anomalous mole fraction effects, similar to conventional transmembrane channels.
Claudin and claudin underlie familial hypercalciuric hypomagnesemia with nephrocalcinosis Claudin and claudin play a major role in the regulation of magnesium reabsorption in the thick ascending limb TAL.Unit 2 Managing Paediatric Illness and Injury Level 2 1.
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Irena Rogelj University of Zagreb, Faculty of Agriculture, Zagreb, hrvaška Science Math-Mathematical Literacy and Cross Curricular Competencies through Interdisciplinary, Mathematising and Moddeling Science IP2 Endophytes in Biotechnology and Agriculture FA dr.
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