Abstract
The growing molecular complexity of the tight junction (TJ), its ability to modulate the degree of sealing according to physiological requirements, and the fact that its transepithelial electrical resistance (TER) ranges over several orders of magnitude, indicate that there must be a number of agents modulating its permeability. The interest to find these agents stems from an urgency to make the TJ tighter (e.g., to prevent antigen absorption in autoimmune diseases), or to make it leakier (e.g., to allow the absorption of orally administered pharmaceutical drugs). In the present chapter we discuss three forms of modifying the degree of sealing of the TJ: (1) A peptidic factor extracted from urine that makes the TJ tighter, decreases the cellular content of claudin-2, and prompts the relocalization of claudin-4; (2) An experimentally induced modification of the lipidic composition of the plasma membrane that changes some basic attributes of the TJ; and (3) ouabain, a substance that specifically inhibits Na+,K+-ATPase both as an enzyme and as a ion pump, and induces an inotropic activity in heart muscle fibers. Yet we discuss here a newly found property of ouabain: the triggering of a cascade of phosphorylations that results in the opening of the TJ, as part of an overall cell detachment. Interestingly, at concentrations of ouabain within physiological ranges that do not fully detach the cell, the release of the grip induced by this substance sends specific nuclear addressed molecules (NACos) from the diverse sites of attachment to the nucleus, where they modulate the expression of genes that influence proliferation and differentiation.
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References
Cereijido M, Shoshani L, Contreras RG. Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity. Am J Physiol Gastrointest Liver Physiol 2000; 279:G477–G482.
Cereijido M, Anderson JM. Tight Junctions. 2nd ed. Boca Raton FL: CRC Press; 2001.
Cereijido M, Robbins ES, Dolan WJ et al. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J Cell Biol 1978; 77:853–880.
Cereijido M, Shoshani L, Contreras RG. Cell adhesion, polarity, and epithelia in the dawn of metazoan. Phy Rev 2004; 84, in press.
Gonzalez-Mariscal L, Betanzos A, Nava P et al. Tight junction proteins. Prog Biophys Mol Biol 2003; 81:1–44.
Balda MS, Matter K. Epithelial cell adhesion and the regulation of gene expression. Trends Cell Biol 2003; 13:310–318.
Matter K, Balda MS. Signalling to and from tight junctions. Nat Rev Mol Cell Biol 2003; 4:225–236.
Stelwagen K, Callaghan MR. Regulation of mammary tight junctions through parathyroid hormone-related peptide-induced activation of apical calcium channels. J Endocrinol 2003; 178:257–264.
Hollande F, Lee DJ, Choquet A et al. Adherens junctions and tight junctions are regulated via different pathways by progastrin in epithelial cells. J Cell Sci 2003; 116:1187–1197.
Blum MS, Toninelli E, Anderson JM et al. Cytoskeletal rearrangement mediates human microvascular endothelial tight junction modulation by cytokines. Am J Physiol 1997; 273:H286–H294.
Ma TY, Iwamoto GK, Hoa NT et al. TNF-alpha-induced increase in intestinal epithelial tight junction permeability requires NF-kappa B activation. Am J Physiol Gastrointest Liver Physiol 2004; 286:G367–G376.
Zech JC, Pouvreau I, Cotinet A et al. Effect of cytokines and nitric oxide on tight junctions in cultured rat retinal pigment epithelium. Invest Ophthalmol Vis Sci 1998; 39:1600–1608.
Wong CH, Mruk DD, Lui WY et al. Regulation of blood-testis barrier dynamics: an in vivo study. J Cell Sci 2004; 117:783–798.
Fischer S, Wobben M, Marti HH et al. Hypoxia-induced hyperpermeability in brain microvessel endothelial cells involves VEGF-mediated changes in the expression of zonula occludens-1. Microvasc Res 2002; 63:70–80.
Singh AB, Harris RC. Epidermal growth factor receptor activation differentially regulates claudin expression and enhances transepithelial resistance in Madin-Darby canine kidney cells. J Biol Chem 2004; 279:3543–3552.
Marmorstein AD, Mortell KH, Ratcliffe DR et al. Epithelial permeability factor: a serum protein that condenses actin and opens tight junctions. Am J Physiol 1992; 262:C1403–C1410.
Jaeger MM, Dodane V, Kachar B. Modulation of tight junction morphology and permeability by an epithelial factor. J Membr Biol 1994; 139:41–48.
Gorodeski GI, Goldfarb J. Seminal fluid factor increases the resistance of the tight junctional complex of cultured human cervical epithelium CaSki cells. Fertil Steril 1998; 69:309–317.
Walsh SV, Hopkins AM, Nusrat A. Modulation of tight junction structure and function by cytokines. Adv Drug Deliv Rev 2000; 41:303–313.
Wang Y, Zhang J, Yi XJ et al. Activation of ERK1/2 MAP kinase pathway induces tight junction disruption in human corneal epithelial cells. Exp Eye Res 2004; 78:125–136.
Wang W, Dentler WL, Borchardt RT. VEGF increases BMEC monolayer permeability by affecting occludin expression and tight junction assembly. Am J Physiol Heart Circ Physiol 2001; 280:H434–H440.
Tedelind S, Ericson LE, Karlsson JO et al. Interferon-gamma down-regulates claudin-1 and impairs the epithelial barrier function in primary cultured human thyrocytes. Eur J Endocrinol 2003; 149:215–221.
Nitz T, Eisenblatter T, Psathaki K et al. Serum-derived factors weaken the barrier properties of cultured porcine brain capillary endothelial cells in vitro. Brain Res 2003; 981:30–40.
Chiba H, Gotoh T, Kojima T et al. Hepatocyte nuclear factor (HNF)-4alpha triggers formation of functional tight junctions and establishment of polarized epithelial morphology in F9 embryonal carcinoma cells. Exp Cell Res 2003; 286:288–297.
Chang C, Wang X, Caldwell RB. Serum opens tight junctions and reduces ZO-1 protein in retinal epithelial cells. J Neurochem 1997; 69:859–867.
Siliciano JD, Goodenough DA. Localization of the tight junction protein, ZO-1, is modulated by extracellular calcium and cell-cell contact in Madin-Darby canine kidney epithelial cells. J Cell Biol 1988; 107:2389–2399.
Liu Y, Nusrat A, Schnell FJ et al. Human junction adhesion molecule regulates tight junction resealing in epithelia. J Cell Sci 2000; 113 (Pt 13):2363–2374.
Reuss L. Tigbt junction permeability to ions and water. In: Cereijido M, Anderson JM, eds. Tight Junctions. 2nd ed. Boca Raton: CRC Press, 2001:61–88.
Reuss L, Finn AL. Electrical properties of the cellular transepithelial pathway in Necturus gallbladder. I. Circuit analysis and steady-state effects of mucosal solution ionic substitutions. J Membr Biol 1975; 25:115–139.
Hegel U, Fromter E, Wick T. Der elektrische wandwiderstand des proximalen konvolutes der rattenniere. Pflügers Arch 1967; 294:274–290.
Malnic G, Giebisch G. Some electrical properties of distal tubular epithelium in the rat. Am J Physiol 1972; 223:797–808.
Seely JF, Boulpaep EL. Renal function studies on the isobaric autoperfused dog kidney. Am J Physiol 1971; 221:1075–1083.
Helman SI, Grantham JJ, Burg MB. Effect of vasopressin on electrical resistance of renal cortical collecting tubules. Am J Physiol 1971; 220:1825–1832.
Rau WS, Fromter E. Electrical properties of the medullary collecting ducts of the golden hamster kidney. II. The transepithelial resistance. Pflugers Arch 1974; 351:113–131.
Lewis SA, Eaton DC, Diamond JM. The mechanism of Na+ transport by rabbit urinary bladder. J Membr Biol 1976; 28:41–70.
Lavelle JP, Meyers SA, Ruiz WG et al. Urothelial pathophysiological changes in feline interstitial cystitis: a human model. Am J Physiol Renal Physiol 2000; 278:F540–F553.
Wang EC, Lee JM, Johnson JP et al. Hydrostatic pressure-regulated ion transport in bladder uroepithelium. Am J Physiol Renal Physiol 2003; 285:F651–F663.
Claude P, Goodenough DA. Fracture faces of zonulae occludentes from “tight” and “leaky” epithelia. J Cell Biol 1973; 58:390–400.
Gonzalez-Mariscal L, Namorado MC, Martin D et al. Tight junction proteins ZO-1, ZO-2, and occludin along isolated renal tubules. Kidney Int 2000; 57:2386–2402.
Balda MS, Whitney JA, Flores C et al. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 1996; 134:1031–1049.
Saitou M, Furuse M, Sasaki H et al. Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol Biol Cell 2000; 11:4131–4142.
Enck AH, Berger UV, Yu AS. Claudin-2 is selectively expressed in proximal nephron in mouse kidney. Am J Physiol Renal Physiol 2001; 281:F966–F974.
Reyes JL, Lamas M, Martin D et al. The renal segmental distribution of claudins changes with development. Kidney Int 2002; 62:476–487.
Kiuchi-Saishin Y, Gotoh S, Furuse M et al. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J Am Soc Nephrol 2002; 13:875–886.
Furuse M, Furuse K, Sasaki H et al. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol 2001; 153:263–272.
Amasheh S, Meiri N, Gitter AH et al. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci 2002; 115:4969–4976.
Yu AS, Enck AH, Lencer WI et al. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J Biol Chem 2003; 278:17350–17359.
Li WY, Huey CL, Yu AS. Expression of claudin-7 and-8 along the mouse nephron. Am J Physiol Renal Physiol 2004; 286:F1063–F1071.
Hulter HN, Ilnicki LP, Harbottle JA et al. Impaired renal H+ secretion and NH3 production in mineralocorticoid-deficient glucocorticoid-replete dogs. Am J Physiol 1977; 232:F136–F146.
Ethier JH, Kamel KS, Magner PO et al. The transtubular potassium concentration in patients with hypokalemia and hyperkalemia. Am J Kidney Dis 1990; 15:309–315.
Liddle GW. Aldosterone antagonists. AMA Arch Intern Med 1958; 102:998–1004.
Van Itallie C, Rahner C, Anderson JM. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J Clin Invest 2001; 107:1319–1327.
Colegio OR, Van Itallie CM, McCrea HJ et al. Claudins create charge-selective channels in the paracellular pathway between epithelial cells. Am J Physiol Cell Physiol 2002; 283:C142–C147.
Wilson FH, Disse-Nicodeme S, Choate KA et al. Human hypertension caused by mutations in WNK kinases. Science 2001; 293:1107–1112.
Yamauchi K, Rai T, Kobayashi K et al. Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins. Proc Natl Acad Sci USA 2004; 101:4690–4694.
Van Itallie CM, Fanning AS, Anderson JM. Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am J Physiol Renal Physiol 2003; 285:F1078–F1084.
Tisher CC. Morphology of the renal tubular paracellular route. In: Bradley SE, Purcell EF, eds. The Paracellular Route. New York: Josiah Macy, Jr. Foundation, 1982:183–201.
Roesinger B, Schiller A, Taugner R. A freeze-fracture study of tight junctions in the pars convoluta and pars recta of the renal proximal tubule. Cell Tissue Res 1978; 186:121–133.
Kuhn K, Reale E. Junctional complexes of the tubular cells in the human kidney as revealed with freeze-fracture. Cell Tissue Res 1975; 160:193–205.
Morita K, Sasaki H, Fujimoto K et al. Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J Cell Biol 1999; 145:579–588.
Cereijido M, González-Mariscal L, Contreras G. Tight junction barrier between higher organisms and environment. News Physiol Sci 1989; 4:72–75.
Alexandre MD, Chen YH. Claudin-7 overexpression decreases the paracellular conductance in kidney epithelial cells. Molecular Biology of the Cell 14[Supplement], 459a. 2003.
Wilcox ER, Burton QL, Naz S et al. Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29. Cell 2001; 104:165–172.
Ben Yosef T, Belyantseva IA, Saunders TL et al. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum Mol Genet 2003; 12:2049–2061.
Simon DB, Lu Y, Choate KA et al. Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption. Science 1999; 285:103–106.
Muller D, Kausalya PJ, Claverie-Martin F et al. A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting. Am J Hum Genet 2003; 73:1293–1301.
Gallardo JM, Hernandez JM, Contreras RG et al. Tight junctions are sensitive to peptides eliminated in the urine. J Membr Biol 2002; 188:33–42.
Herzlinger DA, Easton TG, Ojakian GK. The MDCK epithelial cell line expresses a cell surface antigen of the kidney distal tubule. J Cell Biol 1982; 93:269–277.
Harris RC. Response of rat inner medullary collecting duct to epidermal growth factor. Am J Physiol. 1989; 256:F1117–F1124.
Staehelin LA. Structure and function of intercellular junctions. Int Rev Cytol. 1974; 39:191–283.
Kachar B, Reese TS. Evidence for the lipidic nature of tight junction strands. Nature 1982; 296:464–466.
Pinto dS, Kachar B. On tight-junction structure. Cell 1982; 28:441–450.
Furuse M, Hirase T, Itoh M et al. Occludin: a novel integral membrane protein localizing at tight junctions. J Cell Biol 1993; 123:1777–1788.
Furuse M, Fujita K, Hiiragi T et al. Claudin-1 and-2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 1998; 141:1539–1550.
Furuse M, Sasaki H, Fujimoto K et al. A single gene product, claudin-1 or-2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 1998; 143:391–401.
Kubota K, Furuse M, Sasaki H et al. Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions. Curr Biol 1999; 9:1035–1038.
Turin L, Behe P, Plonsky I et al. Hydrophobic ion transfer between membranes of adjacent hepatocytes: a possible probe of tight junction structure. Proc Natl Acad Sci USA 1991; 88:9365–9369.
Grebenkamper K, Galla HJ. Translational diffusion measurements of a fluorescent phospholipid between MDCK-I cells support the lipid model of the tight junctions. Chem Phys Lipids 1994; 71:133–143.
Kan FW. Cytochemical evidence for the presence of phospholipids in epithelial tight junction strands. J Histochem Cytochem 1993; 41:649–656.
Dragsten PR, Handler JS, Blumenthal R. Fluorescent membrane probes and the mechanism of maintenance of cellular asymmetry in epithelia. Fed Proc 1982; 41:48–53.
Dragsten PR, Blumenthal R, Handler JS. Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane? Nature 1981; 294:718–722.
van Meer G, Simons K. The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J 1986; 5:1455–1464.
van Meer G, Gumbiner B, Simons K. The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next. Nature 1986; 322:639–641.
Calderon V, Lazaro A, Contreras RG et al. Tight junctions and the experimental modifications of lipid content. J Membr Biol 1998; 164:59–69.
Leung LW, Contreras RG, Flores-Maldonado C et al. Inhibitors of glycosphingolipid biosynthesis reduce transepithelial electrical resistance in MDCK I and FRT cells. Am J Physiol Cell Physiol 2003; 284:C1021–C1030.
Venkataraman K, Futerman AH. Ceramide as a second messenger: sticky solutions to sticky problems. Trends in Cell Biology 2000; 10:408–412.
Leroy A, De Bruyne GKP, Oomen LCJM et al. Alkylphospholipids reversibly open epithelial tight junctions. Anticancer Research 2003; 23:27–32.
Balda MS, Gonzalez-Mariscal L, Contreras RG et al. Assembly and sealing of tight junctions: possible participation of G-proteins, phospholipase C, protein kinase C and calmodulin. J Membr Biol 1991; 122:193–202.
Balda MS, Gonzalez-Mariscal L, Matter K et al. Assembly of the tight junction: the role of diacylglycerol. J Cell Biol 1993; 123:293–302.
Avila-Flores A, Rendon-Huerta E, Moreno J et al. Tight-junction protein zonula occludens 2 is a target of phosphorylation by protein kinase C. Biochem J 2001; 360:295–304.
Wu X, Hepner K, Castelino-Prabhu S et al. Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2. Proc Natl Acad Sci USA 2000; 97:4233–4238.
Wu Y, Dowbenko D, Spencer S et al. Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J Biol Chem 2000; 275:21477–21485.
Stankewich MC, Francis SA, Vu QU et al. Alterations in cell cholesterol content modulate Ca2+-induced tight junction assembly by MDCK cells. Lipids 1996; 31:817–828.
Francis SA, Kelly JM, McCormack J et al. Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance. Eur J Cell Biol 1999; 78:473–484.
Nusrat A, Parkos CA, Verkade P et al. Tight junctions are membrane microdomains. J Cell Sci 2000; 113 (Pt 10):1771–1781.
Grindstaff KK, Yeaman C, Anandasabapathy N et al. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 1998; 93:731–740.
Yeaman C, Grindstaff KK, Nelson WJ. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J Cell Sci 2004; 117:559–570.
Polishchuk R, Di Pentima A, Lippincott-Schwartz J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nat Cell Biol 2004; 6:297–307.
Sawai T, Drongowski RA, Lampman RW et al. The effect of phospholipids and fatty acids on tight-junction permeability and bacterial translocation. Pediatr Surg Int 2001; 17:269–274.
Schoner W. Endogenous cardiac glycosides, a new class of steroid hormones. Eur J Biochem 2002; 269:2440–2448.
Blaustein MP. Physiological effects of endogenous ouabain: control of intracellular Ca2+ stores and cell responsiveness. Am J Physiol 1993; 264:C1367–C1387.
Ruch SR, Nishio M, Wasserstrom JA. Effect of cardiac glycosides on action potential characteristics and contractility in cat ventricular myocytes: role of calcium overload. J Pharmacol Exp Ther 2003; 307:419–428.
Nunez-Duran H, Fernandez P. Evidence for an intracellular site of action in the heart for two hydrophobic cardiac steroids. Life Sci 2004; 74:1337–1344.
Ward SC, Hamilton BP, Hamlyn JM. Novel receptors for ouabain: studies in adrenocortical cells and membranes. Hypertension 2002; 39:536–542.
Hamlyn JM, Blaustein MP, Bova S et al. Identification and characterization of a ouabain-like compound from human plasma. Proc Natl Acad Sci USA 1991; 88:6259–6263.
Tymiak AA, Norman JA, Bolgar M et al. Physicochemical characterization of a ouabain isomer isolated from bovine hypothalamus. Proc Natl Acad Sci USA 1993; 90:8189–8193.
Gottlieb SS, Rogowski AC, Weinberg M et al. Elevated concentrations of endogenous ouabain in patients with congestive heart failure. Circulation 1992; 86:420–425.
Ruegg UT. Ouabain-a link in the genesis of high blood pressure? Experientia 1992; 48:1102–1106.
Ferrandi M, Manunta P, Balzan S et al. Ouabain-like factor quantification in mammalian tissues and plasma: comparison of two independent assays. Hypertension 1997; 30:886–896.
Laredo J, Shah JR, Hamilton BP, Hamlyn JM. Alpha-1 adrenergic receptors stimulate secretion of endogenous ouabain from human and bovine adrenocortical cells. In: Taniguchi K, Kayas S, eds. Na/K-ATPase and Related ATPases. Amsterdam: Elsvier Science, 2000:671–679.
Contreras RG, Shoshani L, Flores-Maldonado C et al. Relationship between Na(+),K(+)-ATPase and cell attachment. J Cell Sci. 1999; 112 (Pt 23):4223–4232.
Chen Y, Lu Q, Schneeberger EE et al. Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells. Mol Biol Cell 2000; 11:849–862.
Fujibe M, Chiba H, Kojima T et al. Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions. Exp Cell Res 2004; 295:36–47.
Macek R, Swisshelm K, Kubbies M. Expression and function of tight junction associated molecules in human breast tumor cells is not affected by the Ras-MEKl pathway. Cell Mol Biol (Noisy-le-grand) 2003; 49:1–11.
Rajasekaran AK, Rajasekaran SA. Role of Na-K-ATPase in the assembly of tight junctions. Am J Physiol Renal Physiol 2003; 285:F388–F396.
Rajasekaran SA, Hu J, Gopal J et al. Na,K-ATPase inhibition alters tight junction structure and permeability in human retinal pigment epithelial cells. Am J Physiol Cell Physiol 2003; 284:C1497–C1507.
Rajasekaran SA, Palmer LG, Moon SY et al. Na,K-ATPase activity is required for formation of tight junctions, desmosomes, and induction of polarity in epithelial cells. Mol Biol Cell 2001; 12:3717–3732.
Gonzalez-Mariscal L, Chavez DR, Cereijido M. Tight junction formation in cultured epithelial cells (MDCK). J Membr Biol 1985; 86:113–125.
Nusrat A, Giry M, Turner JR et al. Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia. Proc Natl Acad Sci USA 1995; 92:10629–10633.
Zhong C, Kinch MS, Burridge K. Rho-stimulated contractility contributes to the fibroblastic phenotype of Ras-transformed epithelial cells. Mol Biol Cell 1997; 8:2329–2344.
Takaishi K, Sasaki T, Kotani H et al. Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J Cell Biol 1997; 139:1047–1059.
Benais-Pont G, Punn A, Flores-Maldonado C et al. Identification of a tight junction-associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability. J Cell Biol 2003; 160:729–740.
Hecht G, Pestic L, Nikcevic G et al. Expression of the catalytic domain of myosin light chain kinase increases paracellular permeability. Am J Physiol 1996; 271:C1678–C1684.
Turner JR, Rill BK, Carlson SL et al. Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation. Am J Physiol 1997; 273:C1378–C1385.
Xie Z. Molecular mechanisms of Na/K-ATPase-mediated signal transduction. Ann N Y Acad Sci 2003; 986:497–503.
Xie Z, Cai T. Na+-K+-ATPase-mediated signal transduction: from protein interaction to cellular function. Mol Interv 2003; 3:157–168.
Blanco G, Mercer RW. Isozymes of the Na-K-ATPase: heterogeneity in structure, diversity in function. Am J Physiol 1998; 275:F633–F650.
Jorgensen PL. Aspects of gene structure and functional regulation of the isozymes of Na,K-ATPase. Cell Mol Biol (Noisy-le-grand) 2001; 47:231–238.
Contreras RG, Flores-Maldonado C, Lazaro A et al. Ouabain binding to Na+,K+-ATPase relaxes cell attachment and sends specific signal (NACos) to the nucleus. J Membr Biol 2004; 198:149–158.
Boulpaep EL, Seely JF. Electrophysiology of proximal and distal tubules in the autoperfused dog kidney. Am J Physiol 1971; 221:1084–1096.
Lutz MD, Cardinal J, Burg MB. Electrical resistance of renal proximal tubule perfused in vitro. Am J Physiol 1973; 225:729–734.
Abramow M, Orci L. On the “tightness” of the rabbit descending limb of the loop of Henle-physiological and morphological evidence. Int J Biochem 1980; 12:23–27.
Henin S, Cremaschi D, Schettino T et al. Electrical parameters in gallbladders of different species. Their contribution to the origin of the trans mural potential difference. J Membr Biol 1977; 34:73–91.
Okada Y, Irimajiri A, Inouye A. Electrical properties and active solute transport in rat small intestine. II. Conductive properties of transepithelial routes. J Membr Biol 1977; 31:221–232.
Munck BG, Schultz SG. Properties of the passive conductance pathway across in vitro rat jejunum. J Membr Biol 1974; 16:163–174.
Schultz SG, Frizzell RA, Nellans HN. Active sodium transport and the electrophysiology of rabbit colon. J Membr Biol 1977; 33:351–384.
Wills NK, Lewis SA, Eaton DC. Active and passive properties of rabbit descending colon: a microelectrode and nystatin study. J Membr Biol 1979; 45:81–108.
Peng S, Rahner C, Rizzolo LJ. Apical and basal regulation of the permeability of the retinal pigment epithelium. Invest Ophthalmol Vis Sci 2003; 44:808–817.
Liu F, Schaphorst KL, Verin AD et al. Hepatocyte growth factor enhances endothelial cell barrier function and cortical cytoskeletal rearrangement: potential role of glycogen synthase kinase-3beta. FASEB J 2002; 16:950–962.
Planchon S, Fiocchi C, Takafuji V et al. Transforming growth factor-betal preserves epithelial barrier function: identification of receptors, biochemical intermediates, and cytokine antagonists. J Cell Physiol 1999; 181:55–66.
Planchon SM, Martins CA, Guerrant RL et al. Regulation of intestinal epithelial barrier function by TGF-beta 1. Evidence for its role in abrogating the effect of a T cell cytokine. J Immunol 1994; 153:5730–5739.
Conyers G, Milks L, Conklyn M et al. A factor in serum lowers resistance and opens tight junctions of MDCK cells. Am J Physiol 1990; 259:C577–C585.
Jin M, Barron E, He S et al. Regulation of RPE intercellular junction integrity and function by hepatocyte growth factor. Invest Ophthalmol Vis Sci 2002; 43:2782–2790.
Abe T, Sugano E, Saigo Y et al. Interleukin-lbeta and barrier function of retinal pigment epithelial cells (ARPE-19): aberrant expression of junctional complex molecules. Invest Ophthalmol Vis Sci 2003; 4:4097–4104.
Hanada S, Harada M, Koga H et al. Tumor necrosis factor-alpha and interferon-gamma directly impair epithelial barrier function in cultured mouse cholangiocytes. Liver Int 2003; 23:3–11.
Mortell KH, Marmorstein AD, Cramer EB. Fetal bovine serum and other sera used in tissue culture increase epithelial permeability. In Vitro Cell Dev Biol 1993; 29A:235–238.
Harhaj NS, Barber AJ, Antonetti DA. Platelet-derived growth factor mediates tight junction redistribution and increases permeability in MDCK cells. J Cell Physiol 2002; 193:349–364.
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Shoshani, L., Flores-BenÍtez, D., Gonzalez-Mariscal, L., Contreras, R.G. (2006). Regulation of Tight Junctions’ Functional Integrity. In: Tight Junctions. Springer, Boston, MA. https://doi.org/10.1007/0-387-36673-3_11
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