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Physiology 19: 331-338, 2004; doi:10.1152/physiol.00027.2004
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Physiology, Vol. 19, No. 6, 331-338, December 2004
© 2004 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

The Molecular Physiology of Tight Junction Pores

Christina M. Van Itallie1 and James Melvin Anderson2

1 Departments of Medicine and
2 Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599

jandersn{at}med.unc.edu


   Abstract
 
Tight junctions form selective barriers that regulate paracellular transport across epithelia. A large family of tetraspanning cell-cell adhesion proteins called claudins create the barrier and regulate electrical resistance, size, and ionic charge selectivity. Study of inherited human claudin diseases and the outcome of the genetic manupulation of claudins in mice, Drosophila, and Caenorhabditis elegans are furthering our understanding of paracellular physiology.


   Introduction
Top
 Introduction
Characteristics of Paracellular...
 Physiological Regulation
 The Blind Men and...
 Conclusions
 References
 
The tight junction (TJ) forms a selective barrier in the paracellular space between epithelial cells, limiting transepithelial movement of ions, solutes, and water. Barrier properties vary among epithelia and are influenced by both physiological and more dramatically by pathophysiological stimuli. Although their basic physiological properties were well described by the early 1970s (9, 16), insight into the molecular basis of paracellular transport has only come in the past few years. Our growing understanding of the barrier and its constituents has helped clarify its contribution to normal and pathological transport and has raised speculation that it could be a target for enhancing transepithelial drug delivery. In this brief review, we focus on the evidence that claudins are responsible for the selective properties of TJs (46, 60) and consider how the barrier is physiologically regulated. Excellent reviews are available describing the pathophysiology of the TJ (44), its molecular components (15), and its regulation (5, 43, 61, 71).


   Characteristics of Paracellular Transport
Top
 Introduction
 Characteristics of Paracellular...
Physiological Regulation
 The Blind Men and...
 Conclusions
 References
 
Paracellular transport through the TJ differs in several key ways from transcellular transport across cell membranes. First, it is exclusively passive, driven by electroosmotic gradients produced either by transcellular transport or by extrinsically produced gradients such as ingestion of a meal. Second, it does not rectify, i.e., it shows identical selectivity and conductance in both the mucosal and serosal directions (46). Third, although transcellular transport is clearly highly regulated, there remains controversy about the potential for acute physiological regulation of paracellular transport. Variable properties of paracellular transport described among different epithelia include electrical conductance (~105-fold range), charge selectivity (e.g., PNa/PCl ~ 30-fold) (66), noncharged solute permeability, and size discrimination (46). By complementing trans-cellular transport, the selective back-leak through the junction contributes to the overall physiological characteristics of each epithelium. In general, so-called "leaky" TJs are found in epithelia that move large volumes of isosmotic fluids, like the intestine. "Tight" TJs are found where high electroosmotic gradients are required, as in the distal tubules and collecting ducts of the kidney (46).

The TJ behaves as a barrier perforated by aqueous pores. Compared with transmembrane channels, paracellular pores are larger and thus less discriminating of size and charge (16, 55, 71). Early studies showed that the permeability for hydrophilic nonelectrolytes was inversely related to their size, up to a cutoff characteristic for each tissue (~7- to 15-Å radius) (46), suggesting passage through restricted aqueous spaces with defined pore sizes. The permeability differences for alkali-metal cations is only a few fold, in contrast to the thousandfold differences for cation channels of the plasma membrane. This low discrimination for similarly charged but differently sized cations is consistent with a relatively large pore size (46). That said, TJs pores are by no means free solution pathways and share with transmembrane ion channels an influence of ion concentration on permeability and even competition between different species of transported molecules (55). There is presently no evidence that TJ pores are gated; thus the occasionally used term "channel" seems inappropriate.

The barrier is formed by continuous rows of transmembrane proteins from adjacent cells that contact in the intercellular space. Different numbers of rows and different levels of cross-bridging among rows are seen in different epithelia (13), although the physiological implications of these differing organizations remain unknown. It was once commonly accepted that the number of strands correlated with electrical resistance across the junction (13). Although this simple circuit concept may contribute to resistance, it now appears that the protein composition of the strands is also very important.

A fundamental breakthrough in understanding the barrier structure came in 1998 when the first claudins, isolated by S. Tsukita’s group in Japan, were shown to reconstitute strands when expressed in claudin-null fibroblasts (18) and to be cell-to-cell adhesion molecules (22). Claudins are tetraspan proteins ranging from 20 to 25 kDa and are recognized by the so-called WGLWCC motif in their first extracellular loop (FIGURES 1Go AND 2Go). They are found across a wide range of metazoa. Mammals have at least 24 (57). The puffer fish Fugu presently holds the record, with 56 claudin genes (32). In Drosophila, six claudin sequences are reported (6, 58, 70). Two of these, Megatrachea (Mega) (6) and Sinuous (Sinu) (70), are located at the barrier-forming septate junctions. Tsukita and colleagues (3) have identified five claudin-like proteins in C. elegans and have shown them to be necessary for controlling paracellular permeability across the gut. Some claudins, like claudin-1 in mammals, are rather ubiquitously expressed; others are highly restricted to specific cell types (23, 52) or certain periods of development (63). Another transmembrane strand protein, called occludin (21), was discovered before claudins, but its function remains obscure. Occludin-null mice are viable and have normal-appearing TJs but express a complex and difficult-to-rationalize phenotype (49).



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  		FIGURE 1. Membrane topology model for claudins
Residue positions in the 2 extracellular loops and cytoplasmic tail are indicated along with the location of conserved signature residues; see FIGURE 2Go. Charged residues can influence paracellular charge selectivity. Although untested, it seems likely that the invariant pair of cysteines forms a disulfide bond in the oxidizing extracellular milieu. Where tested, the COOH-terminal PDZ-binding motifs bind ZO-1 and MUPP1. This topology and the signature residues are shared by members of the PMP-22/EMP/MP20/claudin family, although not all have PDZ motifs.

 


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  		FIGURE 2. Sequence alignment and phylogenetic tree of members of the claudin family
A: sequence alignment of the first extracellular loop of members of the human PMP22/EMP22/MP20/claudin family. EMP22, epithelia membrane protein 22; PMP22, peripheral myelin protein; MP20, lens intrinsic membrane protein; {gamma}5-subunit, a subunit of the neuronal voltage-gated calcium channel; CLP24, claudin-like protein-24. The NH2-terminal-most sequences are shown, and the remaining numbers of residues are indicated in parentheses. Members contain the so-called WGLWCC motif (gray shading), except the PMPs, which also have N-glycosylation sites. B: phylogenetic tree of full-length proteins shown in A. Claudin-16 is more similar to the EMP branch than to claudin-1 and -2. CLP24, a demonstrated component of tight junctions (TJs), is more distant from claudin-1 than the {gamma}-subunits of voltage-gated calcium channels. Possible functional similarities within this large family are largely unexplored. Distances were calculated by using DNASTAR-MegAlign rooted algorithm.

 
Several lines of evidence point to claudins as the basis for the selective size, charge, and conductance properties of the paracellular pathway. One approach used by several groups to study the effects of claudins on conductance has been to express individual claudins in monolayers of Madin-Darby canine kidney (MDCK) epithelial cells. A major limitation of this approach is that cultured epithelial cells already express a background of multiple claudins. Thus one cannot define a specific unit of selectivity or conductance for an individual claudin, as for a transmembrane channel, but can only document changes relative to the background. Despite this limitation, a clear pattern of results has emerged. Expression of claudin-1 (26, 36), -4 (65), -8 (28, 72), -14 (7), and -15 (14) dramatically increases resistance when expressed in low-resistance MDCK type II cells. In contrast, expression of claudin-2 in high-resistance MDCK type I monolayers decreased resistance (1, 19). One can speculate that each claudin has a unique conductance and that their ensemble in each epithelium determines the overall conductance.

In the case of claudin-4 (65), -8 (72), and -14 (7), reduced conductance results from selective discrimination against cations. Low-conductance characteristics of claudin-4 and -8 are consistent with their expression in the distal renal tubule segments and those of claudin-14 with its expression in the inner ear, in both cases maintaining high cation gradients by limiting paracellular electrodiffusion. Our own group (14) demonstrated that replacing some, but not other, negative residues with positive ones in the first extracellular loop of claudin-15 converts it from a cation-selective to an anion-selective pore (FIGURE 1Go). Collectivity, these results suggest that fixed charges on the extracellular loops of claudins line the aqueous pores and electrostatically influence passage of soluble ions (FIGURE 3Go). This idea is further supported by the phenotype resulting from human mutations in claudin-16 (paracellin-1). Expression of claudin-16 is highly restricted to the junction of the thick ascending loop of Henle, coinciding with a region where paracellular cation reabsorption occurs down an electrical gradient. Homozygous individuals show urinary Mg2+ and Ca2+ wasting due to a defect in paracellular cation reabsorption in this segment (52). Direct evidence that claudin-16 forms cation pores is presently lacking. However, coincidently it has many more negative residues in the first loop than other claudins. Models of how pores might be organized within strands are well reviewed by Yu (71) and are depicted in FIGURE 3Go.



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  		FIGURE 3. Speculative model of tight junction pores
Tight junctions form as continuous contacts at the apical end of adjacent epithelial cells. Claudins form continuous rows and show homotypic adhesion, and specific extracellular charged residues have an electrostatic influence on paracellular ion movements. These results suggest a model in which claudins seal and provide selective pores in the paracellular pathway. Claudin tails bind PDZ domains of scaffolding proteins MUPP1 and ZO-1. The later binds filamentous actin and myosin, possibly explaining physiological regulation of the barrier by the cytoskeleton.

 
The molecular basis for size selectivity of TJs is obscure; however, recent in vivo studies now provide the first suggestion that claudins also influence this property (41). Brain endothelia express at least claudins-5 and -12 and effectively exclude even small solutes from entering brain tissue. To test the role of claudins in the blood-brain barrier, Nitta et al. (41) created claudin-5-null mice (Table 1Go). These were born with normal-appearing TJs but died a few hours after birth. When the vascular space was perfused with a panel of size markers, vessels from wild-type animals retained markers ranging from albumin (68 kDa) down to the Hoechst dye 33258 (562 Da). Intriguingly, the endothelia of claudin-5-null mice become leaky to the 562-Da marker yet still restricted the next largest (1,862 Da). A role in size selectivity may also be supported by recent work of McLaughlin et al. (37), who were investigating the mechanism by which the mycotoxin ochratoxin A alters the intestinal barrier. Application of toxin to a cultured intestinal cell line induced selective removal of claudins-3 and -4 but not -1. This coincided with an increased permeability for small but not larger fluorescently labeled dextrans. Although these studies reveal a connection between claudins and size discrimination, the molecular mechanism remains unclear and it remains to be determined whether different claudins form pores with different dimensions.


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  		Table 1. Mouse claudin knockouts and transgenics
 
The name "tight junction" was evoked by early electron-microscopic images that incorrectly suggested that the junction was static and impenetrable. Yet TJs in the body must be quite dynamic because they permit transmigration of leukocytes (11) and they slide with respect to each other, all without a break in the barrier. Their dynamic nature has now been observed in a provocative study from the Tsukita laboratory (50). Using green fluorescent protein (GFP)-labeled claudins expressed in a fibroblast cell line, they observed strands breaking and annealing in both an end-to-end and an end-to-side fashion over an interval of minutes. Because of the COOH-terminal GFP tag, these transfected claudins lacked the ability to bind the normal tight junction scaffolding proteins, e.g., ZO-1 and MUPP1. It will be important to repeat these studies in epithelial cells capable of normal protein interactions and to determine whether strand dynamics are physiologically regulated to influence permeability or leukocyte movements.

If TJs contain pores of different sizes, this may help resolve the curious dissociation between ion and solute permeability. Numerous studies have documented experimental manipulations that decrease electrical conductance while simultaneously increasing the paracellular flux of noncharged solutes like mannitol (35). This behavior could be explained if the barrier contained at least two populations of pores. The first might be small pores carrying Na+, Cl–, and the other small electrolytes that predominate during the short, millisecond current pulses used to measure transepithelial electrical resistance. A second population might be larger and permit transport of larger, noncharged molecules, like mannitol. Flux measurements are made over minutes to hours. If the larger pores were few in number, they would contribute little conductance during instantaneous electrical measurements. Opposing changes in the two populations could explain the apparently paradoxical dissociation of transepithelial electrical resistance and flux occasionally observed. Conceivably, the large pores could represent infrequent breaks in the strands, as described above. Further insight will require molecular knowledge of the pores.


   Physiological Regulation
Top
 Introduction
 Characteristics of Paracellular...
 Physiological Regulation
The Blind Men and...
 Conclusions
 References
 
There is substantial evidence that TJ conductance is affected by pathological stimuli, including among others bacterial toxins (51), cytotoxic compounds (46), cytokines (44), and hypoxia (69). Conductance can also be altered by altering second-messenger systems and signaling pathways (4), also supporting the possibility of physiological regulation. However, there remains scant compelling evidence for minute-to-minute regulation of TJs under normal physiological conditions. Conceivably, evolution has left the more subtle mechanisms of transcellular transport to deal with acute regulation.

The best-studied and most plausible example of acute physiological regulation is the intestinal TJs’ response to luminal glucose. The transcellular route for glucose uptake is predominately through a system of saturable Na+-glucose cotransporters (SGLT1). The observation that transport far exceeds the capacity of the SGLT1 system first led to speculation about an inducible diffusion-driven paracellular route that responds to SGLT1 activity (33, 45). Early studies in hamster intestine demonstrated a drop in paracellular impedance in a dose-dependent manner upon activation of transcellular glucose transport (34). This correlated with condensation of the thick band of perijunctional actin and myosin, suggesting that contraction of the actin cytoskeleton leads to subtle opening of the paracellular space. This basic observation has been confirmed in humans and rodents (45) in isolated tissues and in cell lines (64). Myosin light-chain kinase (MLCK) has emerged as a plausible upstream effector of the conductance changes. Glucose transport stimulates perijunctional cytoskeletal contraction by phosphorylation of myosin-regulatory light chain (64), and inhibition of MLCK blocks the effects of glucose on conductance (8). This pathway may also be controlled by other apical Na+-coupled transport systems, such as amino acid transporters (45). Conceivably, MLCK and the actin cytoskeleton form a final common pathway for other signaling pathways. Since claudins bind ZO-1, which in turn binds actin filaments (17), cytoskeletal contraction could feasibly modulate claudin-claudin interactions (FIGURE 3Go).


   The Blind Men and the Elephant: The PMP-22/EMP/MP20/Claudin Family
Top
 Introduction
 Characteristics of Paracellular...
 Physiological Regulation
 The Blind Men and...
Conclusions
 References
 
As the poet John Godfrey Saxe (1816–1887) observed, the six blind men of Indostan each had his own partly correct perception of the elephant. Each was limited to that facet of the elephant that he investigated. Recent reports suggest that we too may lack full vision of the functional complexity of claudins and their possible functional connection to a larger protein family.

Database searching reveals a large number of proteins with structural similarities to claudins but whose functional similarities remain largely unexplored. Making sense of the literature is a challenge because of a lack of consistent nomenclature. Before their naming in 1998 (18), three of the orthodox claudins had already been cloned and given other names and were characterized by nonbarrier functions. This conflict is now resolved, and most authors designate these as TMVCF (cln-5) (40), RVP.1 (cln-3) (39), and SEMP1 (cln-1) (54). Claudin-22 appeared in the literature, yet "claudin-21" cannot be found in the NCBI database or on PubMed. Adding to the confusion, there are many claudin-like sequences grouped under the protein family designation "pfam00822" (NCBI nomenclature; http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=1378), some with several different names and historically characterized by nonbarrier functions. They are all 20–25 kDa and share the tetraspan topology and the WGLWCC signature residues in the first extracellular loops (FIGURES 1Go AND 2Go). All claudins and most other pfam0082 members end in a PDZ-binding motif (FIGURE 1Go). TJ claudins bind PDZ domains in the cytoplasmic scaffolding proteins ZO-1 (27) and MUPP1 (25, 28) (FIGURE 3Go).

The proteins most homologous to claudins are eye lens-specific membrane proteins (MP20, also referred to as lim2 and MP17, 18, or 19) (53); epithelial membrane proteins (EMP-1, -2, and -3) (29); and peripheral myelin protein 22 (PMP22) (42) (FIGURE 2BGo). PMP22 is highly expressed in Schwann cells and is required for myelinization. Two forms of human hereditary sensorineuronal peripheral polyneuropathies result from either mutations or increased dosage of wild-type PMP22 (10) (Table 2Go). Studied for years for its role in apoptosis and cell proliferation, PMP22 was recently shown to be a component of TJs in liver, intestine (42), and the blood-brain barrier (48). The peripheral nerve pathology caused by mutations in PMP22 may be the central nervous system counterpart of myelin-sealing defects caused by genetic deletion of claudin-11 from oligodendrocytes (23). The subcellular location of EMP-1, -2, and -3 has not been reported, and the focus of research has been on their role in apoptosis (56). They were recently described as binding partners for the purineurgic P2X7 ATP-gated family of ion channels and as being required for ATP to induce apoptosis in a culture cell model (68). MP20 is one of the most prevalent proteins of lens fiber cells; human mutations in MP20 cause cataracts (53). The location of MP20 in the eye corresponds to the location of the paracellular diffusion barrier for dyes (24). CLP24 was recently cloned as a transcript upregulated by hypoxia. Although only 8% identical to claudin-1, when expressed in cultured MDCK cells it increases paracellular flux for tracer molecules and localizes to the apical junction complex (30). Interestingly, it colocalizes at the adherens junction, not the TJ.


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  		Table 2. Hereditary human diseases of tight junctions
 
What are these clues trying to tell us? Are the PMPs, EMPs, and MP20 all barrier-forming claudins? Taking the opposite perspective, should we look for additional functions in the orthodox claudins, like involvement in apoptosis and proliferation? Even several orthodox claudins are not restricted to tight junctions; claudin-7, for example, is on the basolateral surface of cells in the kidney tubule epithelium (31). Many other claudins have large pools of protein on the lateral surface distinct from the barrier-forming TJ strands. The role and organization of extrajunctional claudin remains unclear.

Even more enigmatic is inclusion in the pfam0082 family of the {gamma}-subunits of voltage-dependent calcium channels. They are larger but share topology and signature residues (FIGURE 2Go). {gamma}-Subunits bind pore-forming {alpha}-subunits and are required for proper plasma membrane delivery of the {alpha}-subunit (59). Pairing of EMPs with ATP-gated ion channels and {gamma}-subunits with pore-forming subunits of the calcium channel may represent a functional theme to look for in other claudins.

Finally, regulation of both differentiation and cell growth are often dependent on the presence of signals from adjacent cells or matrix. Although numerous adhesion molecules have been implicated in regulation of this process, only recently have there been suggestions that cell-cell interactions at the TJ might figure in these control mechanisms. There are now numerous reports of changes in claudin expression in various epithelial cancers, although both increased (47) and decreased (2) expression levels of specific claudins have been documented. More directly, when a pancreatic cancer cell line was transfected to express claudin-4, its metastatic potential was reduced (38). Although these results are consistent with the idea that claudin interactions may play a role in normal growth regulation, relevant data are still scarce and any mechanistic relationship remains to be demonstrated.


   Conclusions
Top
 Introduction
 Characteristics of Paracellular...
 Physiological Regulation
 The Blind Men and...
 Conclusions
References
 
Morphological and functional data suggest that claudins are the key components of the TJ pore. Furthermore, the biochemical diversity within this family underlies differences in TJ structure and function in specific tissues and cell types. Suggestive data exist to implicate these molecules in acute physiological regulation of paracellular permeability and also in influencing growth and differentiation, as least in some pathological states. Finally, related family members may provide clues as to the roles of claudin-like proteins outside the TJs.

Major questions remain to be answered. One of the most pressing is that of the molecular structure of the presumed claudin complex, that is, the paracellular pore. Although claudins are clearly important constituents of the complex, the contribution of other proteins, namely occludin, is unclear. The mechanism by which claudins interact across the paracellular space is also undefined. Finally, the issue of physiological regulation remains to be further explored, with an eye to potential therapeutic manipulation of the TJ structure for delivery of pharmacological agents or in control of metastatic behavior.


   Acknowledgments
 
We thank the State of North Carolina, the Broad Medical Research Program of the Eli and Edythe L. Broad Foundation, and the National Institute of Diabetes and Digestive and Kidney Diseases (grant nos. DK-61397 and DK-45134) for support of our research.


   References
Top
 Introduction
 Characteristics of Paracellular...
 Physiological Regulation
 The Blind Men and...
 Conclusions
 References
 

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