Spatial expression of claudin family members in various organs of mice

Hwang,Inho; Yang,Hyun; Kang,Hong‑Seok; Ahn,Chang‑Hwan; Lee,Geun‑Shik; Hong,Eui‑Ju; An,Beum‑Soo; Jeung,Eui‑Bae

doi:10.3892/mmr.2014.2031

Spatial expression of claudin family members in various organs of mice

Authors:
- Inho Hwang
- Hyun Yang
- Hong‑Seok Kang
- Chang‑Hwan Ahn
- Geun‑Shik Lee
- Eui‑Ju Hong
- Beum‑Soo An
- Eui‑Bae Jeung
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Affiliations: Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju, Chungbuk 361‑763, Republic of Korea, Laboratory of Veterinary Physiology, College of Veterinary Medicine, Kangwon National University, Chuncheon, Gangwon 200‑701, Republic of Korea, Department of Biomaterials Science, College of National Resources and Life Science, Pusan National University, Miryang, Pusan 627‑706, Republic of Korea
Published online on: March 10, 2014 https://doi.org/10.3892/mmr.2014.2031
Pages: 1806-1812

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Abstract

Claudins (CLDNs) are tetraspan transmembrane proteins, which are components of tight junctions. The CLDN family is composed of 27 members that are responsible for paracellular transport and certain CLDNs form charge‑selective ion channels. CLDNs have two extracellular loops, and the charge of the first extracellular loop determines the ion selectivity of each CLDN. Although the expression and function of each CLDN have been previously investigated, the distribution of CLDNs in various target organs remains to be determined. In the present study, the tissue‑specific mRNA distribution of CLDNs (1‑5, 7‑8, 10a and b, 11‑12, 14‑17 and 19) in the duodenum, ileum, colon, kidney, liver and lung were defined. Among the tested CLDNs, CLDN1, 2, 12 and 16 were selected for further investiagtion. It was observed that CLDN1, CLDN2 and CLDN12 transcripts and proteins were particularly abundant in the investigated organs. Notably, immune‑reactive CLDN16 was detected in a tissue‑specific manner and shown in the renal tubules and portal vein. The tested CLDNs were localized to intercellular apical junctions in the epithelium of the intestine, renal tubule and bronchus. Based on this novel information, the presence of several types of CLDNs is of interest as CLDNs may promote or dampen the paracellular diffusion of specific ions.

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1	Wen H, Watry DD, Marcondes MC and Fox HS: Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol Cell Biol. 24:8408–8417. 2004. View Article : Google Scholar : PubMed/NCBI
2	Amasheh S, Meiri N, Gitter AH, et al: Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J Cell Sci. 115:4969–4976. 2002. View Article : Google Scholar : PubMed/NCBI
3	Hou J, Paul DL and Goodenough DA: Paracellin-1 and the modulation of ion selectivity of tight junctions. J Cell Sci. 118:5109–5118. 2005. View Article : Google Scholar : PubMed/NCBI
4	Colegio OR, Van Itallie C, Rahner C and Anderson JM: Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am J Physiol Cell Physiol. 284:C1346–C1354. 2003. View Article : Google Scholar
5	Alexandre MD, Jeansonne BG, Renegar RH, Tatum R and Chen YH: The first extracellular domain of claudin-7 affects paracellular Cl- permeability. Biochem Biophys Res Commun. 357:87–91. 2007. View Article : Google Scholar : PubMed/NCBI
6	Van Itallie CM, Rogan S, Yu A, Vidal LS, Holmes J and Anderson JM: Two splice variants of claudin-10 in the kidney create paracellular pores with different ion selectivities. Am J Physiol Renal Physiol. 291:F1288–F1299. 2006.PubMed/NCBI
7	Van Itallie CM and Anderson JM: Claudins and epithelial paracellular transport. Annu Rev Physiol. 68:403–429. 2006.PubMed/NCBI
8	Krug SM, Günzel D, Conrad MP, et al: Charge-selective claudin channels. Ann NY Acad Sci. 1257:20–28. 2012. View Article : Google Scholar : PubMed/NCBI
9	Schulzke JD, Günzel D, John LJ and Fromm M: Perspectives on tight junction research. Ann NY Acad Sci. 1257:1–19. 2012. View Article : Google Scholar : PubMed/NCBI
10	Günzel D, Stuiver M, Kausalya PJ, et al: Claudin-10 exists in six alternatively spliced isoforms that exhibit distinct localization and function. J Cell Sci. 122:1507–1517. 2009.PubMed/NCBI
11	Myal Y, Leygue E and Blanchard AA: Claudin 1 in breast tumorigenesis: revelation of a possible novel ‘claudin high’ subset of breast cancers. J Biomed Biotechnol. 2010:9568972010.PubMed/NCBI
12	Inai T, Kobayashi J and Shibata Y: Claudin-1 contributes to the epithelial barrier function in MDCK cells. Eur J Cell Biol. 78:849–855. 1999. View Article : Google Scholar : PubMed/NCBI
13	Weber CR, Nalle SC, Tretiakova M, Rubin DT and Turner JR: Claudin-1 and claudin-2 expression is elevated in inflammatory bowel disease and may contribute to early neoplastic transformation. Lab Invest. 88:1110–1120. 2008. View Article : Google Scholar : PubMed/NCBI
14	Van Itallie C, Rahner C and Anderson JM: Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J Clin Invest. 107:1319–1327. 2001.PubMed/NCBI
15	Hou J, Renigunta A, Yang J and Waldegger S: Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization. Proc Natl Acad Sci USA. 107:18010–18015. 2010. View Article : Google Scholar : PubMed/NCBI
16	Fujita H, Sugimoto K, Inatomi S, et al: Tight junction proteins claudin-2 and -12 are critical for vitamin D-dependent Ca²⁺ absorption between enterocytes. Mol Biol Cell. 19:1912–1921. 2008. View Article : Google Scholar : PubMed/NCBI
17	Hou J, Renigunta A, Konrad M, et al: Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex. J Clin Invest. 118:619–628. 2008.PubMed/NCBI
18	Chao YC, Pan SH, Yang SC, et al: Claudin-1 is a metastasis suppressor and correlates with clinical outcome in lung adenocarcinoma. Am J Respir Crit Care Med. 179:123–133. 2009. View Article : Google Scholar : PubMed/NCBI
19	Kitajiri SI, Furuse M, Morita K, et al: Expression patterns of claudins, tight junction adhesion molecules, in the inner ear. Hear Res. 187:25–34. 2004. View Article : Google Scholar : PubMed/NCBI
20	Zhu Y, Brännström M, Janson PO and Sundfeldt K: Differences in expression patterns of the tight junction proteins, claudin 1, 3, 4 and 5, in human ovarian surface epithelium as compared to epithelia in inclusion cysts and epithelial ovarian tumours. Int J Cancer. 118:1884–1891. 2006. View Article : Google Scholar
21	Furuse M, Furuse K, Sasaki H and Tsukita S: Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol. 153:263–272. 2001. View Article : Google Scholar : PubMed/NCBI
22	Reyes JL, Lamas M, Martin D, et al: The renal segmental distribution of claudins changes with development. Kidney Int. 62:476–487. 2002. View Article : Google Scholar : PubMed/NCBI
23	Rahner C, Mitic LL and Anderson JM: Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. Gastroenterology. 120:411–422. 2001. View Article : Google Scholar : PubMed/NCBI
24	Wolburg H, Wolburg-Buchholz K, Liebner S and Engelhardt B: Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse. Neurosci Lett. 307:77–80. 2001. View Article : Google Scholar : PubMed/NCBI
25	Muto S, Hata M, Taniguchi J, et al: Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules. Proc Natl Acad Sci USA. 107:8011–8016. 2010. View Article : Google Scholar : PubMed/NCBI
26	Hawkins BT and Davis TP: The blood-brain barrier/neurovascular unit in health and disease. Pharmacol Rev. 57:173–185. 2005. View Article : Google Scholar : PubMed/NCBI
27	Belanger M, Asashima T, Ohtsuki S, Yamaguchi H, Ito S and Terasaki T: Hyperammonemia induces transport of taurine and creatine and suppresses claudin-12 gene expression in brain capillary endothelial cells in vitro. Neurochem Int. 50:95–101. 2007. View Article : Google Scholar : PubMed/NCBI
28	Fujita H, Chiba H, Yokozaki H, et al: Differential expression and subcellular localization of claudin-7, -8, -12, -13 and -15 along the mouse intestine. J Histochem Cytochem. 54:933–944. 2006. View Article : Google Scholar : PubMed/NCBI
29	Brandner JM, McIntyre M, Kief S, Wladykowski E and Moll I: Expression and localization of tight junction-associated proteins in human hair follicles. Arch Dermatol Res. 295:211–221. 2003. View Article : Google Scholar : PubMed/NCBI
30	Simon DB, Lu Y, Choate KA, et al: Paracellin-1, a renal tight junction protein required for paracellular Mg²⁺ resorption. Science. 285:103–106. 1999. View Article : Google Scholar : PubMed/NCBI
31	Konrad M, Schaller A, Seelow D, et al: Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am J Hum Genet. 79:949–957. 2006.PubMed/NCBI