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Journal of veterinary science2016; 17(4); 445-451; doi: 10.4142/jvs.2016.17.4.445

Claudin-1, -2, -4, and -5: comparison of expression levels and distribution in equine tissues.

Abstract: Claudins, which are known as transmembrane proteins play an essential role in tight junctions (TJs) to form physical barriers and regulate paracellular transportation. To understand equine diseases, it is helpful to measure the tissue-specific expression of TJs in horses. Major equine diseases such as colic and West Nile cause damage to TJs. In this study, the expression level and distribution of claudin-1, -2, -4, and -5 in eight tissues were assessed by Western blotting and immunohistochemistry methods. Claudin-1 was primarily identified in the lung, duodenum, and uterus, claudin-2 was evenly observed in equine tissues, claudin-4 was abundantly detected in the liver, kidney and uterus, and claudin-5 was strongly expressed in the lung, duodenum, ovary, and uterus, as determined by Western blotting method. The localization of equine claudins was observed by immunohistochemistry methods. These findings provide knowledge regarding the expression patterns and localization of equine claudins, as well as valuable information to understand tight junction-related diseases according to tissue specificity and function of claudins in horses.
Publication Date: 2016-04-01 PubMed ID: 27030194PubMed Central: PMC5204021DOI: 10.4142/jvs.2016.17.4.445Google Scholar: Lookup
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  • Journal Article

Summary

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The research focuses on understanding the role and distribution of certain proteins called claudins in the tissues of horses. These proteins play a significant role in maintaining the health and functioning of cells and have implications in understanding diseases such as colic and West Nile.

The Role of Claudins

  • Claudins are transmembrane proteins that form an essential component of tight junctions (TJs), which are part of the cells that form various tissues and organs in the body.
  • These proteins not only help form physical barriers but also regulate the transfer of substances between cells, a process known as paracellular transportation.
  • Knowing the distribution and levels of these proteins in horse tissues could provide valuable insights into how diseases that affect TJs, such as colic and West Nile, occur and progress.

The Study and its Methods

  • The study focused on the expression and distribution of four types of claudins – claudin-1, claudin-2, claudin-4, and claudin-5 – in eight different types of tissues.
  • The levels and distribution of these proteins were assessed using two methods: Western blotting, which is a technique used to detect specific proteins in a sample, and immunohistochemistry, which involves staining proteins to visualise their location in tissues.

Findings of the Study

  • The study found that the distribution of these claudins varied across different tissues. Claudin-1 was primarily identified in the lung, duodenum, and uterus, claudin-2 was evenly observed in equine tissues, claudin-4 in the liver, kidney and uterus, and claudin-5 was most expressed in the lung, duodenum, ovary, and uterus.
  • The localization of these claudins in horse tissues was also visualized using immunohistochemistry.

Importance of Findings

  • The findings provide new knowledge on where these claudins are most expressed in horse tissues, information that was previously unknown.
  • This information is critical to understanding the function of these proteins and how they may be implicated in TJ-related diseases in horses.

Cite This Article

APA
Lee B, Kang HY, Lee DO, Ahn C, Jeung EB. (2016). Claudin-1, -2, -4, and -5: comparison of expression levels and distribution in equine tissues. J Vet Sci, 17(4), 445-451. https://doi.org/10.4142/jvs.2016.17.4.445

Publication

ISSN: 1976-555X
NlmUniqueID: 100964185
Country: Korea (South)
Language: English
Volume: 17
Issue: 4
Pages: 445-451

Researcher Affiliations

Lee, Bonn
  • Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju 28644, Korea.
Kang, Hee Young
  • Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju 28644, Korea.
Lee, Dong Oh
  • Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju 28644, Korea.
Ahn, Changhwan
  • Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju 28644, Korea.
Jeung, Eui-Bae
  • Laboratory of Veterinary Biochemistry and Molecular Biology, College of Veterinary Medicine, Chungbuk National University, Cheongju 28644, Korea.

MeSH Terms

  • Animals
  • Blotting, Western / veterinary
  • Claudins / genetics
  • Claudins / metabolism
  • Female
  • Gene Expression Regulation
  • Horses / genetics
  • Horses / metabolism
  • Immunohistochemistry / veterinary
  • Male
  • Tissue Distribution

Conflict of Interest Statement

There is no conflict of interest.

References

This article includes 28 references
  1. Amasheh S, Meiri N, Gitter AH, Schöneberg T, Mankertz J, Schulzke JD, Fromm M. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells.. J Cell Sci 2002 Dec 15;115(Pt 24):4969-76.
    pubmed: 12432083doi: 10.1242/jcs.00165google scholar: lookup
  2. Boyer JL. Bile formation and secretion.. Compr Physiol 2013 Jul;3(3):1035-78.
    pmc: PMC4091928pubmed: 23897680doi: 10.1002/cphy.c120027google scholar: lookup
  3. D'Souza T, Sherman-Baust CA, Poosala S, Mullin JM, Morin PJ. Age-related changes of claudin expression in mouse liver, kidney, and pancreas.. J Gerontol A Biol Sci Med Sci 2009 Nov;64(11):1146-53.
    pmc: PMC2759572pubmed: 19692671doi: 10.1093/gerona/glp118google scholar: lookup
  4. Delfín DA, Xu Y, Schill KE, Mays TA, Canan BD, Zang KE, Barnum JA, Janssen PM, Rafael-Fortney JA. Sustaining cardiac claudin-5 levels prevents functional hallmarks of cardiomyopathy in a muscular dystrophy mouse model.. Mol Ther 2012 Jul;20(7):1378-83.
    pmc: PMC3392970pubmed: 22547149doi: 10.1038/mt.2012.81google scholar: lookup
  5. Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin.. J Cell Biol 1998 Jun 29;141(7):1539-50.
    pmc: PMC2132999pubmed: 9647647doi: 10.1083/jcb.141.7.1539google scholar: lookup
  6. Furuse M, Furuse K, Sasaki H, 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 2001 Apr 16;153(2):263-72.
    pmc: PMC2169456pubmed: 11309408doi: 10.1083/jcb.153.2.263google scholar: lookup
  7. Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, Sugitani Y, Noda T, Kubo A, Tsukita S. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice.. J Cell Biol 2002 Mar 18;156(6):1099-111.
    pmc: PMC2173463pubmed: 11889141doi: 10.1083/jcb.200110122google scholar: lookup
  8. Furuse M, Hirase T, Itoh M, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S. Occludin: a novel integral membrane protein localizing at tight junctions.. J Cell Biol 1993 Dec;123(6 Pt 2):1777-88.
    pmc: PMC2290891pubmed: 8276896doi: 10.1083/jcb.123.6.1777google scholar: lookup
  9. Furuse M, Itoh M, Hirase T, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions.. J Cell Biol 1994 Dec;127(6 Pt 1):1617-26.
    pmc: PMC2120300pubmed: 7798316doi: 10.1083/jcb.127.6.1617google scholar: lookup
  10. Furuse M, Sasaki H, Tsukita S. Manner of interaction of heterogeneous claudin species within and between tight junction strands.. J Cell Biol 1999 Nov 15;147(4):891-903.
    pmc: PMC2156154pubmed: 10562289doi: 10.1083/jcb.147.4.891google scholar: lookup
  11. Gobe GC, Johnson DW. Distal tubular epithelial cells of the kidney: Potential support for proximal tubular cell survival after renal injury.. Int J Biochem Cell Biol 2007;39(9):1551-61.
    pubmed: 17590379doi: 10.1016/j.biocel.2007.04.025google scholar: lookup
  12. Grosche A, Morton AJ, Graham AS, Sanchez LC, Blikslager AT, Polyak MM, Freeman DE. Ultrastructural changes in the equine colonic mucosa after ischaemia and reperfusion.. Equine Vet J Suppl 2011 Aug;(39):8-15.
  13. GROSSMAN ML. The glands of Brunner.. Physiol Rev 1958 Oct;38(4):675-90.
    pubmed: 13590933doi: 10.1152/physrev.1958.38.4.675google scholar: lookup
  14. Günzel D, Yu AS. Claudins and the modulation of tight junction permeability.. Physiol Rev 2013 Apr;93(2):525-69.
    pmc: PMC3768107pubmed: 23589827doi: 10.1152/physrev.00019.2012google scholar: lookup
  15. Hou J, Renigunta A, Yang J, Waldegger S. Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization.. Proc Natl Acad Sci U S A 2010 Oct 19;107(42):18010-5.
    pmc: PMC2964195pubmed: 20921420doi: 10.1073/pnas.1009399107google scholar: lookup
  16. Hwang I, Yang H, Kang HS, Ahn CH, Lee GS, Hong EJ, An BS, Jeung EB. Spatial expression of claudin family members in various organs of mice.. Mol Med Rep 2014 May;9(5):1806-12.
    pubmed: 24626855doi: 10.3892/mmr.2014.2031google scholar: lookup
  17. Kojima T, Yamamoto T, Murata M, Chiba H, Kokai Y, Sawada N. Regulation of the blood-biliary barrier: interaction between gap and tight junctions in hepatocytes.. Med Electron Microsc 2003 Sep;36(3):157-64.
    pubmed: 14505059doi: 10.1007/s00795-003-0220-5google scholar: lookup
  18. Krug SM, Schulzke JD, Fromm M. Tight junction, selective permeability, and related diseases.. Semin Cell Dev Biol 2014 Dec;36:166-76.
    pubmed: 25220018doi: 10.1016/j.semcdb.2014.09.002google scholar: lookup
  19. Medigeshi GR, Hirsch AJ, Brien JD, Uhrlaub JL, Mason PW, Wiley C, Nikolich-Zugich J, Nelson JA. West nile virus capsid degradation of claudin proteins disrupts epithelial barrier function.. J Virol 2009 Jun;83(12):6125-34.
    pmc: PMC2687390pubmed: 19369347doi: 10.1128/JVI.02617-08google scholar: lookup
  20. Mitic LL, Van Itallie CM, Anderson JM. Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins.. Am J Physiol Gastrointest Liver Physiol 2000 Aug;279(2):G250-4.
    pubmed: 10915631doi: 10.1152/ajpgi.2000.279.2.G250google scholar: lookup
  21. Morita K, Sasaki H, Furuse M, Tsukita S. Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells.. J Cell Biol 1999 Oct 4;147(1):185-94.
    pmc: PMC2164984pubmed: 10508865doi: 10.1083/jcb.147.1.185google scholar: lookup
  22. Muto S, Hata M, Taniguchi J, Tsuruoka S, Moriwaki K, Saitou M, Furuse K, Sasaki H, Fujimura A, Imai M, Kusano E, Tsukita S, Furuse M. Claudin-2-deficient mice are defective in the leaky and cation-selective paracellular permeability properties of renal proximal tubules.. Proc Natl Acad Sci U S A 2010 Apr 27;107(17):8011-6.
    pmc: PMC2867900pubmed: 20385797doi: 10.1073/pnas.0912901107google scholar: lookup
  23. Nitta T, Hata M, Gotoh S, Seo Y, Sasaki H, Hashimoto N, Furuse M, Tsukita S. Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice.. J Cell Biol 2003 May 12;161(3):653-60.
    pmc: PMC2172943pubmed: 12743111doi: 10.1083/jcb.200302070google scholar: lookup
  24. Rangel LB, Agarwal R, D'Souza T, Pizer ES, Alò PL, Lancaster WD, Gregoire L, Schwartz DR, Cho KR, Morin PJ. Tight junction proteins claudin-3 and claudin-4 are frequently overexpressed in ovarian cancer but not in ovarian cystadenomas.. Clin Cancer Res 2003 Jul;9(7):2567-75.
    pubmed: 12855632
  25. Rokkam D, Lafemina MJ, Lee JW, Matthay MA, Frank JA. Claudin-4 levels are associated with intact alveolar fluid clearance in human lungs.. Am J Pathol 2011 Sep;179(3):1081-7.
  26. Tsukita S, Furuse M, Itoh M. Multifunctional strands in tight junctions.. Nat Rev Mol Cell Biol 2001 Apr;2(4):285-93.
    pubmed: 11283726doi: 10.1038/35067088google scholar: lookup
  27. 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 May;107(10):1319-27.
    pmc: PMC209303pubmed: 11375422doi: 10.1172/JCI12464google scholar: lookup
  28. Van Itallie CM, Anderson JM. Claudins and epithelial paracellular transport.. Annu Rev Physiol 2006;68:403-29.

Citations

This article has been cited 4 times.
  1. Kozieł MJ, Kowalska K, Piastowska-Ciesielska AW. Claudins: New Players in Human Fertility and Reproductive System Cancers. Cancers (Basel) 2020 Mar 18;12(3).
    doi: 10.3390/cancers12030711pubmed: 32197343google scholar: lookup
  2. Ahmad R, Rah B, Bastola D, Dhawan P, Singh AB. Obesity-induces Organ and Tissue Specific Tight Junction Restructuring and Barrier Deregulation by Claudin Switching. Sci Rep 2017 Jul 11;7(1):5125.
    doi: 10.1038/s41598-017-04989-8pubmed: 28698546google scholar: lookup
  3. Ahmad R, Sorrell MF, Batra SK, Dhawan P, Singh AB. Gut permeability and mucosal inflammation: bad, good or context dependent. Mucosal Immunol 2017 Mar;10(2):307-317.
    doi: 10.1038/mi.2016.128pubmed: 28120842google scholar: lookup
  4. Kshersagar J, Damle MN, Sharma R, Joshi MG. Cell Communication in Endometrium: Understanding and Improving Endometrial Biomarkers. Adv Exp Med Biol 2025;1499:27-50.
    doi: 10.1007/5584_2025_867pubmed: 40652128google scholar: lookup