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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/12/10 05:50:41」(JST)

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Claudins are a family of proteins that are the most important components of the tight junctions, where they establish the paracellular barrier that controls the flow of molecules in the intercellular space between the cells of an epithelium. They have four transmembrane domains, with the N-terminus and the C-terminus in the cytoplasm.

Structure

Claudins are small (20–27 kilodalton (kDa)) transmembrane proteins which are found in many organisms, ranging from nematodes to human beings, and are very similar in their structure, although this conservation is not observed on the genetic level. Claudins span the cellular membrane 4 times, with the N-terminal end and the C-terminal end both located in the cytoplasm, and two extracellular loops which show the highest degree of conservation. The first extracellular loop consists on average of 53 amino acids and the second one, being slightly smaller, of 24 amino acids. The N-terminal end is usually very short (4–10 amino acids), the C-terminal end varies in length from 21 to 63 and is necessary for the localisation of these proteins in the tight junctions.^[1] It is suspected that the cysteines of individual or separate claudins form disulfide bonds. All human claudins (with the exception of Claudin 12) have domains that let them bind to PDZ domains of scaffold proteins.

History

Claudins were first named in 1998 by Japanese researchers Mikio Furuse and Shoichiro Tsukita at Kyoto University.^[2] The name claudin comes from Latin word claudere ("to close"), suggesting the barrier role of these proteins.

Genes

In humans, 24 members of the family have been described.

CLDN1, CLDN2, CLDN3, CLDN4, CLDN5, CLDN6, CLDN7, CLDN8, CLDN9, CLDN10, CLDN11, CLDN12, CLDN13, CLDN14, CLDN15, CLDN16, CLDN17, CLDN18, CLDN19, CLDN20, CLDN21, CLDN22, CLDN23

Additional images

References

^ Rüffer C, Gerke V (May 2004). "The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions". Eur. J. Cell Biol. 83 (4): 135–44. doi:10.1078/0171-9335-00366. PMID 15260435.
^ Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S (June 1998). "Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin". J. Cell Biol. 141 (7): 1539–50. doi:10.1083/jcb.141.7.1539. PMC 2132999. PMID 9647647.

UpToDate Contents

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English Journal

Induction of oxidative and nitrosative damage leads to cerebrovascular inflammation in an animal model of mild traumatic brain injury induced by primary blast.

Abdul-Muneer PM, Schuetz H, Wang F, Skotak M, Jones J, Gorantla S, Zimmerman MC, Chandra N, Haorah J.SourceDepartment of Pharmacology and Experimental Neuroscience, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Free radical biology & medicine.Free Radic Biol Med.2013 Jul;60:282-91. doi: 10.1016/j.freeradbiomed.2013.02.029. Epub 2013 Mar 4.
We investigate the hypothesis that oxidative damage of the cerebral vascular barrier interface (the blood-brain barrier, BBB) causes the development of mild traumatic brain injury (TBI) during a primary blast-wave spectrum. The underlying biochemical and cellular mechanisms of this vascular layer-st
PMID 23466554

Analysis of CLDN14 gene in deaf Moroccan patients with non-syndromic hearing loss.

Charif M, Bakhchane A, Abidi O, Boulouiz R, Eloualid A, Roky R, Rouba H, Kandil M, Lenaers G, Barakat A.SourceLaboratoire de Génétique Moléculaire et Humaine, Département de Recherche Scientifique, Institut Pasteur du Maroc, 20100 Casablanca, Morocco.
Gene.Gene.2013 Jul 1;523(1):103-5. doi: 10.1016/j.gene.2013.03.123. Epub 2013 Apr 13.
Mutations in the CLDN14 gene, encoding the tight junction claudin 14 protein has been reported to date in an autosomal recessive form of isolated hearing loss DFNB29. In order to identify the contribution of CLDN14 to inherited deafness in Moroccan population, we performed a genetic analysis of this
PMID 23590985

Japanese Journal

タイトジャンクションと上皮バリア機能 (特集生体バリアと生体防御・免疫系)

古瀬幹夫
臨床免疫・アレルギー科 = Clinical immunology & allergology 64(1), 1-6, 2015-07
NAID 40020540414

糖尿病性腎症とサーチュイン・ニコチン酸代謝異常 (内分泌) -- (臨床分野での進歩)

脇野修,長谷川一宏,村丘寛和 [他]
Annual review. 糖尿病・代謝・内分泌, 198-205, 2015
NAID 40020368679

Nifedipine Prevents Sodium Caprate-Induced Barrier Dysfunction in Human Epidermal Keratinocyte Cultures

Uchino Yoshihiro,Matsumoto Junichi,Watanabe Takuya [他],Hamabashiri Masato,Tsuchiya Takashi,Kimura Ikuya,Yamauchi Atsushi,Kataoka Yasufumi
Biological and Pharmaceutical Bulletin 38(6), 926-929, 2015
… Immunocytochemical observations revealed that nifedipine improved the C10-induced irregular arrangement of claudin-1, a key protein in TJs. … Taken together, these findings suggest that nifedipine prevents epidermal barrier dysfunction, at least in part, by reconstituting the irregular claudin-1 localization at TJs in C10-treated NHEKs. …
NAID 130005072663

Related Pictures

★リンクテーブル★

リンク元	「細胞接着」「クローディン」

「細胞接着」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

PMP22_Claudin
Identifiers
Symbol	PMP22_Claudin
Pfam	PF00822
Pfam clan	CL0375
InterPro	IPR004031
PROSITE	PDOC01045
TCDB	1.H.1
OPM superfamily	492
OPM protein	4p79
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary