Claudin: Difference between revisions - Wikipedia
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Line 1: {{Short description|Group of proteins forming tight junctions between cells}} {{for-multi|the Arthurian character|Prince Claudin|the French composer|Claudin de Sermisy}} {{cs1 config|name-list-style=vanc|display-authors=6}} [[File:Cellular_tight_junction-en.svg|thumb|300px]] '''Claudins''' are a family of [[protein]]s which, along with [[occludin]], are the most important components of the [[tight junction]]s ([[Tight junction|zonulae occludentes]]).<ref name=":0">{{cite book | vauthors = Hou J, Konrad M | chapter = Chapter 7 - Claudins and Renal Magnesium Handling|date=2010-01-01 |title = Current Topics in Membranes|volume=65|pages=151–176| veditors = Yu AS |publisher=Academic Press|language=en|doi=10.1016/s1063-5823(10)65007-7 | isbn = 9780123810397}}</ref><ref>{{cite book | vauthors = Furuse M | chapter = Chapter 1 - Introduction: Claudins, Tight Junctions, and the Paracellular Barrier|date=2010-01-01 | title = Current Topics in Membranes|volume=65|pages=1–19| veditors = Yu AS |publisher=Academic Press|language=en|doi=10.1016/s1063-5823(10)65001-6 | isbn = 9780123810397}}</ref> Tight junctions establish the [[paracellular]] barrier that controls the flow of molecules in the intercellular space between the cells of an [[epithelium]].<ref name=":0" /><ref>{{cite book | vauthors = Szaszi K, Amoozadeh Y | chapter = Chapter Six - New Insights into Functions, Regulation, and Pathological Roles of Tight Junctions in Kidney Tubular Epithelium|date=2014-01-01 | title = International Review of Cell and Molecular Biology|volume=308|pages=205–271| veditors = Jeon KW |publisher=Academic Press|language=en|doi=10.1016/b978-0-12-800097-7.00006-3 | pmid = 24411173| isbn = 9780128000977}}</ref><ref>{{cite journal | vauthors = Otani T, Nguyen TP, Tokuda S, Sugihara K, Sugawara T, Furuse K, Miura T, Ebnet K, Furuse M | title = Claudins and JAM-A coordinately regulate tight junction formation and epithelial polarity | journal = The Journal of Cell Biology | volume = 218 | issue = 10 | pages = 3372–3396 | date = October 2019 | pmid = 31467165 | pmc = 6781433 | doi = 10.1083/jcb.201812157 }}</ref> They have four transmembrane domains, with the [[N-terminus]] and the C-terminus in the cytoplasm. == Structure == Claudins are small (20–24/27 [[Atomic mass unit|kilodalton]] (kDa))<ref name=":1">{{cite book| vauthors = Greene C, Campbell M, Janigro D | chapter = Chapter 1 - Fundamentals of Brain–Barrier Anatomy and Global Functions|date=2019-01-01| title = Nervous System Drug Delivery|pages=3–20| veditors = Lonser RR, Sarntinoranont M, Bankiewicz K |publisher=Academic Press|language=en|doi=10.1016/b978-0-12-813997-4.00001-3|isbn=978-0-12-813997-4 | s2cid = 198273920}}</ref> [[transmembrane protein]]s which are found in many [[organisms]], ranging from [[nematode]]s to [[human]] beings. They all have a very similar structure. 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. Claudins have both cis and trans interactions between cell membranes.<ref>{{cite book| vauthors = Haseloff RF, Piontek J, Blasig IE | chapter = Chapter 5 - The Investigation of cis- and trans-Interactions Between Claudins|date=2010-01-01 | title = Current Topics in Membranes|volume=65|pages=97–112| Generally the tight junction is known for its impermeability. However, depending on the type of claudin and their interactions there is selective permeability. This includes charge selectivity and size selectivity.<ref name=":2" /> Line 34 ⟶ 35: === Studies === A recent review discusses evidence regarding the structure and function of claudin family proteins using a systems approach to understand evidence generated by [[proteomics]] techniques.<ref> {{cite journal | vauthors = Liu F, Koval M, Ranganathan S, Fanayan S, Hancock WS, Lundberg EK, Beavis RC, Lane L, Duek P, McQuade L, Kelleher NL, Baker MS </ref> A chimeric claudin was synthesized to help enhance the understanding of both the structure and function of the tight junction.<ref name=":7">{{cite journal | vauthors = Taylor A, Warner M, Mendoza C, Memmott C, LeCheminant T, Bailey S, Christensen C, Keller J, Suli A, Mizrachi D Computational modeling is also another technique being used to help enhance research into the structure and functions of claudins.<ref name=":6" /> Line 63 ⟶ 64: There are 23 genes found in the human genome for claudin proteins<ref name=":7" /> and there are 27 transmembrane domains across mammals.<ref name=":3" /><ref name=":5" /> The conservation is not observed on a [[Conserved sequence|genetic level]]. Despite the genetic level not being conserved across claudins their structural conservation are very similar. * ''[[CLDN1]]'', ''[[CLDN2]]'', ''[[CLDN3]]'', ''[[CLDN4]]'', ''[[CLDN5]]'', ''[[CLDN6]]'', ''[[CLDN7]]'', ''[[CLDN8]]'', ''[[CLDN9]]'', ''[[CLDN10]]'',<ref>{{cite book | vauthors = Hou J | chapter = Chapter 7 - Paracellular Channel in Organ System|date=2019-01-01 | title = The Paracellular Channel|pages=93–141 | == See also == | |||