Immunohistochemical Analysis of Tight Junction Proteins.
Blood–brain barrier
ImageJ
Immunohistochemistry
Tight junction
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
22
6
2022
pubmed:
23
6
2022
medline:
25
6
2022
Statut:
ppublish
Résumé
Tight junction proteins are integral membrane proteins located apically on epithelial and endothelial cells. They form a selective paracellular barrier restricting the passage of solutes and ions across epithelial and endothelial sheets. In brain endothelial cells, the enrichment of tight junction proteins is one of the unique features of the blood-brain barrier, the physiological boundary that separates the blood from the parenchyma. The predominant tight junction family proteins are the claudins, but several others have been described in recent years including the marvel family, occludin, and lipolysis-stimulated lipoprotein receptor. Together, the tight junctions create a highly electrical-resistant, impermeable paracellular channel that strictly restricts the movement of material from the blood to the parenchyma and vice versa. In this chapter, we will discuss immunohistochemical methods to assess tight junction expression and localization and an ImageJ-based method for quantifying tight junction staining in healthy and diseased states.
Identifiants
pubmed: 35733053
doi: 10.1007/978-1-0716-2289-6_18
doi:
Substances chimiques
Claudins
0
Occludin
0
Tight Junction Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
307-314Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
Références
Sweeney MD et al (2019) Blood-brain barrier: from physiology to disease and Back. Physiol Rev 99(1):21–78
doi: 10.1152/physrev.00050.2017
Abbott NJ et al (2010) Structure and function of the blood-brain barrier. Neurobiol Dis 37(1):13–25
doi: 10.1016/j.nbd.2009.07.030
Cummins PM (2012) Occludin: one protein, many forms. Mol Cell Biol 32(2):242–250
doi: 10.1128/MCB.06029-11
Wolburg H, Lippoldt A (2002) Tight junctions of the blood-brain barrier: development, composition and regulation. Vasc Pharmacol 38(6):323–337
doi: 10.1016/S1537-1891(02)00200-8
Morita K et al (1999) Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci U S A 96(2):511–516
doi: 10.1073/pnas.96.2.511
Itoh M et al (1999) Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 147(6):1351–1363
doi: 10.1083/jcb.147.6.1351
Tornavaca O et al (2015) ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation. J Cell Biol 208(6):821–838
doi: 10.1083/jcb.201404140
Nitta T et al (2003) Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice. J Cell Biol 161(3):653–660
doi: 10.1083/jcb.200302070
Sohet F et al (2015) LSR/angulin-1 is a tricellular tight junction protein involved in blood-brain barrier formation. J Cell Biol 208(6):703–711
doi: 10.1083/jcb.201410131
Lv J et al (2018) Focusing on claudin-5: a promising candidate in the regulation of BBB to treat ischemic stroke. Prog Neurobiol 161:79–96
doi: 10.1016/j.pneurobio.2017.12.001
Knowland D et al (2014) Stepwise recruitment of transcellular and paracellular pathways underlies blood-brain barrier breakdown in stroke. Neuron 82(3):603–617
doi: 10.1016/j.neuron.2014.03.003
Chodobski A, Zink BJ, Szmydynger-Chodobska J (2011) Blood-brain barrier pathophysiology in traumatic brain injury. Transl Stroke Res 2(4):492–516
doi: 10.1007/s12975-011-0125-x
Greene C, Hanley N, Campbell M (2020) Blood-brain barrier associated tight junction disruption is a hallmark feature of major psychiatric disorders. Transl Psychiatry 10(1):373
doi: 10.1038/s41398-020-01054-3
Greene C et al (2018) Dose-dependent expression of claudin-5 is a modifying factor in schizophrenia. Mol Psychiatry 23(11):2156–2166
doi: 10.1038/mp.2017.156
Nishiura K et al (2017) PKA activation and endothelial claudin-5 breakdown in the schizophrenic prefrontal cortex. Oncotarget 8(55):93382–93391
doi: 10.18632/oncotarget.21850
Greene C, Hanley N, Campbell M (2019) Claudin-5: gatekeeper of neurological function. Fluids Barriers CNS 16(1):3
doi: 10.1186/s12987-019-0123-z