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The structural proteins in an adherens junction: These are the principal interactions of structural proteins at a cadherin-based plasma membrane adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins. Gap junctions are also called communicating junctions, macula communicans, or nexuses. These are connections that allow for the direct passage of molecules between two cells. Gap junctions consist of a number of transmembrane channels called pores that are found in a closely packed arrangement.
The number of gap junctions shared between two cells can vary as well. These half channels join together, bridge the extracellular space in the process, and form the entire channel that spans both cell membranes. Each of these half channels is called a connexon. Each connexon is made up of six symmetrical integral membrane protein units called connexins. This means each channel is made up of 12 circularly arranged protein units.
Intercalated disk in heart muscle contains gap junctions: Intercalated disks consist of three different types of cell—cell junctions: actin filaments anchoring adherens junctions, intermediate filaments anchoring desmosomes, and gap junctions. Gap junctions are responsible for electrochemical and metabolic coupling.
The molecules that may cross this channel include the likes of ions, regulatory proteins, and metabolites products of metabolism. Examples of this includes calcium ions and cAMP cyclic adenosine monophosphate.
Depending on the type of gap junction in question, molecules can pass evenly in both directions, or asymmetrically, so in some gap junctions the molecules will move in one direction faster than in the other direction. They fluctuate between being open and closed. The ability of the channel to open or close is made possible in part to calcium ions, which induce a reversible conformational change in the connexin molecules, which leads to the closure of a channel at its extracellular surface.
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Arterioscler Thromb Vasc Biol. Biochem J. Shen L, Turner JR: Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. J Neurosci Res. Biophys J. Picotti P, Aebersold R: Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat Methods. Download references. You can also search for this author in PubMed Google Scholar. Correspondence to Pierre-Olivier Couraud.
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Luissint, AC. Tight junctions at the blood brain barrier: physiological architecture and disease-associated dysregulation. Fluids Barriers CNS 9, 23 Download citation.
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Search all BMC articles Search. Download PDF. Abstract The Blood—brain barrier BBB , present at the level of the endothelium of cerebral blood vessels, selectively restricts the blood-to-brain paracellular diffusion of compounds; it is mandatory for cerebral homeostasis and proper neuronal function. Review Background The BBB maintains the homeostasis of the central nervous system CNS by i strictly limiting the passive diffusion of polar substances from the blood to the brain, ii mediating the transport of nutrients to the brain parenchyma as well as the efflux from the brain of toxic metabolites and xenobiotics, iii regulating the migration of circulating immune cells [ 1 — 3 ].
Components of TJs in brain endothelial cells As in polarized epithelial cells where TJs have been mostly studied, the TJ backbone in brain endothelial cells consists of transmembrane proteins occludin, claudins and JAMs which recruit a number of membrane-associated cytoplasmic proteins. Transmembrane proteins as the BBB TJ backbone Occludin 60kDa , a tetraspan integral membrane protein, was the first TJ-specific protein identified [ 12 , 13 ] in epithelial cells and shown to be functionally important for barrier function [ 14 ].
Membrane-associated cytoplasmic proteins in BBB TJs A number of cytoplasmic proteins have been described to associate with TJ transmembrane proteins and to contribute somehow to TJ integrity in epithelial and brain endothelial cells.