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Related Concept Videos

Tight Junctions01:29

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Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
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Drugs need to permeate cell membranes to reach their target sites after administration. Orally administered drugs must transcend intestinal epithelial membrane barriers to infiltrate the systemic circulation. Drugs with a molecular weight of less than 500 Daltons diffuse through gaps between neighboring cells, called paracellular pathways.
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Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
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ZO-1 and -2 Are Required for TRPV1-Modulated Paracellular Permeability.

J Li1, X Cong2, Y Zhang2

  • 1Department of Oral and Maxillofacial Surgery, Peking University School and Hospital of Stomatology, Beijing, China.

Journal of Dental Research
|October 15, 2015
PubMed
Summary
This summary is machine-generated.

Capsaicin activates TRPV1 channels, increasing saliva secretion by altering tight junctions. Zonula occludens proteins ZO-1 and ZO-2 are key to this process, regulated by the RhoA-ROCK pathway.

Keywords:
capsaicinsalivary cellssalivationtight junctiontransient receptor potential vanilloid subtype 1zonula occludens

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Area of Science:

  • Physiology
  • Cell Biology
  • Gastroenterology

Background:

  • The paracellular pathway, regulated by tight junctions, is vital for saliva secretion.
  • Zonula occludens (ZO) proteins are critical components of tight junctions, but their role in salivary epithelium is not well understood.

Purpose of the Study:

  • To investigate the role of transient receptor potential vanilloid subtype 1 (TRPV1) in saliva secretion.
  • To elucidate the involvement of ZO proteins in TRPV1-mediated regulation of salivary epithelial barrier function and paracellular transport.

Main Methods:

  • In vivo and ex vivo studies using rat saliva secretion models.
  • In vitro experiments with submandibular gland (SMG)-C6 cells to assess paracellular flux and transepithelial electric resistance (TER).
  • Immunofluorescence staining for ZO proteins, small interfering RNA (siRNA) knockdown, and RhoA/ROCK pathway inhibition.

Main Results:

  • TRPV1 activation by capsaicin increased saliva secretion, enlarged tight junction width, and enhanced paracellular flux.
  • TRPV1 activation decreased TER and reduced ZO-1 and ZO-2 staining at cell-cell contacts.
  • Knockdown of ZO-1/ZO-2 increased basal paracellular flux, while their depletion abolished capsaicin-induced permeability increases, and re-expression restored it.
  • TRPV1 activation increased RhoA activity; RhoA/ROCK inhibition prevented capsaicin-induced changes in TER and ZO protein localization.

Conclusions:

  • ZO-1 and ZO-2 are crucial for maintaining salivary epithelial barrier function and regulating TRPV1-mediated paracellular transport.
  • The RhoA-ROCK signaling pathway mediates TRPV1-induced alterations in paracellular permeability and ZO protein redistribution.