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Related Concept Videos

Gap Junctions01:37

Gap Junctions

Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Multi-pass Transmembrane Proteins and β-barrels01:09

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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Position-effect Variegation02:32

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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
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Functional differences between human Cx37 polymorphic hemichannels.

Jean-Paul Derouette1, Thomas Desplantez, Cindy W Wong

  • 1Department of Internal Medicine, Division of Cardiology, Faculty of Medicine, University of Geneva, Geneva, Switzerland.

Journal of Molecular and Cellular Cardiology
|January 27, 2009
PubMed
Summary

The Cx37 P319S polymorphism affects connexin 37 hemichannel and gap junction channel function. This impacts ATP release and cell adhesion, potentially influencing atherosclerosis development.

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Area of Science:

  • Molecular Biology
  • Cardiovascular Research
  • Biophysics

Background:

  • A polymorphism in the human Cx37 gene (C1019T) leads to a P319S amino acid change, proposed as an atherosclerosis prognostic marker.
  • Cx37 hemichannels regulate monocyte adhesion, a key factor in early atherosclerotic plaque development.

Purpose of the Study:

  • To investigate the biophysical properties of Cx37 hemichannels (HCs) and gap junction channels (GJCs) associated with the P319S polymorphism.
  • To determine how these differences affect ATP release and cell adhesion.

Main Methods:

  • Voltage-clamp electrophysiology was used to measure electrical properties of Cx37 HCs and GJCs in transfected HeLa cells.
  • Cell clones expressing either Cx37-P319 or Cx37-S319 were analyzed for HC current, GJC unitary conductance, ATP release, and cell adhesion.

Main Results:

  • Cx37-P319 HCs exhibited a 3-fold larger peak conductance than Cx37-S319 HCs.
  • Cx37-P319 GJCs showed 1.5-fold greater unitary conductance compared to Cx37-S319 GJCs.
  • Cx37-P319 cells released more ATP and displayed reduced adhesion, which was reversible by apyrase.

Conclusions:

  • The P319S polymorphism in Cx37 alters the biophysical properties of both hemichannels and gap junction channels.
  • These alterations lead to differential ATP release and cell adhesion, providing a molecular mechanism for the role of Cx37 in atherosclerosis.