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Related Concept Videos

Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
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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...
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...
Overview of Cell-Cell Junctions01:14

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The complex three-dimensional arrangement of cells in any multicellular organism is defined and maintained by interactions of cells with each other and the extracellular matrix. Cell-cell junctions are specialized structures where the multi-protein complexes on one cell interact with the multi-protein complexes on another  cell. These cell junctions are classified  into three main types based on their function — occluding, anchoring, and gap junctions.
Occluding or Tight Junctions
Tight...
Contact-dependent Signaling01:19

Contact-dependent Signaling

Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
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Adherens Junctions

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Related Experiment Video

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Perturbing Endothelial Biomechanics via Connexin 43 Structural Disruption
09:20

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Published on: October 4, 2019

AGE-BSA down-regulates endothelial connexin43 gap junctions.

Chi-Young Wang1, Hung-Jen Liu, Heng-Ju Chen

  • 1Department of Internal Medicine, Mackay Memorial Hospital, New Taipei City 251, Taiwan.

BMC Cell Biology
|May 18, 2011
PubMed
Summary

Advanced glycation end products (AGE-BSA) reduce connexin43 (Cx43) expression and gap-junction communication in human aortic endothelial cells. This occurs via reduced transcription involving ERK and p38 MAPK pathways.

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Area of Science:

  • Cardiovascular Biology
  • Endothelial Cell Function
  • Molecular Mechanisms of Disease

Background:

  • Advanced glycation end products (AGEs) are implicated in diabetic vascular complications.
  • The impact of AGEs on endothelial cell connexin43 (Cx43) and gap-junctions requires further elucidation.

Purpose of the Study:

  • To investigate the effect of AGE-bovine serum albumin (AGE-BSA) on Cx43 expression and gap-junction communication in human aortic endothelial cells (HAEC).
  • To explore the underlying molecular pathways, specifically mitogen-activated protein kinases (MAPKs), involved in AGE-BSA-induced changes.

Main Methods:

  • HAEC were treated with varying concentrations of AGE-BSA.
  • Cx43 mRNA and protein levels were quantified.
  • Gap-junction communication was assessed.
  • MAPK signaling pathways (ERK, p38) were analyzed using specific inhibitors and by examining protein phosphorylation.

Main Results:

  • AGE-BSA significantly reduced Cx43 transcript and protein levels in a dose-dependent manner.
  • Gap-junction communication was impaired following AGE-BSA treatment.
  • Inhibition of MEK1 (ERK pathway) and p38 MAPK reversed the down-regulation of Cx43 expression.
  • AGE-BSA exposure enhanced ERK and p38 MAPK phosphorylation.
  • Cx43 expression restoration by inhibitors did not fully restore gap-junction function.

Conclusions:

  • AGE-BSA down-regulates Cx43 expression in HAEC primarily by reducing transcription.
  • The ERK and p38 MAPK pathways are involved in mediating AGE-BSA's effect on Cx43 expression.
  • While AGE-BSA impacts Cx43 expression and gap-junction communication, the precise relationship and functional recovery require further investigation.