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Related Concept Videos

Aquaporins01:25

Aquaporins

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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Induction of Paralysis and Visual System Injury in Mice by T Cells Specific for Neuromyelitis Optica Autoantigen Aquaporin-4
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Aquaporin-4 overexpression in rat ALS model.

Charles Nicaise1, Muhammad Shahnawaz Soyfoo, Michèle Authelet

  • 1Laboratory of Histology, Neuroanatomy and Neuropathology, Université Libre de Bruxelles, 808 route de Lennik, Brussels, Belgium.

Anatomical Record (Hoboken, N.J. : 2007)
|December 18, 2008
PubMed
Summary

Amyotrophic lateral sclerosis (ALS) involves altered glial cells. In ALS rats, aquaporin-4 (AQP4) is overexpressed in spinal cord gray matter, surrounding vessels and motor neurons.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by motoneuron death.
  • Astrocytic and glial environments are significantly modified during ALS progression.
  • Mutations in superoxide dismutase 1 (SOD1) are a known cause of familial ALS.

Purpose of the Study:

  • To investigate the expression and localization of aquaporin-4 (AQP4) in the spinal cord of a rat model of ALS.
  • To determine if AQP4 expression changes are associated with disease progression in ALS.

Main Methods:

  • Utilized a transgenic rat model overexpressing mutated human SOD1.
  • Employed immunohistochemistry and double immunofluorescence to detect AQP4 mRNA and protein.
  • Performed pre-embedding immunohistochemistry at the electron microscopic level.

Main Results:

  • Aquaporin-4 (AQP4) mRNA and protein were specifically overexpressed in the gray matter of ALS rats at the end stage of the disease.
  • Increased AQP4 was detected surrounding both blood vessels and motoneuron perikarya in the spinal cord gray matter of ALS rats.
  • Electron microscopy confirmed AQP4 localization associated with swollen astrocytic processes around vessels and on motoneuron perikarya.

Conclusions:

  • Aquaporin-4 (AQP4) expression is upregulated in the spinal cord during the late stages of ALS in a SOD1-mutant rat model.
  • The observed AQP4 upregulation is localized around blood vessels and motoneurons, suggesting a role in glial-vascular and glial-neuronal interactions in ALS.
  • The precise cellular source of AQP4 surrounding motoneurons in ALS remains to be identified.