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An alternately spliced mRNA encoding functional domains of murine MAdCAM-1

S G Schiffer1, E Day, S M Latanision

  • 1Biogen, Inc., Cambridge, MA 02142, USA.

Insights

Researchers identified a shorter form of murine mucosal addressin cell adhesion molecule-1 (MAdCAM-1) mRNA, likely due to alternative splicing. This shorter MAdCAM-1 variant retains the ability to bind the alpha 4 beta 7 integrin.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Adhesion

Background:

  • Mucosal Addressin Cell Adhesion Molecule-1 (MAdCAM-1) is crucial for lymphocyte homing to mucosal tissues.
  • MAdCAM-1 mediates leukocyte-endothelial cell interactions through its integrin counter-receptor, alpha 4 beta 7.

Purpose of the Study:

  • To characterize a newly identified short form of murine MAdCAM-1.
  • To investigate the functional significance of the short MAdCAM-1 variant in ligand binding.

Main Methods:

  • cDNA cloning and sequencing of short and long MAdCAM-1 mRNA variants.
  • Expression of MAdCAM-1 Ig fusion proteins.
  • Binding assays using JY cells expressing alpha 4 beta 7 integrin.

Main Results:

  • A short (0.8 kb) MAdCAM-1 cDNA was identified, differing from the long form by deletion of 432 nucleotides.
  • This short form likely arises from alternative mRNA splicing.
  • Both short and long MAdCAM-1 forms are expressed in murine mesenteric lymph nodes.
  • Immunoglobulin fusion proteins of both MAdCAM-1 variants bind to alpha 4 beta 7 integrin on JY cells.

Conclusions:

  • The two N-terminal Ig-like domains of MAdCAM-1 are sufficient for binding alpha 4 beta 7 integrin.
  • Alternative splicing generates functional MAdCAM-1 variants involved in immune cell trafficking.

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