Tumor Cell De-Adhesion by Aberrant, Single Subunit Integrins.

Abstract

Three alternatively spliced forms of the integrin Beta5 subunit have been identified. Each mRNA splice removes one or more exons from the Beta5 message, but does not alter the reading frame. Consequently, each splice variant encodes a protein that Is lacking domains in the amino terminal portion of the molecule, near the ligand binding site. Each variant of contains transmembrane and cytoplasmic domains that are identical to wild-type Beta5. Analysis of the protein products of each splice variant by immunoprecipitation showed that each variant is translated to protein and expressed on the cell surface. However, the variants of Beta5 do not dimerize with the alphav subunit. This is the first identification of alternative splices in the ectodomain of an integrin that result in the display of a "single subunit. integrin" on the cell surface.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1998
Accession Number
ADA378864

Entities

People

  • Ian N. Jongewaard

Organizations

  • Sanford Burnham Prebys Medical Discovery Institute

Tags

DTIC Thesaurus Topics

  • Adhesion
  • Amino Acids
  • Antibodies
  • Biomedical Research
  • Breast Cancer
  • Cell Line
  • Cell Physiological Processes
  • Cells
  • Chemical Reactions
  • Genetic Code
  • Identification
  • Immune Serums
  • Materials
  • Molecules
  • Neoplasms
  • Polymerase Chain Reaction
  • Proteins

Fields of Study

  • Biology

Readers

  • Molecular Biology and Genetics
  • Molecular Genetics