Tumor Cell De-Adhesion By Aberrant, Single Subunit Integrins

Abstract

Three alternatively spliced forms of the integrin Beta 5 subunit have been identified. Each mRNA splice removes one or more exons from the Beta 5 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 Beta 5 contains transmembrane and cytoplasmic domains that are identical to wild type Beta 5. 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 Beta 5 do not dimerize with the Alpha v 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, 1997
Accession Number
ADA332565

Entities

People

  • Ian Jongewaard

Organizations

  • Sanford Burnham Prebys Medical Discovery Institute

Tags

DTIC Thesaurus Topics

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

Fields of Study

  • Biology

Readers

  • Breast cancer cell signaling and growth regulation.
  • Molecular Genetics