Targeting Alpha5 Beta1 Integrin to Prevent Metastatic Breast Cancer Cell Invasion: PhScN Target Site Definition and Plasma Stability

Abstract

It has been suggested that PHSCN inhibits metastatic invasion by forming a covalent, disulfide bond with a cysteine residue on the beta1 ( 1) subunit of alpha5 beta1 ( 5 1) integrin1. However, these studies were performed with purified 5 1 integrin, which also produces evidence of covalent bond formation with the 5 subunit (tandem mass spectroscopy data not shown). Hence, the specificity of the reported interaction between PHSCN and the 1 subunit1 is suspect. Moreover, the cysteine rich 1 subunit can heterodimerize with 12 distinct alpha integrin subunits2, forming integrins that function in many pathways. In contrast, the 5 subunit interacts uniquely with the 1 subunit2 to induce invasion and support adhesion3-5; hence it is a much more desirable target.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 2013
Accession Number
ADA592840

Entities

People

  • Donna L. Livant

Organizations

  • University of Michigan

Tags

DTIC Thesaurus Topics

  • Amines
  • Amino Acids
  • Blood
  • Blood Proteins
  • Breast Cancer
  • Cells
  • Cellular Structures
  • Covalent Bonds
  • Cysteine
  • Integrins
  • Mass Spectrometry
  • Mass Spectroscopy
  • Molecular Weight
  • Neoplasms
  • Spectrometry
  • Spectroscopy
  • Targets

Fields of Study

  • Biology

Readers

  • Molecular and Cellular Biochemistry
  • Oncology (Cancer Research).